RECOMBINANT NUCLEIC ACIDS THAT ENCODE ONE OR MORE COSMETIC PROTEINS FOR AESTHETIC USES

Abstract

This description provides recombinant nucleic acids comprising one or more polynucleotides encoding one or more cosmetic proteins (e.g., one or more human collagen proteins); viruses comprising the recombinant nucleic acids; compositions (e.g., cosmetic formulations) comprising the viruses and / or recombinant nucleic acids; methods for using them; and products or kits for manufacturing them.

Description

RECOMBINANT NUCLEIC ACIDS ENCODING ONE OR MORE COSMETIC PROTEINS FOR AESTHETIC USES CROSS REFERENCE TO RELATED REQUESTS This application claims the benefit of priority to US Provisional Application No. 62 / 663,476, filed April 27, 2018, which is incorporated herein by this reference in its entirety. PRESENTATION OF THE LIST OF SEQUENCES IN ASCII TEXT FILE The contents of the submitted ASCII text file are incorporated herein in their entirety by this reference: a computer readable form (CRF) of the sequence listing (file name: 761342000640SEQLIST.txt, date of record : April 26, 2019, size: 437 KB. FIELD OF THE INVENTION The present description relates, in part, to recombinant nucleic acids comprising one or more polynucleotides encoding one or more cosmetic proteins (for example, one or more human collagen proteins), to viruses comprising the recombinant nucleic acids, to compositions (for example, cosmetic formulations) comprising the recombinant nucleic acids and / or viruses, methods for using them, as well as manufacturing products or kits thereof. BACKGROUND Like all organs of the human body, the skin undergoes sequential and generally cumulative alterations over time. Skin aging occurs due to a variety of factors including inherent changes in the skin, the effect of gravity and the action of facial muscles on the skin, loss or change in soft tissue, and loss of elasticity. of the tissues. Interestingly, environmental factors, more specifically chronic exposure to ultraviolet radiation (eg, from the sun), can accelerate the "aging" phenotype of the skin. Clinically, the aged skin phenotype can be described as wrinkled, sagging, and / or generally less elastic and resilient than its younger counterpart, although there are variations within the phenotype between natural chronological aging and photoaging. The extracellular dermal matrix (ECM) comprises the largest amount of skin and gives it strength and elasticity. Collagen, one of the main components of the connective tissue that supports the skin, is reduced over time. In aged skin, collagen fibrils show high levels of degradation and fragmentation and are refilled by dermal fibroblasts at slower rates. These clumps of degraded and fragmented collagen become increasingly loose and lose strength (which alters the structural organization of the dermal ECM). This inextricably produces an "aged" manifestation of the skin. Various skin care products have been developed to improve the appearance of human skin. Wrinkles and skin folds are often treated with dermal and subdermal injections of cosmetic facial fillers. However, this superficial approach does not address the structural changes that cause skin aging, particularly collagen damage or loss. Therefore, alternative strategies are clearly needed to supplement, reinforce, or replace dermal ECM components (eg, human collagen) in c / CLnn / Lznz / q / Yi individuals who wish to combat or reverse the physiological effects of aging. of the skin. All references cited herein, including patent applications, patent publications, non-patent literature, and NCBI / UniProtKB / Swiss-Prot accession numbers are incorporated herein in their entirety by this reference, as same way as if each individual reference were specifically and independently indicated as incorporated by said reference. BRIEF SUMMARY In order to meet these and other needs, recombinant nucleic acids (eg, recombinant herpes virus genomes) encoding one or more cosmetic proteins for use in viruses (eg, herpes virus), compositions are provided herein. , formulations, medicaments and / or methods for aesthetic / cosmetic applications (for example, wrinkle treatment). The present inventors have demonstrated that the attenuated recombinant viruses described herein have the ability to 1) efficiently transduce human dermal / epidermal cells and 2) successfully express the exogenous encoded human collagen (mRNA and protein). ), with a protein that can then be localized to the appropriate region in skin-equivalent organotypic cultures (see, for example, Example 2). Additionally, the present inventors have demonstrated that the viruses described herein can be successfully administered topically or intradermally without significant cytotoxicity to host cells, allowing human collagen expression of said viruses for localization. in the appropriate region of the dermal ECM after administration in vivo, without observable damage to the skin (see, for example, Examples 3 and 7). In addition, the present inventors have shown that multiple different HSV backbone structures can be used to construct human collagen expressing viruses (see, for example, Example 2), that multiple strategies can be used to successfully express more of a human collagen protein from a single recombinant genome (see, for example, Example 5), and that candidate viruses can express human collagen proteins successfully in multiple relevant models of chronological or induced by UV in vitro and in vivo (see, for example, Examples 6 and 7). Still further, the present inventors have demonstrated that the viruses described herein can be successfully engineered to express other cosmetic proteins (eg, human laminins), both in vitro and in vivo, and that these proteins are localized to the appropriate region of the dermal ECM (see, for example, Example 8). Without wishing to be bound by theory, the data described herein provide strong evidence that the recombinant nucleic acids and / or viruses of the present disclosure may constitute a novel means for the delivery of cosmetic proteins (eg, proteins such as human collagen 1 and human collagen 3) and, in particular, to complement or replace natural human dermal ECM proteins in aesthetic applications (for example, to reduce the appearance of age-related wrinkles or the light). Accordingly, some aspects of the present disclosure refer to a recombinant herpes virus genome comprising a first polynucleotide encoding a first polypeptide comprising a first cosmetic protein. In some embodiments, the recombinant herpes virus genome comprises two or more copies of the first polynucleotide. In some embodiments, the recombinant herpes virus genome is replication competent c / c i nn / ι znz / zi / Yl·. In some embodiments, the recombinant herpes virus genome is replication defective. In some embodiments that may be combined with any of the above embodiments, the herpes virus recombinant genome is selected from a herpes simplex virus recombinant genome, a varicella zoster virus recombinant genome, a human cytomegalovirus recombinant genome, a herpes virus 6A recombinant genome, a herpes virus 6B recombinant genome, a herpes virus 7 recombinant genome, a Kaposi sarcoma-associated herpes virus recombinant genome, and any derivatives thereof. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes virus genome is a recombinant herpes simplex virus genome. In some embodiments, the recombinant herpes simplex virus genome is a recombinant herpes simplex virus type 1 (HSV-1) genome, a recombinant herpes simplex virus type 2 (HSV-2) genome, or any derivative thereof. In some embodiments, the recombinant herpes simplex virus genome is a recombinant herpes simplex virus type 1 (HSV-1) genome. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation. In some modalities that can be combined with any of the above modalities, the inactivating mutation is in a herpes simplex virus gene. In some embodiments, the inactivating mutation is a deletion of the herpes simplex virus gene coding sequence. In some embodiments, the herpes simplex virus gene is selected from infected cell protein (ICP) 0, ICP4, ICP22, ICP27, ICP47, thymidine kinase (tk), extensive unique region (UL) 41 and UL55. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in one or both copies of the ICP4 gene. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP22 gene. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the UL41 gene. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in one or both copies of the ICPO gene. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP27 gene. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the UL55 gene. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the junction region. In some embodiments, the recombinant herpes simplex virus genome comprises a junction region deletion. In some embodiments that may be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises the first polynucleotide within one or both of the ICP4 viral gene loci. In some modalities that can be combined with any of the above modalities, the first cosmetic c / CLnn / Lznz / q / Yi protein is selected from a first collagen protein, a first fibronectin protein, a first elastin protein, a first lumican protein, a first vitronectin protein, a first vitronectin receptor protein, a first laminin protein, a first neuromodulatory protein, and a first fibrillin protein. In some modalities that can be combined with any of the above modalities, the first cosmetic protein comprises a sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93 %, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with an amino acid sequence selected from SEQ. ID. NO.: 15-21 and 53-64. In some embodiments, the first cosmetic protein is a structural extracellular matrix protein (eg, a collagen protein, an elastin protein, a fibronectin protein, a laminin protein, a fibrillin protein, etc.). In some embodiments, the first cosmetic protein is a collagen protein, elastin protein, fibronectin protein, or laminin protein (eg, human collagen protein, human elastin protein, human fibronectin protein, or a human laminin protein). In some modalities that can be combined with any of the above modalities, the first collagen protein is a human collagen protein. In some embodiments that can be combined with any of the above modalities, the first collagen protein is selected from a collagen alpha-1(I) chain polypeptide (COL1-1), an alpha-2(l) chain polypeptide collagen (COL1-2), a collagen alpha1(11) chain polypeptide (COL2), a collagen alpha-1 (III) chain polypeptide (COL3), a collagen alpha-1 (IV) chain polypeptide (COL4-1), a collagen alpha-2(IV) chain polypeptide (COL4-2), a collagen alpha-3(IV) chain polypeptide (COL4-3), an alpha-4( Collagen IV) (COL4-4), an alpha-5(IV) chain polypeptide of collagen (COL4-5), an alpha-6(IV) chain polypeptide of collagen (COL4-6), an alpha-chain polypeptide collagen alpha-1(V) (COL5-1), collagen alpha-2(V) chain polypeptide (COL5-2), collagen alpha-3(V) chain polypeptide (COL5-3), a collagen alpha-1 (VI) chain polypeptide (COL6-1), a collagen alpha-2 (VI) chain polypeptide (CO L6-2), a collagen alpha-3(VI) chain polypeptide (COL6-3), a collagen alpha-4(VI) chain polypeptide (COL6-4), an alpha-5(VI) chain polypeptide ) (COL6-5), a collagen alpha-6(VI) chain polypeptide (COL6-6), an alpha-1 (VIII) chain polypeptide (COL8), a collagen alpha-1 (IX) chain polypeptide collagen (COL9-1), a collagen alpha-2(IX) chain polypeptide (COL9-2), a collagen alpha-3(IX) chain polypeptide (COL9-3), an alpha-1 chain polypeptide Collagen (X) (COL10), an alpha-1 chain polypeptide (XI) Collagen (COL11-1), an alpha-2 chain polypeptide (XI) Collagen (COL11-2), an alpha chain polypeptide Collagen -1 (XII) (COL12), a collagen alpha-1 (XIII) chain polypeptide (COL13), a collagen alpha-1 (XIV) chain polypeptide (COL14), an alpha-1 chain polypeptide Collagen (XV) (COL15), a collagen alpha-1 (XVI) chain polypeptide (COL16), a collagen alpha-1 (XVII) chain polypeptide (COL17), a collagen ca Collagen alpha-1 (XVIII) dena (COL18), a collagen alpha-1 (XIX) chain polypeptide (COL19), a collagen alpha-1 (XX) chain polypeptide (COL20), an alpha chain polypeptide -1 (XXI) collagen (COL21), an alpha-1 (XXII) chain polypeptide of collagen (COL22), an alpha-1 (XXIII) chain polypeptide of collagen (COL23), an alpha-1 chain polypeptide (XXIV) collagen (COL24), an alpha-1 chain polypeptide (XXV) of collagen (COL25), an alpha-1 chain polypeptide (XXVI) of collagen (COL26), an alpha-1 chain polypeptide (XXVII ) of collagen (COL27) and a collagen alphac / CLnn / Lznz / q / YL (XXVIII) chain polypeptide (COL28).In some modalities that can be combined with any of the above modalities, the first collagen protein is selected from C0L1-1, C0L1-2, C0L3, C0L4-1, COL4-2, C0L6-1 and C0L17. In some modalities that can be combined with any of the above modalities, the first collagen protein comprises a sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with an amino acid sequence selected from SEQ. ID. NO.: 15-21. In some modalities that can be combined with any of the above modalities, the first collagen protein is COL3. In some modalities that can be combined with any of the above modalities, the first collagen protein is human COL3. In some modalities that can be combined with any of the above modalities, the first collagen protein comprises a sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ. ID. NO.: 17. In some embodiments that can be combined with any of the above embodiments, the first cosmetic protein is not a collagen (COL7) alpha-1 (Vil) chain polypeptide. In some embodiments, the first polypeptide consists essentially of the first cosmetic protein. In some embodiments, the first polypeptide consists of the first cosmetic protein. In some embodiments, the first polypeptide comprises: (a) the first cosmetic protein, (b) another cosmetic protein, and (c) a linker polypeptide that links (a) to (b). In some embodiments, the other cosmetic protein is selected from a collagen protein, a fibronectin protein, an elastin protein, a lumican protein, a vitronectin protein, a vitronectin receptor protein, a laminin protein, a neuromodulator and a fibrillin protein. In some embodiments, the other cosmetic protein is a structural extracellular matrix protein (eg, collagen protein, elastin primer, fibronectin protein, laminin protein, fibrillin protein, etc.). In some embodiments, the other cosmetic protein is a collagen protein, elastin protein, fibronectin protein, or laminin protein (eg, human collagen protein, human elastin protein, human fibronectin protein, or a human laminin protein). In some embodiments, the other collagen protein (eg, other human collagen protein) is selected from COL1-1, COL1-2, COL2, COL3, COL4-1, COL4-2, COL4-3, COL4-4, COL4-5, COL4-6, COL5-1, COL5-2, COL5-3, COL6-1, COL6-2, COL6-3, COL6-4, COL6-5, COL6-6, COL7, COL8, COL9- 1, COL9-2, COL9-3, COL10, COL11-1, COL11-2, COL12, COL13, COL14, COL15, COL16, COL17, COL18, COL19, COL20, COL21, COL22, COL23, COL24, COL25, COL26, COL27 and COL28. In some embodiments, the other collagen protein (eg, other human collagen protein) is selected from COL1-1, COL1-2, COL3, COL4-1, COL4-2, COL6-1, COL7, and COL17. In some embodiments, the first cosmetic protein and the other cosmetic protein are different. In some embodiments, the first cosmetic protein is COL1-1 (eg, human COL1-1) and the other cosmetic protein is COL1-2 (eg, human COL1-2). In some embodiments, the linker polypeptide is a cleavable linker polypeptide. In some embodiments, the linker polypeptide comprises a sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95% , at least 96%, at c / CLnn / Lznz / q / Yi minus 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence selected from SEQ. ID. NO.: 28-31. In some embodiments that can be combined with any of the above embodiments, the first polynucleotide encodes a polycistronic mRNA comprising: (a) a first open reading frame (ORE) encoding the first polypeptide, (b) a second ORF encoding an additional cosmetic protein and (c) an intraribosome entry point (IRES) that separates (a) from (b). In some embodiments, the additional cosmetic protein is selected from a collagen protein, a fibronectin protein, an elastin protein, a lumican protein, a vitronectin protein, a vitronectin receptor protein, a laminin protein, a of neuromodulator and a fibrillin protein. In some embodiments, the additional cosmetic protein is a structural extracellular matrix protein (eg, collagen protein, elastin primer, fibronectin protein, laminin protein, fibrillin protein, etc.). In some embodiments, the additional cosmetic protein is a collagen protein, elastin protein, fibronectin protein, or laminin protein (for example, human collagen protein, human elastin protein, human fibronectin protein, or a human laminin protein). In some embodiments, the additional collagen protein (eg, an additional human collagen protein) is selected from COL1-1, COL1-2, COL2, COL3, COL4-1, COL4-2, COL4-3, COL4-4 , COL4-5, COL4-6, COL5-1, COL5-2, COL5-3, COL6-1, COL6-2, COL6-3, COL6-4, COL6-5, COL6-6, COL7, COL8, COL9 -1, COL9-2, COL9-3, COL10, COL11-1, COL11-2, COL12, COL13, COL14, COL15, COL16, COL17, COL18, COL19, COL20, COL21, COL22, COL23, COL24, COL25, COL26 , COL27 and COL28. In some embodiments, the additional collagen protein (eg, an additional human collagen protein) is selected from COL1-1, COL1-2, COL3, COL4-1, COL4-2, COL6-1, COL7, and COL17. In some embodiments, the first cosmetic protein and the additional cosmetic protein are different. In some embodiments, the first cosmetic protein is COL1-1 (eg, human COL1-1) and the additional cosmetic protein is COL1-2 (eg, human COL1-2). In some embodiments, the nucleic acid sequence encoding the IRES is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a nucleic acid sequence selected from SEQ. ID. NO.: 22 or SEQ. ID. NO.: 23. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes virus genome further comprises a second polynucleotide encoding a second cosmetic protein. In some embodiments, the second cosmetic protein is selected from a collagen protein, a fibronectin protein, an elastin protein, a lumican protein, a vitronectin protein, a vitronectin receptor protein, a laminin protein, a of neuromodulator and a fibrillin protein. In some embodiments, the second cosmetic protein is a structural extracellular matrix protein (eg, a collagen protein, an elastin primer, a fibronectin protein, a laminin protein, a fibrillin protein, etc.). In some embodiments, the second cosmetic protein is a collagen protein, elastin protein, fibronectin protein, or laminin protein (eg, human collagen protein, human elastin protein, human fibronectin protein, or a human laminin protein). In some c / CLnn / Lznz / q / Yi modalities, the second collagen protein (eg, a second human collagen protein) is selected from COL1-1, COL1-2, COL2, COL3, COL4-1, COL4- 2, COL4-3, COL4-4, COL4-5, COL4-6, COL5-1, COL5-2, COL5-3, COL6-1, COL6-2, COL6-3, COL6-4, COL6-5, COL6-6, COL7, COL8, COL9-1, COL9-2, COL9-3, COL10, COL11-1, COL11-2, COL12, COL13, COL14, COL15, COL16, COL17, COL18, C0L19, COL20, COL21, COL22, COL23, COL24, COL25, COL26, COL27 and COL28. In some embodiments, the second collagen protein (eg, a second human collagen protein) is selected from COL1-1, COL1-2, COL3, COL4-1, COL4-2, COL6-1, COL7, and COL17. In some embodiments, the first and second cosmetic proteins are different. In some embodiments, the first cosmetic protein is COL1-1 (eg, human COL1-1) and the second cosmetic protein is C0L1-2 (eg, human COL1-2). In some embodiments, the first cosmetic protein is C0L1-1 (eg, human COL1-1) and the second cosmetic protein is COL3 (eg, human COL3). In some embodiments that can be combined with any of the above embodiments, the recombinant herpes virus genome exhibits lower cytotoxicity when introduced into a target cell compared to a corresponding wild type herpes virus genome. In some embodiments, the target cell is a cell of the epidermis and / or the dermis. In some embodiments, the target cell is a human cell. In some embodiments, the target cell is a fibroblast. Other aspects of the present disclosure relate to a herpes virus comprising any of the recombinant herpes virus genomes described herein. In some embodiments, the herpes virus is replication competent. In some embodiments, the herpes virus is replication defective. In some modalities, the herpes virus is attenuated. In some modalities that can be combined with any of the above modalities, the herpes virus exhibits lower cytotoxicity compared to a corresponding wild type herpes virus. In some modalities that can be combined with any of the above modalities, the herpes virus is selected from a herpes simplex virus, a varicella zoster virus, a human cytomegalovirus, a herpes virus 6A, a herpes virus 6B, a herpes virus 7 and a herpes virus associated with Kaposi's sarcoma. In some modalities that can be combined with any of the above modalities, the herpes virus is a herpes simplex virus. In some embodiments, the herpes simplex virus is a herpes simplex virus type 1 (HSV-1), a herpes simplex virus type 2 (HSV-2) or any derivative thereof. In some embodiments, the herpes simplex virus is a herpes simplex virus type 1 (HSV-1). Other aspects of the present description refer to a composition comprising: (a) any of the recombinant genomes of the herpes virus described herein and / or any of the herpes viruses described herein and (b) a excipient. In some embodiments, the composition is sterile. In some modalities that can be combined with any of the above modalities, the composition is suitable for topical, transdermal, subcutaneous, intradermal, oral, intranasal, intratracheal, sublingual, buccal, rectal, vaginal, inhaled, intravenous, intraarterial, intramuscular, intracardiac, intraosseous, intraperitoneal, transmucosal, intravitreal, subretinal, intraarticular, periarticular, local, or epicutaneous. In some modalities that can be combined with any of the above modalities, the composition is suitable for intradermal administration. In some modalities that can be combined with any of the above modalities, the composition is c / CLnn / Lznz / q / Yi suitable for superficial injection. In some modalities that can be combined with any of the above modalities, the composition is a cosmetic composition. In some modalities that can be combined with any of the above modalities, the composition is a skin care product. Other aspects of the present disclosure refer to the use of any of the recombinant herpesvirus genomes described herein and / or any of the herpesviruses described herein as a medicament (eg, for cosmetic use). . Other aspects of the present disclosure refer to the use of any of the recombinant genomes of the herpes virus described herein and / or any of the herpes viruses described herein as therapy (for example, as aesthetic or cosmetic therapy ). Other aspects of the present description refer to the use of any of the recombinant genomes of the herpes virus described herein and / or any of the herpes viruses described herein in the manufacture of a medicament useful for treating one or more signs or symptoms of dermatological aging. Other aspects of the present disclosure relate to a method of enhancing, augmenting, increasing, and / or supplementing the levels of one or more of the extracellular dermal matrix proteins in a subject, wherein the method comprises administering to the subject an amount effective of any of the herpes viruses described herein and / or any of the compositions described herein. Other aspects of the present disclosure relate to a method of improving, augmenting, increasing, and / or supplementing the levels of one or more of the collagen proteins in a subject, wherein the method comprises administering to the subject an effective amount of either of the herpes viruses described herein and / or any of the compositions described herein. In some embodiments, the collagen protein(s) is collagen 3. In some embodiments, the reduction in endogenous collagen 3 levels is due to photoaging or chronological aging. Other aspects of the present disclosure relate to a method of improving, augmenting, augmenting, and / or supplementing a subject's soft tissue, wherein the method comprises administering to the subject an effective amount of any of the described herpes viruses herein and / or any of the compositions described herein. In some embodiments, the composition is injected into the subject's soft tissue. Other aspects of the present description refer to a method for improving the condition, quality and / or appearance of the skin in a subject in need thereof, wherein the method comprises administering to the subject an effective amount of any of the viruses from herpes described herein and / or any of the compositions described herein. In some embodiments, the composition is administered to one or more points of sun damage or other UV exposure, rough texture, sagging skin, wrinkles, or any combination of these. Other aspects of the present disclosure relate to a method of reducing the appearance of one or more superficial depressions in the skin of a subject in need thereof, wherein the method comprises administering to the subject an effective amount of any of the herpes viruses described herein and / or any of the compositions described herein. In some modalities, the superficial depression(s) in the skin are selected from the group consisting of nasolabial folds, crow's feet, frown marks, c / CLnn / Lznz / q / Yi expression lines, scars, glabellar lines, ptosis eyelids, tear grooves, nasojugal lines, rabbit furrows, cheek / midline ptosis, marionette wrinkles, blackhead marks, smile wrinkles, laugh lines, furrows of the chin, neck wrinkles, platysma of the neck and any combination of these. Other aspects of the present description refer to a method of increasing and / or improving at least one of the texture, softness, elasticity or tension of the skin of a subject in need thereof, wherein the method comprises administering to the subject an amount effective of any of the herpes viruses described herein and / or any of the compositions described herein. In some modalities that can be combined with any of the above modalities, the subject's skin is aged skin. In some modalities that can be combined with any of the above modalities, the subject's skin is damaged by exposure to ultraviolet light. In some modalities that can be combined with any of the above modalities, the subject's skin is wrinkled. Other aspects of the present disclosure relate to a method of reducing one or more dermatological signs of aging in a subject in need thereof, wherein the method comprises administering to the subject an effective amount of any of the herpes viruses described in herein and / or any of the compositions described herein. In some modalities, the reduction of one or more dermatological signs of aging is accomplished by: (a) treating, reducing, and / or preventing lines and / or wrinkles, (b) reducing the size of skin pores, (c) improvement of the thickness, firmness and / or resistance of the skin, (d) improvement of the softness, smoothness and / or silkiness of the skin, (e) improvement of the tone, luminosity and / or clarity of the skin, (f) improvement of collagen and / or pro-collagen production, (g) improvement of skin texture and / or promotion of retexturization, (h) improvement of the appearance of skin contours, (i) restoration of radiance and / or shine of the skin, (j) improvement of the deteriorated appearance of the skin due to aging and / or menopause, (k) improvement of the hydration of the skin, (I) increase of the elasticity and / or resistance of the skin , (m) treatment, reduction and / or prevention of sagging skin, (n) improvement of skin firmness, (o) reduction of pigmentation, discolored skin and / or scarring (c such as acne scars), (p) enhancement of the optical properties of the skin by light reflection or diffraction, or (q) any combination of these. In some modalities that can be combined with any of the above modalities, the subject is a human. In some modalities that can be combined with any of the above modalities, the herpes virus or composition is administered to the subject via topical, transdermal, subcutaneous, epicutaneous, intradermal, oral, sublingual, buccal, rectal, vaginal, intravenous, intraarterial, intramuscular, intraosseous, intracardial, intraperitoneal, transmucosal, intravitreal, subretinal, intraarticular, periarticular, local, or by inhalation. In some modalities that can be combined with any of the above modalities, the herpes virus or the composition is administered to the subject intradermally. In some modalities that can be combined with any of the above modalities, the herpes virus or composition is administered by superficial injection. Other aspects of the present disclosure refer to a composition comprising: a herpes simplex virus (HSV) comprising a recombinant nucleic acid, wherein the recombinant nucleic acid comprises a first polynucleotide encoding a first polypeptide comprising a first protein of human collagen and a c / CLnn / Lznz / q / Yi excipient. In some embodiments, the recombinant nucleic acid comprises two or more copies of the first polynucleotide. In some modalities that can be combined with any of the above modalities, HSV is replication defective. In some modalities that can be combined with any of the above modalities, HSV is replication competent. In some modalities that can be combined with any of the above modalities, HSV is a herpes simplex virus type 1, a herpes simplex virus type 2, or any derivative thereof. In some embodiments, the recombinant nucleic acid is a herpes simplex virus amplicon. In some embodiments, the herpes simplex virus amplicon is an HSV-1 amplicon or a hybrid HSV-1 amplicon. In some embodiments, the HSV-1 hybrid amplicon is a hybrid HSV / AAV amplicon, a hybrid HSV / EBV amplicon, and a hybrid HSV / EBV / RV amplicon or a hybrid HSV / Sleeping Beauty amplicon. In some embodiments, the recombinant nucleic acid is a recombinant herpes simplex virus genome. In some embodiments, the recombinant herpes simplex virus genome is a recombinant HSV-1 genome, a recombinant HSV-2 genome, or any derivative thereof. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in a herpes simplex virus gene. In some embodiments, the herpes simplex virus gene is selected from the group consisting of infected cell protein (ICP) 0, ICP4, ICP22, ICP27, ICP47, thymidine kinase (tk), extensive unique region (UL) 41, and UL55. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in one or both copies of the ICP4 gene. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP22 gene. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the UL41 gene. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICPO gene. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP27 gene. In some modalities that can be combined with any of the above modalities, the inactivating mutation is a deletion of the coding sequence of the gene(s). In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises the first polynucleotide within a viral gene locus. In some embodiments that may be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises the first polynucleotide within one or both copies of the ICP4 viral gene loci. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises the first polynucleotide within the ICP22 viral gene locus. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises the first polynucleotide within the UL41 viral gene locus. In some c / c i nn / ι znz / zi / Yl· modalities that can be combined with any of the above modalities, HSV exhibits lower cytotoxicity compared to a wild-type herpes simplex virus. In some embodiments that can be combined with any of the above modalities, the first human collagen protein is selected from a collagen alpha-1(I) chain polypeptide (C0L1-1), an alpha-2(l) chain polypeptide ) collagen (COL1-2), an alpha-1(II) chain polypeptide of collagen (COL2), an alpha1(111) chain polypeptide of collagen (COL3), an alpha-1(IV) chain polypeptide of collagen (COL4-1), a collagen alpha2(IV) chain polypeptide (COL4-2), a collagen alpha-3(IV) chain polypeptide (COL4-3), a collagen alpha4(IV) chain polypeptide collagen (COL4-4), a collagen alpha-5(lV) chain polypeptide (COL4-5), a collagen alpha6(IV) chain polypeptide (COL4-6), an alpha-1 (V) chain polypeptide ) collagen (COL5-1), a collagen alpha2(V) chain polypeptide (COL5-2), a collagen alpha-3(V) chain polypeptide (COL5-3), an alpha-chain polypeptide ( VI) collagen (COL6-1), an alpha-2(VI) chain polypeptide of collagen (C OL6-2), an alpha-chain polypeptide Collagen 3(VI) (COL6-3), an alpha-chain polypeptide Collagen 4(VI) (COL6-4), an alpha5(VI) chain polypeptide (COL6-5), an alpha-chain polypeptide Collagen 6(VI) (COL6-6), a collagen alpha-1 (Vil) chain polypeptide (COL7), an alpha-1 (VIII) chain polypeptide (COL8), an alpha-1 (Vil) chain polypeptide IX) collagen (COL91), a collagen alpha-2(IX) chain polypeptide (COL9-2), a collagen alpha-3(IX) chain polypeptide (COL93), an alpha-1 chain polypeptide ( X) collagen (COL10), an alpha-1 (XI) chain polypeptide of collagen (COL111), an alpha-2 (XI) chain polypeptide of collagen (COL11-2), an alpha-1 chain polypeptide ( XII) of collagen (COL12), an alpha-1 chain polypeptide (XIII) of collagen (COL13), an alpha-1 chain polypeptide (XIV) of collagen (COL14), an alpha-1 chain polypeptide (XV) collagen (COL15), a collagen alpha-1(XVI) chain polypeptide (COL16), a collagen alpha-1(XVII) chain polypeptide (COL17), a collagen polypeptide collagen alpha-1 (XVIII) chain peptide (COL18), collagen alpha-1 (XIX) chain polypeptide (COL19), collagen alpha-1 (XX) chain polypeptide (COL20), collagen alpha-1 (XX) chain polypeptide collagen alpha-1 (XXI) chain (COL21), collagen alpha-1 (XXII) chain polypeptide (COL22), collagen alpha-1 (XXIII) chain polypeptide (COL23), alpha chain polypeptide -1 (XXIV) collagen (COL24), an alpha-1 (XXV) chain polypeptide of collagen (COL25), an alpha1 (XXVI) chain polypeptide of collagen (COL26), an alpha-1 chain polypeptide (XXVII ) collagen (COL27) and a collagen alpha-1 (XXVIII) chain polypeptide (COL28). In some embodiments that can be combined with any of the above embodiments, the first human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-1, COL6-1, COL7, and COL17. In some embodiments that can be combined with any of the above embodiments, the nucleic acid sequence encoding the first human collagen protein is at least 80%, at least 85%, at least 90%, at least 91%, at at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an acid sequence nucleic acid selected from SEQ. ID. NO.: 1-14. In some embodiments that can be combined with any of the above embodiments, the first human collagen protein comprises a sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with an amino acid sequence selected from SEQ. ID. NO.: 15-21. In some modalities that c / CLnn / Lznz / q / Yi can be combined with any of the above modalities, the first human collagen protein is not C0L7. In some embodiments that can be combined with any of the above embodiments, the first polypeptide comprises: (a) the first human collagen protein, (b) another human collagen protein, and (c) a linker polypeptide that binds (a) to (b). In some embodiments, the linker polypeptide is a cleavable linker polypeptide. In some embodiments, the linker polypeptide comprises a sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95% , at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence selected from SEQ. ID. NO.: 28-31. In some embodiments, the other human collagen protein is selected from COL1-1, COL1-2, COL2, COL3, COL4-1, COL4-2, COL4-3, COL4-4, COL4-5, COL4-6, COL5 -1, COL5-2, COL5-3, COL6-1, COL6-2, COL6-3, COL6-4, COL6-5, COL6-6, COL7, COL8, COL9-1, COL9-2, COL9-3 , COL10, COL11-1, COL11-2, COL12, COL13, COL14, COL15, COL16, COL17, COL18, COL19, COL20, COL21, COL22, COL23, COL24, COL25, COL26, COL27 and COL28. In some embodiments, the other human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-1, COL6-1, COL7, and COL17. In some embodiments, the nucleic acid sequence encoding the other human collagen protein is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with a nucleic acid sequence selected from SEQ. ID. NO.: 1-14. In some embodiments, the other human collagen protein comprises a sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence selected from SEQ. ID. NO.: 15-21. In some embodiments, the first human collagen protein and the other human collagen protein are different. In some embodiments that can be combined with any of the above embodiments, the first polynucleotide encodes a polycistronic mRNA comprising: (a) a first open reading frame (ORE) encoding the first polypeptide, (b) a second ORF encoding an additional human collagen protein and (c) an intraribosome entry point (IRES) separating (a) from (b). In some embodiments, the nucleic acid sequence encoding the IRES is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a nucleic acid sequence selected from SEQ. ID. NO.: 22 or SEQ. ID. NO.: 23. In some embodiments, the additional human collagen protein is selected from COL1-1, COL1-2, COL2, COL3, COL4-1, COL4-2, COL4-3, COL4-4, COL4-5, COL4-6, COL5-1, COL5-2, COL5-3, COL6-1, COL6-2, COL6-3, COL6-4, COL6-5, COL6-6, COL7, COL8, COL9-1, COL9- 2, COL9-3, COL10, COL11-1, COL11-2, COL12, COL13, COL14, COL15, COL16, COL17, COL18, COL19, COL20, COL21, COL22, COL23, COL24, COL25, COL26, COL27 and COL28. In some embodiments, the additional human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-1, COL6-1, COL7, and COL17. In some embodiments, the nucleic acid sequence encoding the additional human collagen protein is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% c / CLnn / Lznz / q / Yi sequence identity to a nucleic acid sequence Selected from SEQ. ID. NO.: 1-14. In some embodiments, the additional human collagen protein comprises a sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence selected from SEQ. ID. NO.: 15-21. In some embodiments, the first human collagen protein and the additional human collagen protein are different. In some embodiments that can be combined with any of the above embodiments, the recombinant nucleic acid further comprises a second polynucleotide encoding a second human collagen protein. In some embodiments, the recombinant nucleic acid comprises two or more copies of the second polynucleotide. In some embodiments, the second human collagen protein is selected from COL1-1, COL1-2, COL2, COL3, COL4-1, COL4-2, COL4-3, COL4-4, COL4-5, COL4-6, COL5. -1, COL5-2, COL5-3, COL6-1, COL6-2, COL6-3, COL6-4, COL6-5, COL6-6, COL7, COL8, COL9-1, COL9-2, COL9-3 , COL10, COL11-1, COL11-2, COL12, COL13, COL14, COL15, COL16, COL17, COL18, COL19, COL20, COL21, COL22, COL23, COL24, COL25, COL26, COL27 and COL28. In some embodiments, the second human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-1, COL6-1, COL7, and COL17. In some embodiments, the nucleic acid sequence encoding the second human collagen protein is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with a nucleic acid sequence selected from SEQ. ID. NO.: 1-14. In some embodiments, the second human collagen protein comprises a sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence selected from SEQ. ID. NO.: 15-21. In some embodiments, the first and second human collagen proteins are different. In some embodiments that may be combined with any of the above embodiments, the recombinant nucleic acid is a recombinant herpes simplex virus genome, wherein the recombinant herpes simplex virus genome comprises the second polynucleotide within a viral gene locus. . In some embodiments, the recombinant herpes simplex virus genome comprises the second polynucleotide within one or both copies of the ICP4 viral gene loci. In some embodiments, the recombinant herpes simplex virus genome comprises the second polynucleotide within the ICP22 viral gene locus. In some embodiments, the recombinant herpes simplex virus genome comprises the second polynucleotide within the UL41 viral gene locus. In some embodiments, the recombinant herpes simplex virus genome comprises the first polynucleotide within one or both copies of the ICP4 viral gene loci and the second polynucleotide within the ICP22 viral gene locus. In some embodiments, the recombinant herpes simplex virus genome comprises the first polynucleotide within one or both copies of the ICP4 viral gene loci and the second polynucleotide within the UL41 viral gene locus. In some modalities that can be combined with any of the above modalities, the excipient is adapted for cutaneous (systemic or topical), transdermal, subcutaneous and / or intradermal administration. In c / CLnn / Lznz / q / Yi some modalities that can be combined with any of the above modalities, the excipient comprises a hydroxypropylmethylcellulose gel. In some modalities that can be combined with any of the above modalities, the excipient is adapted for intradermal administration. In some embodiments that can be combined with any of the above embodiments, the excipient comprises a phosphate buffer. In some embodiments that can be combined with any of the above embodiments, the excipient comprises glycerol. In some embodiments that can be combined with any of the above embodiments, the excipient comprises a lipid carrier. In some embodiments that can be combined with any of the above embodiments, the excipient comprises a nanoparticle carrier. In some modalities that can be combined with any of the above modalities, the composition is a cosmetic composition. In some embodiments, the cosmetic composition is a skin care product. Other aspects of the present disclosure relate to a kit comprising any of the compositions described herein and instructions for administering the composition. Other aspects of the present disclosure relate to a method of improving, augmenting, increasing, and / or supplementing the levels of one or more of the human collagen proteins in a subject, wherein the method comprises administering to the subject an effective amount of any of the compositions described herein. Other aspects of the present disclosure relate to a method of improving, augmenting, augmenting, and / or supplementing a subject's soft tissue, wherein the method comprises administering to the subject an effective amount of any of the compositions described herein. In some embodiments, the composition is injected into a subject's soft tissue. Other aspects of the present description refer to a method of improving the quality, condition and / or appearance of the skin in a subject in need thereof, wherein the method comprises administering to the subject an effective amount of any of the compositions described in the present. In some modalities, the condition is selected from sun damage, aging, UV exposure, rough texture, sagging skin, wrinkles, and any combination of these. Other aspects of the present disclosure refer to a method of reducing the appearance of one or more superficial depressions in the skin of a subject in need thereof, wherein the method comprises administering to the subject an effective amount of any of the compositions described in the present. In some embodiments, administration of the composition reduces the appearance of the superficial depression(s) in the subject's skin for at least about three months, at least about six months, at least about nine months, or at least about 12 months. months. In some embodiments, the appearance of the superficial depression(s) in the subject's skin is reduced after administration of the composition compared to the appearance of the superficial depression(s) in the subject's skin prior to administration of the composition. Other aspects of the present description refer to a method of increasing and / or improving at least one of the texture, softness, elasticity or tension of the skin of a subject in need thereof, wherein the method comprises administering to the subject an amount effectiveness of any of the compositions described herein. In some modalities, the subject's skin maintains at least one of greater and / or better texture, smoothness, elasticity, or tension for at least about three months, at least about six months, at least about nine months, or c / CLnn / Lznz / q / Yi minus about 12 months after administration of the composition. In some embodiments, at least one of the subject's skin texture, smoothness, elasticity, or tightness is increased and / or improved upon administration of the composition as compared to the subject's skin texture, smoothness, elasticity, or tightness before administration of the composition. In some modalities that can be combined with any of the above modalities, the subject's skin is aged skin. In some modalities that can be combined with any of the above modalities, the subject's skin is damaged by exposure to ultraviolet light. In some modalities that can be combined with any of the above modalities, the subject's skin is wrinkled. Other aspects of the present disclosure relate to a method of reducing one or more dermatological signs of aging in a subject in need thereof, wherein the method comprises administering to the subject an effective amount of any of the compositions described herein. In some modalities, the reduction of one or more dermatological signs of aging is selected from: (a) treatment, reduction and / or prevention of lines and / or wrinkles, (b) reduction of the size of skin pores, (c ) improvement of the thickness, firmness and / or resistance of the skin, (d) improvement of the softness, smoothness and / or silkiness of the skin, (e) improvement of the tone, luminosity and / or clarity of the skin , (f) improvement of collagen and / or procollagen production, (g) improvement of skin texture and / or promotion of retexturization, (h) improvement of appearance of skin contours, (i) return of splendor and / or shine of the skin, (j) improvement of the deteriorated appearance of the skin due to aging and / or menopause, (k) improvement of the hydration of the skin, (I) increase of the elasticity and / or resistance of the skin, (m) treatment, reduction and / or prevention of sagging skin, (n) improvement of skin firmness, (o) reduction of pigmentation, discolored skin and / or scarring r acne, (p) enhancement of the optical properties of the skin by light reflection or diffraction, and (q) any combination of these. In some embodiments, the dermatological sign(s) of aging in the subject is reduced after administration of the composition compared to the dermatological sign(s) of aging in the subject prior to administration of the composition. In some modalities that can be combined with any of the above modalities, the subject is a human. In some modalities that can be combined with any of the above modalities, the composition is administered to the subject via the dermal (systemic or topical), transdermal, subcutaneous, or intradermal routes. In some embodiments, the composition is administered by superficial injection. In some embodiments, the administration is administered to the subject intradermally. In some embodiments, the administration is administered to the subject only once. In some embodiments, the composition is administered to the subject at least twice. In some embodiments, at least about 15, at least about 30, at least about 60, at least about 90, or at least about 120 days elapse between administrations. In some modalities that can be combined with any of the above modalities, the composition is administered to one or more affected and / or unaffected areas of the subject. In some modalities that can be combined with any of the above modalities, the skin is abraded prior to administration. Other aspects of the present disclosure refer to a recombinant nucleic acid comprising a first polynucleotide encoding a first polypeptide comprising a first human collagen protein, wherein the c / CLnn / Lznz / q / Yi recombinant nucleic acid is a recombinant genome. of the herpes simplex virus. In some embodiments, the recombinant nucleic acid comprises two or more copies of the first polynucleotide. In some embodiments, the recombinant herpes simplex virus genome is a recombinant HSV-1 genome, a recombinant HSV-2 genome, or any derivative thereof. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in a herpes simplex virus gene. In some embodiments, the herpes simplex virus gene is selected from the group consisting of infected cell protein (ICP) 0, ICP4, ICP22, ICP27, ICP47, thymidine kinase (tk), extensive unique region (UL) 41, and UL55. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in one or both copies of the ICP4 gene. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP22 gene. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the UL41 gene. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICPO gene. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP27 gene. In some modalities that can be combined with any of the above modalities, the inactivating mutation is a deletion of the coding sequence of the gene(s). In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises the first polynucleotide within a viral gene locus. In some embodiments that may be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises the first polynucleotide within one or both copies of the ICP4 viral gene loci. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises the first polynucleotide within the ICP22 viral gene locus. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises the first polynucleotide within the UL41 viral gene locus. In some modalities that can be combined with any of the above modalities, HSV exhibits lower cytotoxicity compared to a wild-type herpes simplex virus. In some modalities that can be combined with any of the above modalities, the first human collagen protein is selected from COL1-1, COL1-2, COL2, C0L3, COL4-1, COL4-2, COL4-3, COL4-4 , COL4-5, COL46, COL5-1, COL5-2, COL5-3, COL6-1, COL6-2, COL6-3, COL6-4, COL6-5, COL6-6, C0L7, COL8, C0L9-1 , COL9-2, COL9-3, COL10, COL11-1, C0L11-2, COL12, COL13, COL14, COL15, COL16, COL17, COL18, COL19, COL20, COL21, COL22, COL23, COL24, COL25, COL26, COL27 and C0L2. In some embodiments that can be combined with any of the above embodiments, the first human collagen protein is selected from C0L1-1, COL1-2, COL3, COL4-1, COL6-1, C0L7, and C0L17. In some embodiments that can be combined with any of the above c / CLnn / Lznz / q / Yi embodiments, the nucleic acid sequence encoding the first human collagen protein is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% of sequence identity with a nucleic acid sequence selected from SEQ. ID. NO.: 1-14. In some embodiments that can be combined with any of the above embodiments, the first human collagen protein comprises a sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with an amino acid sequence selected from SEQ. ID. NO.: 15-21. In some modalities that can be combined with any of the above modalities, the first human collagen protein is not COL7. In some embodiments that can be combined with any of the above embodiments, the first polypeptide comprises: (a) the first human collagen protein, (b) another human collagen protein, and (c) a linker polypeptide that binds (a) to (b). In some embodiments, the linker polypeptide is a cleavable linker polypeptide. In some embodiments, the linker polypeptide comprises a sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95% , at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence selected from SEQ. ID. NO.: 28-31. In some embodiments, the other human collagen protein is selected from COL1-1, COL1-2, COL2, COL3, COL4-1, COL4-2, COL4-3, COL4-4, COL4-5, COL4-6, COL5 -1, COL5-2, COL5-3, COL6-1, COL6-2, COL6-3, COL6-4, COL6-5, COL6-6, COL7, COL8, COL9-1, COL9-2, COL9-3 , COL10, COL11-1, COL11-2, COL12, COL13, COL14, COL15, COL16, COL17, COL18, COL19, COL20, COL21, COL22, COL23, COL24, COL25, COL26, COL27 and COL28. In some embodiments, the other human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-1, COL6-1, COL7, and COL17. In some embodiments, the nucleic acid sequence encoding the other human collagen protein is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with a nucleic acid sequence selected from SEQ. ID. NO.: 1-14. In some embodiments, the other human collagen protein comprises a sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence selected from SEQ. ID. NO.: 15-21. In some embodiments, the first human collagen protein and the other human collagen protein are different. In some embodiments that can be combined with any of the above embodiments, the first polynucleotide encodes a polycistronic mRNA comprising: (a) a first open reading frame (ORE) encoding the first polypeptide, (b) a second ORF encoding an additional human collagen protein and (c) an intraribosome entry point (IRES) separating (a) from (b). In some embodiments, the nucleic acid sequence encoding the IRES is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a nucleic acid sequence selected from SEQ. ID. NO.: 22 or SEQ. ID. NO.: c / CLnn / Lznz / q / Yi 23. In some embodiments, the additional human collagen protein is selected from COL1-1, COL1-2, COL2, COL3, C0L4-1, COL4-2, COL4-3, COL4-4, COL4-5, COL4-6 , C0L5-1, COL5-2, COL5-3, C0L6-1, COL6-2, COL6-3, COL6-4, COL6-5, COL6-6, C0L7, COL8, C0L9-1, COL9-2, COL9 -3, COL10, COL11-1, C0L11-2, COL12, COL13, COL14, COL15, COL16, C0L17, C0L18, C0L19, COL20, C0L21, COL22, COL23, COL24, COL25, COL26, COL27 and COL28. In some embodiments, the additional human collagen protein is selected from COL1-1, C0L1-2, C0L3, COL4-1, COL6-1, C0L7, and C0L17. In some embodiments, the nucleic acid sequence encoding the additional human collagen protein is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with a nucleic acid sequence selected from SEQ. ID. NO.: 1-14. In some embodiments, the additional human collagen protein comprises a sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence selected from SEQ. ID. NO.: 15-21. In some embodiments, the first human collagen protein and the additional human collagen protein are different. In some embodiments that can be combined with any of the above embodiments, the recombinant nucleic acid further comprises a second polynucleotide encoding a second human collagen protein. In some embodiments, the recombinant nucleic acid comprises two or more copies of the second polynucleotide. In some embodiments, the second human collagen protein is selected from COL1-1, COL1-2, COL2, COL3, COL4-1, COL4-2, COL4-3, COL4-4, COL4-5, COL4-6, COL5. -1, COL5-2, COL5-3, COL6-1, COL6-2, COL6-3, COL6-4, COL6-5, COL6-6, COL7, COL8, COL9-1, COL9-2, COL9-3 , COL10, COL11-1, COL11-2, COL12, COL13, COL14, COL15, COL16, COL17, COL18, COL19, COL20, COL21, COL22, COL23, COL24, COL25, COL26, COL27 and COL28. In some embodiments, the second human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-1, COL6-1, COL7, and COL17. In some embodiments, the nucleic acid sequence encoding the second human collagen protein is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with a nucleic acid sequence selected from SEQ. ID. NO.: 1-14. In some embodiments, the second human collagen protein comprises a sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence selected from SEQ. ID. NO.: 15-21. In some embodiments, the first and second human collagen proteins are different. In some embodiments that can be combined with any of the above embodiments, the recombinant herpes simplex virus genome comprises the second polynucleotide within a viral gene locus. In some embodiments, the recombinant herpes simplex virus genome comprises the second polynucleotide within one or both copies of the ICP4 viral gene loci. In some embodiments, the recombinant herpes simplex virus genome comprises the second polynucleotide within the ICP22 viral gene locus. In some embodiments, the c / CLnn / Lznz / q / Yi recombinant herpes simplex virus genome comprises the second polynucleotide within the UL41 viral gene locus. In some embodiments, the recombinant herpes simplex virus genome comprises the first polynucleotide within one or both copies of the ICP4 viral gene loci and the second polynucleotide within the ICP22 viral gene locus. In some embodiments, the recombinant herpes simplex virus genome comprises the first polynucleotide within one or both copies of the ICP4 viral gene loci and the second polynucleotide within the UL41 viral gene locus. Other aspects of the present disclosure relate to a host cell comprising any of the recombinant nucleic acids described herein. In some embodiments, the host cell is a eukaryotic cell. In some embodiments, the host cell is a mammalian cell. In some embodiments, the host cell is a human cell or a non-human primate cell. In some embodiments, the host cell is a Vero cell. In some embodiments, the host cell is a complementary host cell. Other aspects of the present disclosure relate to a method of harvesting a herpes simplex virus, wherein the method comprises: (a) contacting a complementary host cell with any of the recombinant nucleic acids described herein, and (b ) harvesting the herpes simplex virus generated by the complementary host cell. Other aspects of the present disclosure relate to a method of harvesting a herpes simplex virus, wherein the method comprises: (a) culturing the host cell comprising any of the recombinant nucleic acids described herein, and (b) harvesting the herpes simplex virus generated by the host cell. BRIEF DESCRIPTION OF THE DRAWINGS The application or patent file contains at least one color drawing. The office will provide copies of this patent or patent application publication with color drawings upon request and payment of the necessary fee. Figures 1A-1N show schematics of wild type and modified herpes simplex virus genomes. Figure 1A shows a wild type herpes simplex virus genome. Figure 1B shows a modified herpes simplex virus genome comprising deletions of the coding sequences of ICP4 (both copies) and ICP22, with a polynucleotide containing the coding sequence of a first human collagen polypeptide operably linked to a heterologous promoter integrated into each of the ICP4 loci. Figure 1C shows a modified herpes simplex virus genome comprising ICP4 coding sequence deletions (both copies), with a polynucleotide containing the coding sequence for a first human collagen polypeptide operably linked to a promoter. integrated heterolog at each of the ICP4 loci. Figure 1D shows a modified herpes simplex virus genome comprising deletions of the coding sequences of ICP4 (both copies) and ICP22, with a polynucleotide containing 1) the coding sequence of a first formably linked human collagen polypeptide. operatively linked to a first heterologous promoter and 2) the coding sequence for a second human collagen polypeptide operably linked to a second heterologous promoter integrated into each of the ICP4 loci. Both the first and second human collagen polypeptides are encoded on the same DNA strand. Figure 1E shows a modified simple c / CLnn / Lznz / q / Yi herpesvirus genome comprising deletions of the ICP4 coding sequence (both copies), with a polynucleotide containing 1) the coding sequence of a primer. human collagen polypeptide operatively linked to a first heterologous promoter and 2) the coding sequence for a second human collagen polypeptide operatively linked to a second heterologous promoter integrated into each of the ICP4 loci. Both the first and second human collagen polypeptides are encoded on the same DNA strand. Figure 1F shows a modified herpes simplex virus genome comprising deletions of the coding sequences of ICP4 (both copies) and ICP22, with a polynucleotide containing 1) the coding sequence of a first formably linked human collagen polypeptide. operatively linked to a first heterologous promoter and 2) the coding sequence for a second human collagen polypeptide operably linked to a second heterologous promoter integrated into each of the ICP4 loci. The first and second human collagen polypeptides are encoded on opposite strands of DNA. Figure 1G shows a modified herpes simplex virus genome comprising deletions of the ICP4 coding sequence (both copies), with a polynucleotide containing 1) the coding sequence of a first human collagen polypeptide operably linked to a first heterologous promoter and 2) the coding sequence for a second human collagen polypeptide operably linked to a second heterologous promoter integrated into each of the ICP4 loci. The first and second human collagen polypeptides are encoded on opposite strands of DNA. Figure 1H shows a modified herpes simplex virus genome comprising deletions of the coding sequences of ICP4 (both copies) and ICP22, with a polynucleotide encoding polycistronic mRNA operatively linked to a heterologous promoter integrated into each of the . ICP4 loci. The polycistronic mRNA contains the coding sequence for a first human collagen polypeptide and a second human collagen polypeptide separated by an intraribosome entry site (IRES). Figure 11 shows a modified herpes simplex virus genome comprising deletions of the ICP4 coding sequence (both copies), with a polynucleotide encoding polycistronic mRNA operably linked to a heterologous promoter integrated into each of the HSV loci. ICP4. The polycistronic mRNA contains the coding sequence for a first human collagen polypeptide and a second human collagen polypeptide separated by an intraribosome entry site (IRES).Figure 1J shows a modified herpes simplex virus genome comprising deletions of the coding sequences of ICP4 (both copies) and ICP22, with a polynucleotide containing the coding sequence of a chimeric polypeptide operatively linked to a heterologous promoter. integrated into each of the ICP4 loci. The chimeric polypeptide comprises the amino acid sequence of a first human collagen polypeptide and a second human collagen polypeptide separated by a cleavable linker. Figure 1K shows a modified herpes simplex virus genome comprising deletions of the ICP4 coding sequence (both copies), with a polynucleotide containing the coding sequence for a chimeric polypeptide operatively linked to a heterologous promoter integrated into each of the ICP4 loci. The chimeric polypeptide comprises the amino acid sequence of a first human collagen polypeptide and a second human collagen polypeptide separated by a cleavable linker. Figure 1L shows a modified herpes simplex virus genome comprising deletions of the c / CLnn / Lznz / q / Yi sequences coding for ICP4 (both copies) and ICP22, with a first polynucleotide containing the coding sequence for a first human collagen polypeptide operably linked to a heterologous promoter integrated into each of the ICP4 loci and a second polynucleotide containing the coding sequence for a second human collagen polypeptide operatively linked to a heterologous promoter integrated into the ICP22 locus. Figure 1M shows a modified herpes simplex virus genome comprising deletions of the coding sequences of ICP4 (both copies), ICP22 and UL41, with a first polynucleotide containing the coding sequence of a first human collagen polypeptide linked to operably linked to a heterologous promoter integrated into each of the ICP4 loci and a second polynucleotide containing the coding sequence for a second human collagen polypeptide operably linked to a heterologous promoter integrated into the UL41 locus. Figure 1N shows a modified herpes simplex virus genome comprising deletions of the coding sequences of ICP4 (both copies) and UL41, with a first polynucleotide containing the coding sequence of a first operably linked human collagen polypeptide. to a heterologous promoter integrated into each of the ICP4 loci and a second polynucleotide containing the coding sequence for a second human collagen polypeptide operably linked to a heterologous promoter integrated into the UL41 locus. Figures 2A-2B show schematics of replication-defective herpes simplex virus type 1 containing human collagen 7 (COL7) expression cassettes. Figure 2A shows a schematic of the "KCA211" virus. Figure 2B shows a schematic of the "SAR-COL7" virus. Figures 3A-3B show COL7 expression in HaCaT cells infected with KCA211 or SAR-COL7 at the indicated MOIs. Figure 3A shows the expression of COL7 in HaCaT cells infected with KCA211 or SAR-COL7 at the indicated MOIs, as assessed via qPCR. Data are shown as multiple change from SAR-COL7, after normalization for GAPDH. Figure 3B shows the expression of COL7 in naive HaCaT cells or HaCaT cells infected with KCA211 or SAR-COL7 at the indicated MOIs, as assessed by Western blot analysis. Figures 4A-4B show immunofluorescence images of human COL7 expression in mock-infected primary human cells isolated from a healthy (normal) patient, and mock- or SAR-COL7-infected primary human cells isolated from a patient. suffering from recessive dystrophic epidermolysis bullosa (RAEB). Figure 4A shows the expression of human COL7 in wild-type and EADR primary human keratinocytes, mock-infected, or in EADR-infected primary human keratinocytes with SAR-COL7 at the indicated multiplicity of infections (MOI). Figure 4B shows the expression of human COL7 in wild-type and EADR primary human fibroblasts, mock-infected, or in EADR-infected primary human fibroblasts with SAR-COL7 at the indicated MOIs. Figures 5A-5B show a quantitative POR analysis of human C0L7 expression in mock-infected primary human cells isolated from a healthy patient and mock- or SARCOL7-infected primary human cells isolated from a patient suffering from epidermolysis. recessive dystrophic bullosa (AD). Figure 5A shows the expression of human COL7 in wild-type (N-HDK) and EADR c / CLnn / Lznz / q / YL (EB-HDK) primary human keratinocytes, mock-infected, or in EADR-infected primary human keratinocytes. SAR-COL7 at the indicated MOIs. C0L7 expression is shown as the relative multiple change relative to mock-infected wild-type primary human keratinocytes. Figure 5B shows the expression of human C0L7 in wild-type (N-HDF) and EADR (EB-HDF) primary human fibroblasts, mock-infected, or in EADR-infected primary human fibroblasts with SAR-COL7 at the indicated MOIs. C0L7 expression is shown as the relative multiple change relative to mock-infected wild-type primary human fibroblasts. Figures 6A-6B show cell adhesion of SARC0L7-infected or uninfected (control) primary human keratinocytes with EADR to treated or untreated (plastic) wells of a microwell plate. Figure 6A shows cell adhesion to untreated (plastic) wells or wells treated with increasing concentrations of rat tail collagen 1. Figure 6B shows cell adhesion to untreated (plastic) wells or wells treated with increasing concentrations of human plasma fibronectin. Figure 7 shows representative immunofluorescence images of human COL7 expression and basement membrane zone (BMZ) deposition at day 5, in organotypic cultures made from primary human keratinocytes and fibroblasts with EADR. , infected with SAR-COL7. Both keratinocytes and fibroblasts were infected in situ at the indicated MOI after culture construction. Figures 8A-8D show the human COL7A1 genome and transcript levels observed in the skin of a mouse without infection (control) or in the skin of a mouse after topical or intradermal delivery of SAR-COL7, as assessed by of qPCR. Error bars represent SEM. Figure 8A shows human COL7A1 transcript levels / 100 ng total RNA in mouse skin, 3 days post infection. Figure 8B shows the number of human COL7A1 DNA copies / 100 ng of total DNA in the skin of a mouse, 3 days post infection. Figure 8C shows human COL7A1 transcript levels / 100 ng total RNA in mouse skin, 6 days post infection. Figure 8D shows the number of human COL7A1 DNA copies / 100 ng total DNA in the skin of a mouse, 6 days post infection. Figures 9A-9B show representative immunofluorescence images of human COL7 expression in mouse skin after SAR-COL7 delivery. Figure 9A shows a representative immunofluorescent image of human COL7 expression in mouse skin following intradermal delivery of SAR-COL7. Figure 9B shows a representative immunofluorescent image of human COL7 expression in mouse skin following topical delivery of SAR-COL7. Figures 10A-10B show the human COL7A1 genome and transcript levels observed in the skin of a BALB / c mouse after intradermal delivery of vehicle, SAR-COL7 or KCA211, as assessed via qPCR. Figure 10A shows human COL7A1 transcript levels / 100 ng total RNA in the skin of a BALB / c mouse. Figure 10B shows the number of human COL7A1 DNA copies / 100 ng total DNA in the skin of a BALB / c mouse. Figures 11A-11B show the human COL7A1 genome and transcript levels observed at each injection site in the skin of a hypomorph mouse following intradermal delivery of high doses of HSV-GFP (GFP control) or SAR-COL7, as evaluation through qPCR. Each bar represents a single sample at the indicated c / CLnn / Lznz / q / Yi time point. Figure 11A shows human COL7A1 transcript levels / 100 ng total RNA in the skin of a hypomorph mouse. Figure 11B shows the number of human COL7A1 DNA copies / 100 ng of total DNA in the skin of a hypomorph mouse. Figures 12A-12B show representative immunofluorescence images of human COL7 expression in the skin of a hypomorph mouse following intradermal delivery of high doses of HSV-GFP (GFP control) or SARCOL7. Figure 12A shows control immunofluorescence imaging (GFP) and SAR-COL7 of hypomorph mouse 1 (extracted on day 3), at 10 and 20x magnification. Figure 12B shows immunofluorescence imaging of SAR-COL7 from hypomorph mouse 2 and hypomorph mouse 3 (extracted on day 7). The figure represents a 16-field boxed image obtained with a 10x lens, showing the entire skin section. Figure 13 presents H&E stained samples from hypomorph mice 1, 2 and 3 (drawn on days 3 and 3). Samples were obtained from the skin of a hypomorphic mouse without treatment and the skin of a hypomorphic mouse after intradermal delivery of HSV-GFP or SAR-COL7. Figures 14A-14B show representative electron micrograph images of human COL7 expression in the skin of a hypomorph mouse following intradermal delivery of SAR-COL7. The lamina densa is the dark band indicated in the middle of the images; black dots are the stained NC domains of human COL7I; blue arrows indicate anchoring fibril formation. Figure 14A shows electron micrograph images of the skin of an infected hypomorph mouse stained with an antibody specific for the NC2 domain of human COL7 (LH24). Figure 14B shows electron micrograph images of the skin of an infected hypomorph mouse stained with an antibody specific for the NC1 domain of human COL7 (NP185). Figures 15A-15B show the human COL7A1 genome and transcript levels observed at each injection site in the skin of a hypomorph mouse following intradermal delivery of low doses of SAR-COL7, as assessed by qPCR. Each bar represents a single sample at the indicated time. Figure 15A shows human COL7A1 transcript levels / 100 ng total RNA in the skin of a hypomorph mouse. Figure 15B shows the number of human COL7A1 DNA copies / 100 ng of total DNA in the skin of a hypomorph mouse. Figure 16 shows representative immunofluorescence images of human COL7 expression in the skin of a hypomorph mouse (from mouse 1) following intradermal delivery of low doses of SAR-COL7. Figures 17A-17C show protein and nucleic acid analyzes of human COL1A1 and COL1A2 in Vero cells infected with the indicated HSV clones encoding COL1A1 alone (inserted at ICP4 loci) or COL1A1 and COL1A2 (inserted at ICP4 loci). and ICP22, respectively). Figure 17A shows the levels of human COL1A1 transcript present in Vero cells 5 days after infection with the indicated HSV clones, as determined by qRT-PCR analysis. Data from two replicates ± SEM are presented. Figure 17B shows the levels of human COL1A2 transcript present in Vero cells 5 days after infection with the indicated HSV clones, as determined by qRT-PCR analysis. Data from two replicates ± SEM are presented. Figure 17C shows a Western blot analysis of human COL1A1 and COL1A2 protein expression in Vero cells, 5 days after infection with the indicated COL1A1 / COL1A2 positive clones, as determined by qRT-PCR. Vero cells without infection (mock) were used as a negative control. c / CLnn / Lznz / q / Yi was used GAPDH as charge control. Figure 18 shows a Western blot analysis of human COL1A1 and COL1A2 protein expression in Vero cells, 5 days after infection with an HSV isolate encoding a COL1A1-IRESCOL1A2 sequence (IRES-isolate 6) inserted into the cells. ICP4 loci. Infection with an isolate without the IRES construct (no insert) was used as a negative control. GAPDH was used as a loading control. Figures 19A-19B show protein and nucleic acid analyzes of human C0L3 in immortalized human keratinocytes (HaCaT), infected with C3vec01. Figure 19A shows the levels of human COL3A1 transcript present in immortalized human keratinocytes (HK) after infection with C3vec01 at the indicated MOIs. Uninfected (mock) and HSV-mCherry-infected (mCherry) cells were used as negative controls. Data from two replicates ± SEM are presented. Figure 19B shows representative immunofluorescence images of human C0L3 protein expression in immortalized human keratinocytes, 48 ​​hours after C3vec01 infection at the indicated MOIs. Cells without infection (mock) were used as negative controls. Figures 20A-20B show protein and nucleic acid analyzes of human C0L3 in immortalized human dermal fibroblasts (HDFs), infected with C3vec01. Figure 20A shows the levels of human COL3A1 transcript present in immortalized human dermal fibroblasts (HDF) after infection with C3vec01 at the indicated MOIs. Uninfected (mock) and HSV-mCherry-infected (mCherry) cells were used as negative controls. Data from two replicates ± SEM are presented. Figure 20B shows representative immunofluorescence images of human COL3 protein expression in immortalized human dermal fibroblasts, 48 ​​hours after infection with C3vec01 at the indicated MOIs. Cells without infection (mock) were used as negative controls. Figures 21A-21D show protein and nucleic acid analyzes of human COL3 in aged primary human fibroblasts (HDF), obtained from two different vendors, infected with C3vec01 at the indicated MOIs. Figure 21A shows the levels of human COL3A1 transcript present in primary HDFs taken from a 65-year-old patient or a 73-year-old patient (supplier 1), after infection with C3vec01 at the indicated MOIs. Cells without infection (mock) were used as a negative control. Data from two replicates ± SEM are presented. Figure 21B shows a Western blot analysis of human COL3A1 protein expression in primary HDFs taken from a 73-year-old patient (supplier 1), after infection with C3vec01 at the indicated MOIs. Cells without infection (mock) were used as a negative control. Recombinant human COL3A1 (rC0L3A1) was used as a positive control. GAPDH was used as a loading control. Figure 21C shows the levels of human COL3A1 transcript present in primary HDFs taken from a 75-year-old patient or a 73-year-old patient (supplier 2), after infection with C3vec01 at the indicated MOIs. Cells without infection (mock) were used as a negative control. Data from two replicates ± SEM are presented. Figure 21D shows a Western blot analysis of human COL3A1 protein expression in primary HDFs taken from a 75-year-old female patient (supplier 2), after infection with C3vec01 at the indicated MOIs. Cells without infection (mock) were used as a negative control. Recombinant human COL3A1 (rC0L3A1) was used as a positive control. GAPDH was used as a loading control. Figures 22A-22B show protein and nucleic acid analyzes of human C0L3 in immortalized human c / CLnn / Lznz / q / Yi dermal fibroblasts (HDF), following UV exposure. Figure 22A shows the concentration of C0L3 secreted in the supernatant of cultured HDFs, 24 hours after exposure to various doses and durations of UV light, as assessed by an ELISA. Supernatant collected from HDF without UV exposure (-UV), grown in parallel, was used as a control. Figure 22B shows the levels of human COL3A1 transcript present in UV-exposed immortalized human dermal fibroblasts (HDFs) after infection with C3vec01 at the indicated MOIs. Uninfected (mock) and HSV-mCherry-infected (mCherry) cells were used as negative controls. Data from two replicates ± SEM are presented. Figures 23A-23C show protein and nucleic acid analyzes of C0L3 from skin biopsies taken from young (6 to 8 weeks old) and older (~13 months old) C57BL / 6 mice treated with C3vec01 or control, 48 hours. after intradermal application. Figure 23A shows the levels of human COL3A1 DNA present in skin biopsies taken from young and old mice, 48 hours after intradermal administration of C3vec01 or vehicle control, as assessed by qPCR analysis. Figure 23B shows the levels of human COL3A1 transcript present in skin biopsies taken from young and old mice, 48 hours after intradermal administration of C3vec01 or vehicle control, as assessed by qRT-PCR analysis. For each condition in the qPCR and qRT-PCR analysis, data are presented as the average of four tissue samples (two replicates / tissue sample) ± SEM. Figure 23C shows representative immunofluorescence images of human COL3 expression in skin biopsies taken from young and old mice, 48 hours after intradermal administration of C3vec01. A young mouse receiving intradermal administration of vehicle alone was used as a negative control. DAPI staining was used to visualize the nuclei. Figures 24A-24B show expression of wild-type (WT) human LamB3 in Vero cells infected with the indicated viral isolates. Figure 24A shows the expression of wild-type human LAMB3 in infected Vero cells, as assessed by qPCR analysis. Figure 24B shows the expression of wild-type human LamB3 protein in infected Vero cells, as assessed by Western blotting. Figure 25 shows the expression of codon-optimized (CO) or wild-type (WT) human LamB3 protein in Vero cells infected with the indicated viral isolates, as assessed by Western blotting. Vero cells without infection were used as a negative control. Figure 26 shows codon-optimized (CO) or wild-type (WT) human LamB3 protein expression in primary human keratinocytes infected with the indicated viral isolates, as assessed by Western blotting. Primary keratinocytes without infection were used as a negative control. Figures 27A-27C show expression of wild-type (WT) and codon-optimized (CO) human LamC2 in Vero cells infected with the indicated viral isolates. Figure 27A shows the expression of wild-type human LAMC2 in infected Vero cells, as assessed by qPCR analysis. Figure 27B shows codon-optimized human LAMC2 expression in infected Vero cells, as assessed by qPCR analysis. Figure 27C shows the expression of wild-type and codon-optimized human LamC2 protein in infected Vero cells, as assessed by Western blotting. The boxed 'LGA' viral isolate, expressing LamC2 with codon optimization, was selected for further experiments. c / CLnn / Lznz / q / Yi Figures 28A-28C show human LAMC2 expressed in the "LGA" viral isolate in immortalized primary human keratinocytes, infected at the indicated multiplicities of infection (MOI). Figure 28A shows the number of viral genome copies in primary immortalized human keratinocytes after infection with the "LGA" viral isolate at the indicated MOIs. Figure 28B shows the codon-optimized LAMC2 transcript level in primary immortalized human keratinocytes following infection with the "LGA" viral isolate at the indicated MOIs. Figure 28C shows the expression of human LamC2 protein in primary immortalized human keratinocytes following infection with the "LGA" viral isolate at the indicated MOIs, as assessed by Western blotting. Figures 29A-29D show protein and nucleic acid analysis of LAMC2 from skin biopsies taken from mice treated with the HSV isolate "LGA" or control (vehicle), 72 hours after intradermal application. Figure 29A shows a schematic of the intradermal injection sites in the treated animals. Figure 29B shows the levels of human LAMC2 DNA present in skin biopsies taken from mice, 72 hours after intradermal administration of the HSV LGA isolate or vehicle control, as assessed by qPCR analysis. Figure 29C shows the levels of human LAMC2 transcript present in skin biopsies taken from mice, 72 hours after intradermal administration of the HSV LGA isolate or vehicle control, as assessed by qRT-PCR analysis. In each condition in the qPCR and qRT-PCR analysis, data are presented as the average of two replicates ± SEM. Figure 29D shows representative immunofluorescence images of human LAMC2 expression in skin biopsies taken from mice, 72 hours after intradermal administration of the HSV LGA isolate. A spot that received intradermal administration of vehicle alone was used as a negative control. DAPI staining was used to visualize the nuclei. pKal staining was used to visualize mouse laminin-332. DETAILED DESCRIPTION In some embodiments, the present disclosure refers to recombinant nucleic acids (eg, recombinant herpes virus genomes) encoding one or more cosmetic proteins, as well as uses of these recombinant nucleic acids in viruses (eg, in a virus herpes), compositions, formulations, medicaments, and / or methods for delivering one or more cosmetic proteins to the skin, such as on, into, and / or through the skin (eg, in dermal ECM). In some embodiments, the present disclosure refers to recombinant nucleic acids (eg, recombinant herpes virus genomes) encoding one or more cosmetic proteins, as well as uses of these recombinant nucleic acids in viruses (eg, in a virus herpes), compositions, formulations, medicaments and / or methods for augmenting, augmenting and / or supplementing one or more dermal ECM proteins (eg, one or more collagen proteins). In some embodiments, the present disclosure refers to recombinant nucleic acids (eg, recombinant herpes virus genomes) encoding one or more cosmetic proteins, as well as uses of these recombinant nucleic acids in viruses (eg, in a virus herpes), compositions, formulations, medicaments and / or methods in the aesthetic field (for example, to reduce one or more dermatological signs of aging). In some embodiments, the present disclosure refers to compositions comprising a recombinant herpes virus vector and c / CLnn / Lznz / q / Yi methods comprising delivery of the recombinant herpes virus vector onto, into, and / or through the skin of a mammal, wherein the recombinant herpes viral vector comprises a promoter that can be used in a mammalian cell and a heterologous nucleic acid that is expressed to achieve a cosmetic effect on the skin of the mammal. The heterologous nucleic acid can be delivered to a target skin cell of a mammal, which comprises contacting the epidermis, dermis, or a subcutaneous tissue of the mammal with the composition comprising the recombinant herpes virus vector, in conditions in which the recombinant herpes virus vector is transported to the surface, into and / or through the epidermis, dermis or subcutaneous tissue and introduced into the target skin cell, for expression. Without wishing to be bound by theory, it is believed that administration of one or more viruses, formulations, and / or recombinant nucleic acids described herein to an individual would allow increased production of functional dermal ECM proteins (eg, human collagen ) in the individual. Also, without wishing to be bound by theory, it is believed that cosmetic protein levels are increased, increased, and / or supplemented in an individual through the administration of one or more of the viruses, formulations, and / or acids recombinant nucleica described herein lead to at least one of: 1) soft tissue enhancement, augmentation, and / or complementation; 2) improvement of the quality, condition and / or appearance of the skin; 3) the reduction of one or more superficial depressions in the skin (eg, wrinkles); 4) improving the texture, smoothness, elasticity and / or tightness of the skin; and / or 5) the reduction of one or more dermatological signs of aging. Ultimately and without wishing to be bound by theory, it is believed that the viruses, compositions, recombinant nucleic acids and methods described herein provide a novel strategy for the delivery of functional cosmetic proteins in aesthetic settings. The description below presents examples of methods, parameters and the like. However, it should be recognized that this is not intended as a limitation of the scope of the present description, but rather is provided as a description of exemplary embodiments. I. General techniques The techniques and procedures described or outlined herein are generally understood and commonly used in conventional methodology by those skilled in the art, such as the widely used methodologies described in Sambrook et al., Molecular Cloning : A Laboratory Manual 3rd Edition (2001) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.; Current Protocol In Molecular Biology (F.M. Ausubel, et al. eds., (2003)); the Methods In Enzymology series (Academic Press, Inc.): PCR 2: A Practica! Approach (M.J. MacPherson, B.D. Hames and G.R. Taylor eds. (1995)), Harlow and Lane, eds. (1988); Oligonucleotide Synthesis (M.J. Gait, ed., 1984); Methods in Molecular Biology, Humana Press; Cell Biology: A Laboratory Notebook (J.E. Cellis, ed., 1998) Academic Press; Animal Cell Culture (R.l. Freshney), ed., 1987); Introduction to Cell and Tissue Culture (J.P. Mather and P.E. Roberts, 1998) Plenum Press; Cell and Tissue Culture: Laboratory Procedures (A. Doyle, J.B. Griffiths, and D.G. Newell, eds., 1993-8) J. Wiley & Sons; Gene Transfer Vectors for Mammalian Cells (J.M. Miller and M.P. Calos, eds., 1987); PCR: The Polymerase Chain Reaction, (Mullis et al., eds., 1994); Short Protocols in Molecular Biology (Wiley & Sons, 1999). II. Definitions Before describing in detail the described modalities, it should be understood that the present description is not limited to particular compositions or biological systems which, of course, can vary. It should also be understood that the terminology used herein is solely for the purpose of describing particular embodiments and is not intended to be exhaustive. As used herein, the singular forms "a / an" and "the" include plural referents, unless the context clearly indicates otherwise. Thus, for example, reference to "a molecule" optionally includes a combination of two or more such molecules and the like. As used herein, the term "and / or" may include any and all of one or more of the associated listed items. For example, the term "a and / or b" may refer to "a only", "b only", "a or b" or "a and b"; the term "a, b and / or c" can refer to "only a", "only b", "only c", "a or b", "a or c", "b or c", "a, b or c", "a and b", "a and c", "b and c" or "a, b and c", etc. As used herein, the term "about" refers to the usual error range for the respective value that is readily known to one skilled in the art. A reference to "about" a value or parameter herein includes (and describes) modalities directed to that value or parameter itself. Aspects and modalities in this description are understood to include "comprising / consisting", "consisting / consisting" and "consisting / essentially of" aspects and modalities. As used herein, the terms "polynucleotide", "nucleic acid sequence", "nucleic acid" and variations thereof are to be construed as generic to polydeoxyribonucleotides (with 2-deoxy-D-ribose), polyribonucleotides (with D -ribose), any other type of polynucleotide that is an N-glycoside of a purine or pyrimidine base, and of other polymers containing non-nucleotide backbones, provided that the polymers contain nucleobases in a configuration that allows for base pairing and stacking of bases, as found in DNA and RNA. Thus, these terms include known types of nucleic acid modifications, eg, substitution of one or more natural nucleotides with an analogue, and internucleotide modifications. As used herein, a nucleic acid is "operably linked" when it is placed into a functional relationship with another nucleic acid sequence. For example, a promoter or enhancer is operably linked to a coding sequence if it affects transcription of the sequence, or a ribosome binding site is operably linked to a coding sequence if it is positioned so that facilitate translation. In general, "operably linked" or "operably linked" means that the linked DNA sequences are contiguous. As used herein, the term "vector" refers to separate elements that are used to introduce heterologous nucleic acids into cells for expression or replication. An expression vector includes vectors capable of expressing nucleic acids operably linked to regulatory sequences, such as promoter regions, capable of achieving expression of said nucleic acids. Thus, an expression vector can refer to a DNA or RNA construct, such as a plasmid, phage, recombinant virus, or other vector that, when introduced into a suitable host cell, causes expression of the nucleic acids. Suitable expression vectors are known to those skilled in the art and include those that can replicate in eukaryotic cells, c / CLnn / Lznz / q / Yi as well as those that remain in the episome or integrate into the cell's genome. hostess. As used herein, an "open reading frame" or "ORF" refers to a continuous stretch of nucleic acids, either DNA or RNA, that encode a protein or polypeptide. In general, nucleic acids comprise a start codon or translation start signal, such as ATG or AUG, and a stop codon. As used herein, a "non-translational region" or "UTR" refers to non-translational nucleic acids at the 5' and / or 3' ends of an open reading frame. Inclusion of one or more UTRs in a polynucleotide may affect post-translational regulation, mRNA stability, and / or translation of the polynucleotide. As used herein, the term "transgene" refers to a polynucleotide capable of RNA transcription and translation and / or expression under suitable conditions upon introduction into a cell. In some aspects, it imparts a desired property to a cell into which it is introduced or otherwise leads to a desired cosmetic, therapeutic, or diagnostic result. As used herein, the terms "polypeptide", "protein" and "peptide" are used interchangeably and can refer to a polymer of two or more amino acids. As used herein, a "subject," "host," or "individual" refers to any animal classified as a mammal, including humans, domestic and farm animals, as well as zoo animals, sport animals, or pets, such as dogs, horses, cats, cows, as well as animals used in research, such as mice, rats, hamsters, rabbits and non-human primates, etc. In some embodiments, the mammal is human. As used herein, the terms "pharmaceutical formulation" or "pharmaceutical composition" refer to a preparation in such a way as to allow the efficacy of the biological activity of the active ingredient(s) and that it does not contain additional components with unacceptable toxicity. for a subject to whom the composition or formulation would be administered. "Pharmaceutically acceptable" excipients (eg, carriers, additives) are those that can reasonably be administered to a subject to provide an effective dose of the active ingredient(s) used. As used herein, "dermal administration" or "dermal administration" refers to the delivery of a composition to a subject through contact, direct or otherwise, of a formulation comprising the composition with the whole (" systemic") or a part ("topical") of a subject's skin. The term encompasses various routes of administration including, but not limited to, topical and transdermal. Topical administration can be used as a means of delivering a composition to the epidermis or dermis of a subject or to a specific layer thereof. As used herein, "treatment" refers to a clinical intervention designed to alter the natural course of the individual or cell under treatment during the course of clinical pathology. Desirable effects of treatment include slowing of the disease / disorder / defect progression, improvement or alleviation of the disease / disorder / defect status, and remission or improvement of prognosis. For example, an individual is considered "treated" successfully if one or more symptoms associated with dermatologic aging are reduced, mitigated, or eliminated, including the reduction or elimination of wrinkles. c / CLnn / Lznz / q / Yi As used herein, the term "delaying the progression of" a disease / disorder / defect refers to the postponement, hindering, slowing down, stabilization, and / or delaying the development of the disease / disorder / defect. the defect (for example, wrinkles in the skin). This delay may be of variable length or duration, depending on the history of the disease / disorder / defect and / or the individual being treated. As is apparent to those skilled in the art, a sufficient or significant delay may indeed encompass prevention, given that the individual does not develop the disease / disorder / defect. III. recombinant nucleic acids Certain aspects of this disclosure refer to recombinant nucleic acids (eg, isolated recombinant nucleic acids) comprising one or more polynucleotides (eg, one or more, two or more, three or more, four or more, five or more , ten or more, etc.) that code for a cosmetic protein. The polynucleotides of the present disclosure may encode any suitable cosmetic protein described herein or known in the art, including, for example, collagen proteins, fibronectins, elastins, lumicans, vitronectins / vitronectin receptors, laminins, neuromodulators, fibrillins, others. dermal ECM proteins, etc. In some embodiments, the cosmetic protein is a structural extracellular matrix protein (eg, collagen, elastin, fibronectin, laminin, fibrillin, etc.). In some embodiments, the cosmetic protein is a collagen, elastin, fibronectin, or laminin (eg, human collagen, elastin, fibronectin, or laminin). In some embodiments, the present disclosure refers to recombinant nucleic acids (eg, isolated recombinant nucleic acids) that comprise one or more polynucleotides (eg, one or more, two or more, three or more, four or more, five or more, ten or more, etc.) that code for a collagen protein. In some embodiments, the collagen protein is a human collagen protein. In some embodiments, the present disclosure relates to recombinant nucleic acids comprising one or more polynucleotides encoding a homotrimeric collagen (eg, a homotrimeric human collagen, such as human collagen 3 (eg, with three COL3A1 (COL3) polypeptides). ) or human collagen 7 (eg, with three COL7A1 (COL7) polypeptides).In some embodiments, the present disclosure refers to recombinant nucleic acids comprising one or more polynucleotides encoding a heterotrimeric collagen (eg, a heterotrimeric human, such as human collagen 1 (eg, with two COL1A1 (COL1-1) polypeptides and one COL1A2 (COL1-2) polypeptide) or human collagen 4 (eg, with two COL4A1 (COL4-1) polypeptides ) and a COL4A2 (COL4-2) polypeptide). homotrimeric collagen and heterotrimeric collagen (eg, a recombinant nucleic acid comprising one or more polynucleotides encoding a human collagen 1 and a human collagen 3). In some embodiments, the present disclosure refers to recombinant nucleic acids comprising one or more polynucleotides encoding human collagen 1. In some embodiments, the present disclosure refers to recombinant nucleic acids comprising one or more polynucleotides encoding human collagen 3. In some embodiments, the present disclosure relates to recombinant nucleic acids comprising a c / CLnn / Lznz / q / Yi first polynucleotide encoding a first polypeptide comprising a first cosmetic protein (eg, a first human collagen protein). In some embodiments, the first polypeptide consists essentially of or consists of the first cosmetic protein (eg, it consists essentially of or consists of a first human collagen protein). In some embodiments, the present disclosure refers to recombinant nucleic acids comprising a first polynucleotide encoding a first polypeptide comprising a first cosmetic protein (eg, a first human collagen protein), a linker polypeptide, and another cosmetic protein (eg, a first human collagen protein). example, another human collagen protein). In some embodiments, the first cosmetic protein and the other cosmetic protein (eg, the first human collagen protein and the other human collagen protein) are the same. In some embodiments, the first cosmetic protein and the other cosmetic protein (eg, the first human collagen protein and the other human collagen protein) are different. In some embodiments, the linker polypeptide is a cleavable linker polypeptide. In some embodiments, the present disclosure refers to recombinant nucleic acids comprising a first polynucleotide encoding a first polypeptide comprising a first cosmetic protein (eg, a first human collagen protein), where the first polynucleotide encodes a polycistronic mRNA that It comprises: a first open reading frame (ORE) encoding the first polypeptide, an intraribosome entry site (IRES), and a second ORF encoding an additional cosmetic protein (eg, an additional human collagen protein). In some embodiments, the first cosmetic protein and the additional cosmetic protein (eg, the first human collagen protein and the additional human collagen protein) are the same. In some embodiments, the first cosmetic protein and the additional cosmetic protein (eg, the first human collagen protein and the additional human collagen protein) are different. In some embodiments, the present disclosure refers to recombinant nucleic acids comprising a first polynucleotide encoding a first polypeptide comprising a first cosmetic protein (eg, a first human collagen protein) and a second polynucleotide encoding a second cosmetic protein. (eg a second human collagen protein). In some embodiments, the first cosmetic protein and the second cosmetic protein (eg, the first human collagen protein and the second human collagen protein) are the same. In some embodiments, the first cosmetic protein and the second cosmetic protein (eg, the first human collagen protein and the second human collagen protein) are different. In some embodiments, the recombinant nucleic acid is a vector. In some embodiments, the recombinant nucleic acid is a viral vector. In some embodiments, the recombinant nucleic acid is a herpes viral vector. In some embodiments, the recombinant nucleic acid is a herpes simplex virus amplicon. In some embodiments, the recombinant nucleic acid is a recombinant herpes virus genome. In some embodiments, the recombinant nucleic acid is a recombinant herpes simplex virus genome. In some embodiments, the recombinant herpes simplex virus genome is a recombinant herpes simplex virus type 1 (HSV1) genome. Polynucleotides Encoding Cosmetic Proteins Polynucleotides Encoding Collagen Proteins c / CLnn / Lznz / q / Yi In some embodiments, the present disclosure refers to a recombinant nucleic acid comprising one or more polynucleotides comprising the coding sequence for a collagen gene. The coding sequence of any collagen gene (including any of its isoforms) from any suitable species known in the art may be encoded by a polynucleotide of the present disclosure, including, for example, human collagen genes (see, for example, NCBI gene IDs: 1277, 1278, 1281, 1282, 1284, 1291, 1294, 1308, etc.), mouse collagen genes (see, for example, NCBI gene IDs: 12842, 12843, 12825, 12826, 12827, 12833, 12836, 12821, etc.), chimpanzee collagen genes (see, for example, NCBI gene IDs: 104001053, 455117, 459815, 452689, 452661, 450204, 1010510619, etc. .), rat collagen genes (see, for example, NCBI gene IDs: 29393, 84352, 84032, 290905, 306628, 294337, 301012, 294027, etc.), rabbit collagen genes (see, for example, , NCBI Gene IDs: 100347598, 100008997, 100009177, 100358256, 100358522, 100343947, 100356561, 100339335, etc.), etc. Methods for identifying orthologs / homologs of collagen genes in additional species are known in the art and include, for example, the use of a nucleic acid sequence alignment program such as BLAST® software. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity to the sequence of any of the collagen genes (and / or their coding sequences) described herein or known in the art. In some embodiments, a polynucleotide of the present disclosure comprises a codon-optimized variant of the coding sequence of any of the collagen genes described herein or known in the art. In some embodiments, the use of a codon-optimized variant of the coding sequence of a collagen gene increases the stability and / or yield of heterologous expression (RNA and / or protein) of the encoded collagen protein in a collagen gene. target cell (such as a cell of the epidermis and / or dermis), compared to the stability and / or yield of heterologous expression of a wild-type sequence, without codon optimization. Any suitable method known in the art can be used to perform codon optimization of a sequence for expression in one or more target cells (eg, one or more human cells), for example, through the methods described by Fath et al., (PLoS One. 2011 Mar 3;6(3):e17596). In some embodiments, the present disclosure refers to one or more polynucleotides (ie, one or more first polynucleotides and / or one or more second polynucleotides) that comprise the coding sequence of a human collagen gene. A nucleic acid of the present disclosure may encode any suitable human collagen gene (including any isoform thereof) known in the art, including, for example, a COL1A1 gene (see, for example, NCBI Gene ID: 1277). , SEQ. ID. NO.: 1), a COL1A2 a gene (see, for example, NCBI Gene ID: 1278, SEQ. ID. NO.: 3), a COL2A1 a gene (see, for example, NCBI gene ID: 1280), a COL3A1 a gene (see, for example, NCBI gene ID: 1281, SEQ. ID. NO.: 5), a COL4A1 a gene (see, eg, NCBI Gene ID: 1282, SEQ ID NO: 7), a COL4A2 a gene (see, eg, NCBI Gene ID: 1284), a c / CLnn / Lznz / q / Yi COL4A3 a gene (see, for example, NCBI gene ID: 1285), a COL4A4 a gene (see, for example, NCBI gene ID: 1286), a COL4A5 a gene (see, for example, example, NCBI Gene ID: 1287), a COL4A6 a gene (see, for example, NCBI Gene ID: 1288), a COL5A1 a gene (see, for example, NCBI Gene ID : 1289), a COL5A2 a gene (see, for example, NCBI Gene ID: 1290), a COL5A3 a gene (see, for example, NCBI Gene ID: 50509), a COL6A1 a gene ( see, eg, NCBI Gene ID: 1291, SEQ. ID. NO.: 9), a COL6A2 a gene (see, for example, NCBI gene ID: 1292), a COL6A3 a gene (see, for example, NCBI gene ID: 1293), a COL6A4 gene a (see, for example, NCBI gene ID: 344875), a COL6A5 a gene (see, for example, NCBI gene ID: 256076), a COL6A6 a gene (see, for example, NCBI gene ID in NCBI: 131873), a COL7A1 a gene (see, for example, NCBI Gene ID: 1294, SEQ. ID. NO.: 10), a COL8A1 a gene (see, for example, Gene ID at NCBI: 1295), a COL9A1 a gene (see, for example, NCBI Gene ID: 1297), a COL9A2 a gene (see, for example, NCBI Gene ID: 1298), a COL9A3 gene a (see, for example, NCBI gene ID: 1299), a COL10A1 a gene (see, for example, NCBI gene ID: 1300), a COL11A1 a gene (see, for example, NCBI gene ID at NCBI: 1301), a COL11A2 a gene (see, for example, NCBI Gene ID: 1302), a COL12A1 a gene (see, for example, NCBI Gene ID: 1303), a COL13A1 gene to (see, for example or, NCBI Gene ID: 1305), a COL14A1 a gene (see, for example, NCBI Gene ID: 7373), a COL15A1 a gene (see, for example, NCBI Gene ID: 1306) , a COL16A1 a gene (see, for example, NCBI Gene ID: 1307), a COL17A1 a gene (see, for example, NCBI Gene ID: 1308, SEQ. ID. NO.: 12), a COL18A1 a gene (see, for example, NCBI gene ID: 80781), a COL19A1 a gene (see, for example, NCBI gene ID: 1310), a COL20A1 gene a (see, for example, NCBI gene ID: 57642), a COL21A1 a gene (see, for example, NCBI gene ID: 81578), a COL22A1 a gene (see, for example, NCBI gene ID at NCBI: 169044), a COL23A1 a gene (see, for example, NCBI Gene ID: 91522), a COL24A1 a gene (see, for example, NCBI Gene ID: 255631), a COL25A1 gene a (see, for example, NCBI gene ID: 84570), a COL26A1 a gene (see, for example, NCBI gene ID: 136227), a COL27A1 a gene (see, for example, NCBI gene ID in NCBI: 85301), a COL28A1 gene (see, for example, NCBI gene ID: 340267), etc. In some embodiments, a polynucleotide (ie, one or more first polynucleotides and / or one or more second polynucleotides) of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86 %, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96 %, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the sequence of any of the human collagen genes (and / or their coding sequences) described herein or known elsewhere The technique. In some embodiments, a polynucleotide (ie, one or more first polynucleotides and / or one or more second polynucleotides) of the present disclosure comprises a codon-optimized variant of any of the human collagen genes described herein. In some embodiments, the use of a codon-optimized variant of a human collagen gene increases the stability and / or yield of heterologous expression (RNA and / or protein) of human collagen in a target cell (such as a fibroblast or human keratinocyte), compared to the stability and / or yield of heterologous expression of a wild-type sequence, without codon optimization. c / CLnn / Lznz / q / YL In some embodiments, a polynucleotide of the present disclosure comprises the coding sequence of the human COL1A1 gene (or a codon-optimized variant thereof). In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity with the sequence of SEQ. ID. NO.: 1 or SEQ. ID. NO.: 2. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of SEQ. ID. NO.: 1 or SEQ. ID. NO.: 2. In some embodiments, a polynucleotide of the present disclosure comprises a 5' truncation, a 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 1 or SEQ. ID. NO.: 2. In some embodiments, the 5' truncation, the 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 1 or SEQ. ID. NO.: 2 is a polynucleotide with at least 25, at least 50, at least 75, at least 100, at least 125, at least 150, at least 175, at least 200, at least 250, at least 300, or at least 350, at least 400, at least 450, at least 500, at least 750, at least 1000, at least 1250, at least 1500, at least 1750, at least 2000, at least 2500, at least 3000, at least 3500, at least 4000, but less than 4395 consecutive nucleotides of SEQ. ID. NO.: 1 or SEQ. ID. NO.: 2. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least least 99% or 100% sequence identity to the sequence of nucleic acids 1-4392 of SEQ. ID. NO.: 1 or SEQ. ID. NO.: 2. In some embodiments, a polynucleotide of the present disclosure comprises the nucleic acid sequence 1-4392 of SEQ. ID. NO.: 1 or SEQ. ID. NO.: 2. In some embodiments, a polynucleotide of the present disclosure comprises the coding sequence of the human COL1A2 gene (or a codon-optimized variant thereof). In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity with the sequence of SEQ. ID. NO.: 3 or SEQ. ID. NO.: 4. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of SEQ. ID. NO.: 3 or SEQ. ID. NO.: 4. In some embodiments, a polynucleotide of the present disclosure comprises a 5' truncation, a 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 3 or SEQ. ID. NO.: 4. In some embodiments, the 5' truncation, the 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 3 or SEQ. ID. NO.: 4 is a polynucleotide with at least 25, at least 50, at least 75, at least 100, at least 125, at least 150, at least 175, at least 200, at least 250, at least 300, or at least 350, at least 400, at least 450, at least 500, at least 750, at least 1000, at least 1250, at least 1500, at least 1750, at least 2000, at least 2500, at least 3000, at least 3500, at least 4000, but less than 4101 consecutive nucleotides of SEQ. ID. NO.: 3 or SEQ. ID. NO.: 4. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at at least 89%, at least 90%, at least 91%, at c / c i nn / ι znz / zi / Yl minus 92%, at least 93%, at least 94%, at least 95%, at least 96% , at least 97%, at least 98%, at least 99% or 100% sequence identity with the sequence of nucleic acids 1-4098 of SEQ. ID. NO.: 3 or SEQ. ID. NO.: 4. In some embodiments, a polynucleotide of the present disclosure comprises the nucleic acid sequence 1-4098 of SEQ. ID. NO.: 3 or SEQ. ID. NO.: 4. In some embodiments, a polynucleotide of the present disclosure comprises the coding sequence of the human COL3A1 gene (or a codon-optimized variant thereof). In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity with the sequence of SEQ. ID. NO.: 5 or SEQ. ID. NO.: 6. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of SEQ. ID. NO.: 5 or SEQ. ID. NO 6. In some embodiments, a polynucleotide of the present disclosure comprises a 5' truncation, a 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 5 or SEQ. ID. NO.: 6. In some embodiments, the 5' truncation, the 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 5 or SEQ. ID. NO.: 6 is a polynucleotide with at least 25, at least 50, at least 75, at least 100, at least 125, at least 150, at least 175, at least 200, at least 250, at least 300, or at least 350, at least 400, at least 450, at least 500, at least 750, at least 1000, at least 1250, at least 1500, at least 1750, at least 2000, at least 2500, at least 3000, at least 3500, at least 4000, but less than 4401 consecutive nucleotides of SEQ. ID. NO.: 5 or SEQ. ID. NO.: 6. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least least 99% or 100% sequence identity to the sequence of nucleic acids 1-4398 of SEQ. ID. NO.: 5 or SEQ. ID. NO.: 6. In some embodiments, a polynucleotide of the present disclosure comprises the nucleic acid sequence 1-4398 of SEQ. ID. NO.: 5 or SEQ. ID. NO 6. In some embodiments, a polynucleotide of the present disclosure comprises the coding sequence of the human COL4A1 gene (or a codon-optimized variant thereof). In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity with the sequence of SEQ. ID. NO.: 7 or SEQ. ID. NO.: 8. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of SEQ. ID. NO.: 7 or SEQ. ID. NO.: 8. In some embodiments, a polynucleotide of the present disclosure comprises a 5' truncation, a 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 7 or SEQ. ID. NO.: 8. In some embodiments, the 5' truncation, the 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 7 or SEQ. ID. NO.: 8 is a polynucleotide with at least 25, at least 50, at least 75, at least 100, at least 125, at least 150, at least 175, at least 200, at least 250, at least 300, or at least 350, at least 400, at least 450, at least 500, at least 750, at least 1000, al c / CLnn / Lznz / q / Yi minus 1250, at least 1500, at least 1750, at least 2000, at least 2500 , at least 3000, at least 3500, at least 4000, at least 4500, at least 5000 but less than 5010 consecutive nucleotides of SEQ. ID. NO.: 7 or SEQ. ID. NO.: 8. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least least 99% or 100% sequence identity to the sequence of nucleic acids 1-5007 of SEQ. ID. NO.: 7 or SEQ. ID. NO.: 8. In some embodiments, a polynucleotide of the present disclosure comprises the nucleic acid sequence 1-5007 of SEQ. ID. NO.: 7 or SEQ. ID. NO.: 8. In some embodiments, a polynucleotide of the present disclosure comprises the coding sequence of the human COL6A1 gene (or a codon-optimized variant thereof). In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity with the sequence of SEQ. ID. NO.: 9 or SEQ. ID. NO.: 10. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of SEQ. ID. NO.: 9 or SEQ. ID. NO.: 10. In some embodiments, a polynucleotide of the present disclosure comprises a 5' truncation, a 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 9 or SEQ. ID. NO.: 10. In some embodiments, the 5' truncation, the 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 9 or SEQ. ID. NO.: 10 is a polynucleotide with at least 25, at least 50, at least 75, at least 100, at least 125, at least 150, at least 175, at least 200, at least 250, at least 300, or at least 350, at least 400, at least 450, at least 500, at least 750, at least 1000, at least 1250, at least 1500, at least 1750, at least 2000, at least 2500, at least 3000, but less than 3087 consecutive nucleotides of SEQ. ID. NO.: 9 or SEQ. ID. NO.: 10. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least least 99% or 100% sequence identity to the sequence of nucleic acids 1-3084 of SEQ. ID. NO.: 9 or SEQ. ID. NO.: 10. In some embodiments, a polynucleotide of the present disclosure comprises the nucleic acid sequence 1-3084 of SEQ. ID. NO.: 9 or SEQ. ID. NO.: 10. In some embodiments, a polynucleotide of the present disclosure comprises the coding sequence of the human COL7A1 gene (or a codon-optimized variant thereof). In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity with the sequence of SEQ. ID. NO.: 11 or SEQ. ID. NO.: 12. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of SEQ. ID. NO.: 11 or SEQ. ID. NO.: 12. In some embodiments, a polynucleotide of the present disclosure comprises a 5' truncation, a 3' truncation c / CLnn / Lznz / q / Yi or a fragment of the sequence of SEQ. ID. NO.: 11 or SEQ. ID. NO.: 12. In some embodiments, the 5' truncation, the 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 11 or SEQ. ID. NO.: 12 is a polynucleotide with at least 25, at least 50, at least 75, at least 100, at least 125, at least 150, at least 175, at least 200, at least 250, at least 300, or at least 350, at least 400, at least 450, at least 500, at least 750, at least 1000, at least 1250, at least 1500, at least 1750, at least 2000, at least 2500, at least 3000, at least 3500, at least 4000, at least 4500, at least 5000, at least 5500, at least 6000, at least 6500, at least 7000, at least 7500, at least 8000, at least 8500, but less than 8835 consecutive nucleotides of SEQ. ID. NO.: 11 or SEQ. ID. NO.: 12. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least least 99% or 100% sequence identity to the sequence of nucleic acids 1-8832 of SEQ. ID. NO.: 11 or SEQ. ID. NO.: 12. In some embodiments, a polynucleotide of the present disclosure comprises the nucleic acid sequence 1-8832 of SEQ. ID. NO.: 11 or SEQ. ID. NO.: 12. In some embodiments, a polynucleotide of the present disclosure comprises the coding sequence of the human COL17A1 gene (or a codon-optimized variant thereof). In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity with the sequence of SEQ. ID. NO.: 13 or SEQ. ID. NO.: 14. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of SEQ. ID. NO.: 13 or SEQ. ID. NO.: 14. In some embodiments, a polynucleotide of the present disclosure comprises a 5' truncation, a 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 13 or SEQ. ID. NO.: 14. In some embodiments, the 5' truncation, the 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 13 or SEQ. ID. NO.: 14 is a polynucleotide with at least 25, at least 50, at least 75, at least 100, at least 125, at least 150, at least 175, at least 200, at least 250, at least 300, or at least 350, at least 400, at least 450, at least 500, at least 750, at least 1000, at least 1250, at least 1500, at least 1750, at least 2000, at least 2500, at least 3000, at least 3500, at least 4000, but less than 4494 consecutive nucleotides of SEQ. ID. NO.: 13 or SEQ. ID. NO.: 14. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least least 99% or 100% sequence identity to the sequence of nucleic acids 1-4491 of SEQ. ID. NO.: 13 or SEQ. ID. NO.: 14. In some embodiments, a polynucleotide of the present disclosure comprises the nucleic acid sequence 1-4491 of SEQ. ID. NO.: 13 or SEQ. ID. NO.: 14. In some embodiments, a polynucleotide of the present disclosure that encodes one or more human collagen proteins (for example, a first human collagen protein, another human collagen protein, a further human collagen protein, and / or a second human collagen protein). human) has at least 80%, at least 85%, c / CLnn / Lznz / q / Yi at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a nucleic acid sequence selected from SEQ. ID. NO.: 1-14. In some embodiments, a polynucleotide of the present disclosure that encodes one or more human collagen proteins (for example, a first human collagen protein, another human collagen protein, a further human collagen protein, and / or a second human collagen protein). human) comprises a sequence selected from SEQ. ID. NO.: 1-14. Polynucleotides Encoding Fibronectin Proteins In some embodiments, the present disclosure refers to a recombinant nucleic acid comprising one or more polynucleotides comprising the coding sequence for a fibronectin gene. The coding sequence of any fibronectin gene (including any of its isoforms) from any suitable species known in the art may be encoded by a polynucleotide of the present disclosure, including, for example, a human fibronectin gene (see , for example, NCBI gene ID: 2335), a mouse fibronectin gene (see, for example, NCBI gene ID: 14268), a chimpanzee fibronectin gene (see, for example, NCBI gene ID: NCBI: 459926), a rat fibronectin gene (see, for example, NCBI Gene ID: 25661), a rabbit fibronectin gene (see, for example, NCBI Gene ID: 100328589), etc. Methods for identifying orthologs / homologs of fibronectin genes in additional species are known to those skilled in the art. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity to the sequence of any of the fibronectin genes (and / or their coding sequences) described herein or known in the art. In some embodiments, a polynucleotide of the present disclosure comprises a codon-optimized variant of any of the fibronectin genes (and / or their coding sequences) described herein or known in the art. In some embodiments, the present disclosure refers to one or more polynucleotides (ie, one or more first polynucleotides and / or one or more second polynucleotides) that comprise the coding sequence of a human fibronectin gene. In some embodiments, a polynucleotide of the present disclosure comprises the coding sequence of the human FN1 gene (or a codon-optimized variant thereof). In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity with the sequence of SEQ. ID. NO.: 35 or SEQ. ID. NO.: 36. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of SEQ. ID. NO.: 35 or SEQ. ID. NO.: 36. In some embodiments, a polynucleotide of the present disclosure comprises a 5' truncation, a 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 35 or SEQ. ID. NO.: 36. In some embodiments, the 5' truncation, the 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 35 or SEQ. ID. NO.: 36 is a c / CLnn / Lznz / q / Yi polynucleotide with at least 25, at least 50, at least 75, at least 100, at least 125, at least 150, at least 175, at least 200, at least at least 250, at least 300 or at least 350, at least 400, at least 450, at least 500, at least 750, at least 1000, at least 1250, at least 1500, at least 1750, at least 2000, at least 2500 , at least 3,000, at least 3,500, at least 4,000, at least about 4,500, at least about 5,000, at least about 5,500, at least about 6,000, at least about 6,500, at least about 7,000, but fewer than 7434 consecutive nucleotides of SEQ. ID. NO.: 35 or SEQ. ID. NO.: 36. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least least 99% or 100% sequence identity to the sequence of nucleic acids 1-7431 of SEQ. ID. NO.: 35 or SEQ. ID. NO.: 36. In some embodiments, a polynucleotide of the present disclosure comprises the nucleic acid sequence 1-7431 of SEQ. ID. NO.: 35 or SEQ. ID. NO.: 36. Polynucleotides Encoding Elastin Proteins In some embodiments, the present disclosure refers to a recombinant nucleic acid comprising one or more polynucleotides comprising the coding sequence for an elastin gene. The coding sequence of any elastin gene (including any of its isoforms) from any suitable species known in the art may be encoded by a polynucleotide of the present disclosure, including, for example, a human elastin gene (see , for example, NCBI gene ID: 2006), a mouse elastin gene (see, for example, NCBI gene ID: 13717), a chimpanzee elastin gene (see, for example, NCBI gene ID: NCBI: 463943), a rat elastin gene (see, for example, NCBI Gene ID: 25043), a rabbit elastin gene (see, for example, NCBI Gene ID: 100344271), etc. Methods for identifying orthologs / homologs of elastin genes in additional species are known to those skilled in the art. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity to the sequence of any of the elastin genes (and / or their coding sequences) described herein or known in the art. In some embodiments, a polynucleotide of the present disclosure comprises a codon-optimized variant of any of the elastin genes (and / or their coding sequences) described herein or known in the art. In some embodiments, the present disclosure refers to one or more polynucleotides (ie, one or more first polynucleotides and / or one or more second polynucleotides) that comprise the coding sequence of a human elastin gene. In some embodiments, a polynucleotide of the present disclosure comprises the coding sequence of the human ELN gene (or a codon-optimized variant thereof). In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % c / c i nn / ι znz / zi / Yl· sequence identity with the sequence of SEQ. ID. NO.: 37 or SEQ. ID. NO.: 38. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of SEQ. ID. NO.: 37 or SEQ. ID. NO.: 38. In some embodiments, a polynucleotide of the present disclosure comprises a 5' truncation, a 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 37 or SEQ. ID. NO.: 38. In some embodiments, the 5' truncation, the 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 37 or SEQ. ID. NO.: 38 is a polynucleotide with at least 25, at least 50, at least 75, at least 100, at least 125, at least 150, at least 175, at least 200, at least 250, at least 300, or at least 350, at least 400, at least 450, at least 500, at least 750, at least 1000, at least 1250, at least 1500, at least 1750, at least 2000, at least 2250, but less than 2361 consecutive nucleotides of the I KNOW THAT. ID. NO.: 37 or SEQ. ID. NO.: 38. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least least 99% or 100% sequence identity to the sequence of nucleic acids 1-2358 of SEQ. ID. NO.: 37 or SEQ. ID. NO.: 38. In some embodiments, a polynucleotide of the present disclosure comprises the nucleic acid sequence 1-2358 of SEQ. ID. NO.: 37 or SEQ. ID. NO.: 38. Polynucleotides Encoding Lumican Proteins In some embodiments, the present disclosure refers to a recombinant nucleic acid comprising one or more polynucleotides comprising the coding sequence of a lumican gene. The coding sequence of any lumican gene (including any of its isoforms) from any suitable species known in the art may be encoded by a polynucleotide of the present disclosure, including, for example, a human lumican gene (see , for example, NCBI gene ID: 4060), a mouse lumican gene (see, for example, NCBI gene ID: 17022), a chimpanzee lumican gene (see, for example, NCBI gene ID: NCBI: 452119), a rat lumican gene (see, for example, NCBI gene ID: 81682), a rabbit lumican gene (see, for example, NCBI gene ID: 100008665), etc. Methods for identifying orthologs / homologs of luminican genes in additional species are known to those skilled in the art. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity to the sequence of any of the lumican genes (and / or their coding sequences) described herein or known in the art. In some embodiments, a polynucleotide of the present disclosure comprises a codon-optimized variant of any of the lumican genes (and / or their coding sequences) described herein or known in the art. In some embodiments, the present disclosure refers to one or more polynucleotides (ie, one or more first polynucleotides and / or one or more second polynucleotides) that comprise the coding sequence of a human lumican gene. In some embodiments, a polynucleotide of the present disclosure comprises the coding sequence of the human LUM gene (or a codon-optimized variant thereof). In some embodiments, c / CLnn / Lznz / q / Yi a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the sequence of SEQ. ID. NO.: 39 or SEQ. ID. NO.: 40. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of SEQ. ID. NO.: 39 or SEQ. ID. NO.: 40. In some embodiments, a polynucleotide of the present disclosure comprises a 5' truncation, a 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 39 or SEQ. ID. NO.: 40. In some embodiments, the 5' truncation, the 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 39 or SEQ. ID. NO.: 40 is a polynucleotide with at least 25, at least 50, at least 75, at least 100, at least 125, at least 150, at least 175, at least 200, at least 250, at least 300, or at least 350, at least 400, at least 450, at least 500, at least 750, at least 1000, but less than 1017 consecutive nucleotides of SEQ. ID. NO.: 39 or SEQ. ID. NO.: 40. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least least 99% or 100% sequence identity to the sequence of nucleic acids 1-1014 of SEQ. ID. NO.: 39 or SEQ. ID. NO.: 40. In some embodiments, a polynucleotide of the present disclosure comprises the nucleic acid sequence 1-1014 of SEQ. ID. NO.: 39 or SEQ. ID. NO.: 40. Polynucleotides Encoding Vitronectin and Vitronectin Receptor Proteins In some embodiments, the present disclosure refers to a recombinant nucleic acid comprising one or more polynucleotides comprising the coding sequence for a vitronectin gene or the vitronectin receptor. The coding sequence of any vitronectin gene or the vitronectin receptor (including any of its isoforms) from any suitable species known in the art may be encoded by a polynucleotide of the present disclosure, including, for example, a gene vitronectin gene or the human vitronectin receptor (see, for example, NCBI gene IDs: 7448 and 3685), a vitronectin gene, or the mouse vitronectin receptor (see, for example, NCBI gene IDs: 22370 and 16410), a vitronectin gene or the chimpanzee vitronectin receptor (see, for example, NCBI gene IDs: 738261 and 459807), a vitronectin gene or the rat vitronectin receptor (see, for example, NCBI genes: 29169 and 257645), a vitronectin gene or the rabbit vitronectin receptor (see, for example, NCBI gene IDs: 100009128 and 100008956), etc. Methods for identifying orthologs / homologs of vitronectin genes or the vitronectin receptor in additional species are known to those skilled in the art. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity to the sequence of any of the vitronectin or vitronectin receptor genes (and / or their coding sequences) described herein or known in the art. In some embodiments, a polynucleotide of the present disclosure comprises a codon-optimized variant of any of the vitronectin or vitronectin receptor genes (and / or their c / CLnn / Lznz / q / Yi coding sequences) described in the invention. present or known in the art. In some embodiments, the present disclosure refers to one or more polynucleotides (ie, one or more first polynucleotides and / or one or more second polynucleotides) that comprise the coding sequence for a human vitronectin receptor or vitronectin gene. In some embodiments, a polynucleotide of the present disclosure comprises the coding sequence of the human VTN gene (or a codon-optimized variant thereof). In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity with the sequence of SEQ. ID. NO.: 41 or SEQ. ID. NO.: 42. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of SEQ. ID. NO.: 41 or SEQ. ID. NO.: 42. In some embodiments, a polynucleotide of the present disclosure comprises a 5' truncation, a 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 41 or SEQ. ID. NO.: 42. In some embodiments, the 5' truncation, the 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 41 or SEQ. ID. NO.: 42 is a polynucleotide with at least 25, at least 50, at least 75, at least 100, at least 125, at least 150, at least 175, at least 200, at least 250, at least 300, or at least 350, at least 400, at least 450, at least 500, at least 750, at least 1000, at least about 1250, but less than 1437 consecutive nucleotides of SEQ. ID. NO.: 41 or SEQ. ID. NO.: 42. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least least 99% or 100% sequence identity to the sequence of nucleic acids 1-1034 of SEQ. ID. NO.: 41 or SEQ. ID. NO.: 42. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of nucleic acids 1-1034 of SEQ. ID. NO.: 41 or SEQ. ID. NO.: 42. Polynucleotides Encoding Laminin Proteins In some embodiments, the present disclosure refers to a recombinant nucleic acid comprising one or more polynucleotides comprising the coding sequence for a laminin gene. The coding sequence of any laminin gene (including any of its isoforms) from any suitable species known in the art may be encoded by a polynucleotide of the present disclosure, including, for example, human laminin genes (see, for example, NCBI gene IDs: 284217, 3908, 3909, 3910, 3911, 3912, 3913, 3914, 3915, 3918, and 10319), mouse laminin genes (see, for example, NCBI gene IDs: 16774 , 16780, and 16782), a chimpanzee laminin gene (see, for example, NCBI gene IDs: 455339, 469668, and 457571), a rat laminin gene (see, for example, NCBI gene IDs: 307582 , 305078 and 192362), a rabbit laminin gene (see, for example, NCBI gene IDs: 100346886 and 100342905), etc. Methods for identifying orthologs / homologs of laminin genes in additional species are known to those skilled in the art. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at at least 90%, at least 91%, at least 92%, at least 93%, at least c / CLnn / Lznz / q / Yi%, at least 95%, at least 96%, at least 97%, at least 98 %, at least 99%, or 100% sequence identity to the sequence of any of the laminin genes (and / or their coding sequences) described herein or known in the art. In some embodiments, a polynucleotide of the present disclosure comprises a codon-optimized variant of any of the laminin genes (and / or their coding sequences) described herein or known in the art. In some embodiments, the present disclosure refers to one or more polynucleotides (ie, one or more first polynucleotides and / or one or more second polynucleotides) that comprise the coding sequence of a human laminin gene, such as the gene human LAMA1 (see, for example, NCBI gene ID: 284217), a human LAMA2 gene (see, for example, NCBI gene ID: 3908), a human LAMA3 gene (see, for example, NCBI gene ID: 3909), a human LAMA4 gene (see, for example, NCBI gene ID: 3910), a human LAMA5 gene (see, for example, NCBI gene ID: 3911), a human LAMBI (see, for example, NCBI gene ID: 3912), a human LAMB2 gene (see, for example, NCBI gene ID: 3913), a human LAMB3 gene (see, for example, NCBI gene ID: 3914), a human LAMC1 gene (see, for example, NCBI gene ID: 3915), a human LAMC2 gene (see, for example, NCBI gene ID: 3918), or a Human LAMC3 (see, for example, ID of genes in NCBI: 10319). In some embodiments, a polynucleotide of the present disclosure comprises the coding sequence of the human LAMA3 gene (or a codon-optimized variant thereof). In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity with the sequence of SEQ. ID. NO.: 43 or SEQ. ID. NO.: 44. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of SEQ. ID. NO.: 43 or SEQ. ID. NO.: 44. In some embodiments, a polynucleotide of the present disclosure comprises a 5' truncation, a 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 43 or SEQ. ID. NO.: 44. In some embodiments, the 5' truncation, the 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 43 or SEQ. ID. NO.: 44 is a polynucleotide with at least 25, at least 50, at least 75, at least 100, at least 125, at least 150, at least 175, at least 200, at least 250, at least 300, or at least 350, at least 400, at least 450, at least 500, at least 750, at least 1000, at least 1250, at least 1500, at least 1750, at least 2000, at least 2500, at least 3000, at least 3500, at least 4000, at least about 4500, at least about 5000 but less than 5175 consecutive nucleotides of SEQ. ID. NO.: 43 or SEQ. ID. NO.: 44. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least least 99% or 100% sequence identity to the sequence of nucleic acids 1-5172 of SEQ. ID. NO.: 43 or SEQ. ID. NO.: 44. In some embodiments, a polynucleotide of the present disclosure comprises the nucleic acid sequence 1-5172 of SEQ. ID. NO.: 43 or SEQ. ID. NO.: 44. c / CLnn / Lznz / q / Yi In some embodiments, a polynucleotide of the present disclosure comprises the coding sequence of the human LAMB3 gene (or a codon-optimized variant thereof). In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity with the sequence of SEQ. ID. NO.: 45 or SEQ. ID. NO.: 46. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of SEQ. ID. NO.: 45 or SEQ. ID. NO.: 46. In some embodiments, a polynucleotide of the present disclosure comprises a 5' truncation, a 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 45 or SEQ. ID. NO.: 46. In some embodiments, the 5' truncation, the 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 45 or SEQ. ID. NO.: 46 is a polynucleotide with at least 25, at least 50, at least 75, at least 100, at least 125, at least 150, at least 175, at least 200, at least 250, at least 300, or at least 350, at least 400, at least 450, at least 500, at least 750, at least 1000, at least 1250, at least 1500, at least 1750, at least 2000, at least 2500, at least 3000, at least 3500, but less than 3519 consecutive nucleotides of SEQ. ID. NO.: 45 or SEQ. ID. NO.: 46. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least least 99% or 100% sequence identity to the sequence of nucleic acids 1-3516 of SEQ. ID. NO.: 45 or SEQ. ID. NO.: 46. In some embodiments, a polynucleotide of the present disclosure comprises the nucleic acid sequence 1-3516 of SEQ. ID. NO.: 45 or SEQ. ID. NO.: 46. In some embodiments, a polynucleotide of the present disclosure comprises the coding sequence of the human LAMC2 gene (or a codon-optimized variant thereof). In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity with the sequence of SEQ. ID. NO.: 47 or SEQ. ID. NO.: 48. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of SEQ. ID. NO.: 47 or SEQ. ID. NO.: 48. In some embodiments, a polynucleotide of the present disclosure comprises a 5' truncation, a 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 47 or SEQ. ID. NO.: 48. In some embodiments, the 5' truncation, the 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 47 or SEQ. ID. NO.: 48 is a polynucleotide with at least 25, at least 50, at least 75, at least 100, at least 125, at least 150, at least 175, at least 200, at least 250, at least 300, or at least 350, at least 400, at least 450, at least 500, at least 750, at least 1000, at least 1250, at least 1500, at least 1750, at least 2000, at least 2500, at least 3000, at least 3500, but less than 3582 consecutive nucleotides of SEQ. ID. NO.: 47 or SEQ. ID. NO.: 48. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at at least 89%, at least 90%, at least 91%, at least 92%, at c / CLnn / Lznz / q / Yi at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the sequence of nucleic acids 1-3579 of SEQ. ID. NO.: 47 or SEQ. ID. NO.: 48. In some embodiments, a polynucleotide of the present disclosure comprises the nucleic acid sequence 1-3579 of SEQ. ID. NO.: 47 or SEQ. ID. NO.: 48. Polynucleotides Encoding Neuromodulatory Proteins In some embodiments, the present disclosure refers to a recombinant nucleic acid comprising one or more polynucleotides comprising the coding sequence for a neuromodulator gene. The coding sequence of any neuromodulator gene (including any isoforms thereof) from any suitable species known in the art may be encoded by a polynucleotide of the present disclosure, including, for example, a clostridium botulinum neuromodulator gene (see , for example, NCBI gene IDs: 5185061 and 39483740), etc. Methods for identifying orthologs / homologs of neuromodulatory genes in additional species are known to those skilled in the art. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity to the sequence of any of the neuromodulatory genes (and / or their coding sequences) described herein or known in the art. In some embodiments, a polynucleotide of the present disclosure comprises a codon-optimized variant of any of the neuromodulatory genes (and / or their coding sequences) described herein or known in the art. In some embodiments, the present disclosure refers to one or more polynucleotides (ie, one or more first polynucleotides and / or one or more second polynucleotides) that comprise the coding sequence of a clostridium botulinum neuromodulator gene. In some embodiments, a polynucleotide of the present disclosure comprises the coding sequence of the Clostridium botulinum botA gene (or a codon-optimized variant thereof). In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity with the sequence of SEQ. ID. NO.: 49 or SEQ. ID. NO.: 50. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of SEQ. ID. NO.: 49 or SEQ. ID. NO.: 50. In some embodiments, a polynucleotide of the present disclosure comprises a 5' truncation, a 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 49 or SEQ. ID. NO.: 50. In some embodiments, the 5' truncation, the 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 49 or SEQ. ID. NO.: 50 is a polynucleotide with at least 25, at least 50, at least 75, at least 100, at least 125, at least 150, at least 175, at least 200, at least 250, at least 300, or at least 350, at least 400, at least 450, at least 500, at least 750, at least 1000, at least about 1250, at least 1500, at least 1750, at least 2000, at least 2500, at least 3000, at least 3500, but less than 3891 consecutive nucleotides of SEQ. ID. NO.: 49 or SEQ. ID. NO.: 50. In some c / CLnn / Lznz / q / Yi embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the sequence of nucleic acids 1-3888 of SEQ. ID. NO.: 49 or SEQ. ID. NO.: 50. In some embodiments, a polynucleotide of the present disclosure comprises the nucleic acid sequence 1-3888 of SEQ. ID. NO.: 49 or SEQ. ID. NO.: 50. In some embodiments, a polynucleotide of the present disclosure comprises the coding sequence of the Clostridium botulinum botB gene (or a codon-optimized variant thereof). In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity with the sequence of SEQ. ID. NO.: 51 or SEQ. ID. NO.: 52. In some embodiments, a polynucleotide of the present disclosure comprises the sequence of SEQ. ID. NO.: 51 or SEQ. ID. NO.: 52. In some embodiments, a polynucleotide of the present disclosure comprises a 5' truncation, a 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 51 or SEQ. ID. NO.: 52. In some embodiments, the 5' truncation, the 3' truncation, or a fragment of the sequence of SEQ. ID. NO.: 51 or SEQ. ID. NO.: 52 is a polynucleotide with at least 25, at least 50, at least 75, at least 100, at least 125, at least 150, at least 175, at least 200, at least 250, at least 300, or at least 350, at least 400, at least 450, at least 500, at least 750, at least 1000, at least about 1250, at least 1500, at least 1750, at least 2000, at least 2500, at least 3000, at least 3500, but less than 3876 consecutive nucleotides of SEQ. ID. NO.: 51 or SEQ. ID. NO.: 52. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least least 99% or 100% sequence identity to the sequence of nucleic acids 1-3873 of SEQ. ID. NO.: 51 or SEQ. ID. NO.: 52. In some embodiments, a polynucleotide of the present disclosure comprises the nucleic acid sequence 1-3873 of SEQ. ID. NO.: 51 or SEQ. ID. NO.: 52. Polynucleotides Encoding Fibrillin Proteins In some embodiments, the present disclosure refers to a recombinant nucleic acid comprising one or more polynucleotides comprising the coding sequence for a fibrillin gene. The coding sequence of any fibrillin gene (including any of its isoforms) from any suitable species known in the art may be encoded by a polynucleotide of the present disclosure, including, for example, human fibrillin genes (see, for example, NCBI gene IDs: 2200, 2201, and 84467), a mouse fibrillin gene (see, for example, NCBI gene IDs: 14118 and 14119), a chimpanzee fibrillin gene (see, for example, , NCBI gene IDs: 453411, 471621, and 455669), a rat fibrillin gene (see, for example, NCBI gene IDs: 83727 and 689008), a rabbit fibrillin gene (see, for example, NCBI gene IDs: of genes in NCBI: 100350931, 100357126 and 100359336), etc. Methods for identifying orthologs / homologs of fibrillin genes in additional c / CLnn / Lznz / q / Yi species are known to those skilled in the art. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity to the sequence of any of the fibrillin genes (and / or their coding sequences) described herein or known in the art. In some embodiments, a polynucleotide of the present disclosure comprises a codon-optimized variant of any of the fibrillin genes (and / or their coding sequences) described herein or known in the art. In some embodiments, the present disclosure refers to one or more polynucleotides (i.e., one or more first polynucleotides and / or one or more second polynucleotides) that comprise the coding sequence of a human fibrillin gene, such as the human FBN1 gene. (see, for example, NCBI Gene ID: 2200), a human FBN2 gene (see, for example, NCBI Gene ID: 2201), or a human FBN3 gene (see, for example, NCBI Gene ID: 2201). NCBI: 84467). Examples of polynucleotides In some embodiments, a polynucleotide of the present disclosure that encodes one or more human collagen proteins (for example, a first cosmetic collagen protein, another cosmetic collagen protein, another cosmetic collagen protein, and / or a second cosmetic collagen protein). ) has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a nucleic acid sequence selected from SEQ. ID. NO.: 1-14 or 35-52. In some embodiments, a polynucleotide of the present disclosure that encodes one or more human collagen proteins (eg, a first cosmetic protein, another cosmetic protein, another cosmetic protein, and / or a second cosmetic protein) comprises a sequence selected from the following: I KNOW THAT. ID. NO.: 1-14 or 35-52. In some embodiments, a polynucleotide of the present disclosure that encodes one or more human collagen proteins (for example, a first cosmetic collagen protein, another cosmetic collagen protein, another cosmetic collagen protein, and / or a second cosmetic collagen protein). ) has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a nucleic acid sequence selected from SEQ. ID. NO.: 1-14, 35-38 or 43-48. In some embodiments, a polynucleotide of the present disclosure that encodes one or more human collagen proteins (eg, a first cosmetic protein, another cosmetic protein, another cosmetic protein, and / or a second cosmetic protein) comprises a sequence selected from the following: I KNOW THAT. ID. NO.: 1-14, 35-38 or 43-48. A polynucleotide of the present disclosure that encodes a cosmetic protein (eg, a human collagen protein) may further encode additional coding and non-coding sequences. Examples of additional coding and non-coding sequences may include, but are not limited to, sequences encoding additional polypeptide tags (for example, encoded in the same frame as the cosmetic protein, to produce a fusion protein), introns (for natural, modified, or heterologous introns), 5' and / or 3' UTR (for example, c / CLnn / Lznz / q / Yi natural, modified or heterologous 5' and / or 3' UTR) and the like. Examples of suitable polypeptide tags may include, but are not limited to, any combination of purification tags, such as his tags, flag tags, glutathione S-transferase and maltose binding protein tags, detection tags, such as tags that can detected by photometric means (eg green fluorescent protein, red fluorescent protein, etc.) and tags with detectable enzymatic activity (eg alkaline phosphatase, etc.), tags with secretion sequences, signal sequences, leader sequences, and / or stabilization sequences, protease cleavage sites (eg, furin cleavage sites, TEV cleavage sites, thrombin cleavage sites, etc.) and the like. In some embodiments, 5' and / or 3' UTRs increase the stability, localization, and / or translation efficiency of polynucleotides. In some embodiments, 5' and / or 3' UTRs enhance the level and / or duration of protein expression. In some embodiments, the 5' and / or 3' UTRs include elements (eg, one or more miRNA binding sites, etc.) that can block or reduce off-target expression (eg, inhibition of expression in specific cell types (for example, neuronal cells), at specific times in the cell cycle, at specific developmental stages, etc.). In some embodiments, the 5' and / or 3' UTRs include elements (eg, one or more miRNA binding sites, etc.) that can enhance expression of cosmetic proteins in specific cell types (such as fibroblasts and / or human keratinocytes). In some embodiments, a polynucleotide of the present disclosure encoding a cosmetic protein (eg, a human collagen protein) is operatively linked to one or more (eg, one or more, two or more, three or more , four or more, five or more, ten or more, etc.) regulatory sequences. The term "regulatory sequence" can include enhancers, insulators, promoters, and other expression control elements (eg, polyadenylation signals). Any suitable enhancer known in the art may be used, including, for example, enhancer sequences from mammalian genes (such as globin, elastase, albumin, o-fetoprotein, insulin, and the like), enhancer sequences from a eukaryotic cell virus (such as the enhancer of SV40 on the late side of the replication origin (bp 100-270), the cytomegalovirus early promoter enhancer, the polyoma enhancer on the late side of the replication origin, adenovirus enhancers, and the like), as well as any combination of these. Any isolate known in the art can be used, including, for example, the HSV chromatin delimiting elements (CTCF / CTRL isolator / binding) CTRL1 and / or CTRL2, chicken hot spot isolate 4 (cHS4), element ubiquitous chromatin opening gap (UCOE) of HNRPA2B1—CBX3 in humans, the matrix / backbone junction region (S / MAR) of the human interferon beta (IFNB1) gene , as well as any combination of these. Any suitable promoter (eg, suitable for transcription in mammalian host cells) known in the art can be used, including, for example, promoters derived from the genomes of viruses (such as polyoma virus, avian pox virus, adenovirus ( such as adenovirus 2), bovine papilloma virus, avian sarcoma virus, cytomegalovirus, a retrovirus, hepatitis B virus, simian virus 40 (SV40) and the like), heterologous mammalian gene promoters (such as the actin promoter (for example, the β-actin promoter), a ubiquitin promoter (for example, a ubiquitin C (UbC) promoter), a phosphoglycerate kinase (PGK) promoter, an immunoglobulin promoter, heat shock promoter and the like), promoters from homologous mammalian genes (for example, natural human c / CLnn / Lznz / q / Yi collagen, fibronectin, elastin, lumican, vitronectin, laminin and / or fibrillin promoters), synthetic promoters (such as the promoter of CAGG) and any combination of these, provided that such promoters are compatible with the host cells. Regulatory sequences may include those that directly express a nucleic acid constitutively, as well as repressible or inducible and / or tissue-specific regulatory sequences. In some embodiments, a polynucleotide of the present disclosure encoding a cosmetic protein (eg, a human collagen protein) is operatively linked to one or more heterologous promoters. In some embodiments, the heterologous promoter(s) are one or more constitutive promoters, tissue-specific promoters, temporal promoters, spatial promoters, inducible promoters, and repressible promoters. In some embodiments, the heterologous promoter(s) are one or more of the human cytomegalovirus (HCMV) immediate early promoter, the human elongation factor 1 (EF1) promoter, the human β-actin promoter, the human UbC promoter, the human PGF promoter, the synthetic CAGG promoter, and any combination of these. In some embodiments, a polynucleotide of the present disclosure encoding a cosmetic protein (eg, a human collagen protein) is operatively linked to an HCMV promoter. In some embodiments, a polynucleotide of the present disclosure does not comprise the coding sequence for (eg, a transgene encoding) a collagen alpha-1 (Vil) chain (COL7) polypeptide. In some embodiments, a polynucleotide of the present disclosure does not comprise the coding sequence for (eg, a transgene encoding) a lysylhydroxylase 3 (LH3) polypeptide. In some embodiments, a polynucleotide of the present disclosure does not comprise the coding sequence for (eg, a transgene encoding) a keratin type I cytoskeletal 17 (KRT17) polypeptide. In some embodiments, a polynucleotide of the present disclosure does not comprise the coding sequence for (eg, a transgene encoding) a transglutaminase (TGM) polypeptide (eg, a human transglutaminase polypeptide, such as a human TGM1 polypeptide). . In some embodiments, a polynucleotide of the present disclosure does not comprise the coding sequence for (eg, a transgene encoding) a laminin beta-3 subunit (LAMB3) polypeptide. In some embodiments, a polynucleotide of the present disclosure does not comprise the coding sequence for (eg, a transgene encoding) an alpha-1 (Vil) collagen chain polypeptide, a lysylhydroxylase 3 polypeptide, a cytoskeletal polypeptide 17 type I keratin and / or any chimeric polypeptide thereof. In some embodiments, a polynucleotide of the present disclosure does not comprise the coding sequence for (eg, a transgene encoding) a collagen alpha-1 (Vil) chain polypeptide, a lysylhydroxylase 3 polypeptide, a cytoskeletal polypeptide 17 type I keratin polypeptide, a transglutaminase (TGM) polypeptide (eg, a human transglutaminase polypeptide such as a human TGM1 polypeptide), a laminin beta-3 subunit (LAMB3) polypeptide (eg, a LamB3 polypeptide human) and / or any chimeric polypeptide thereof. cosmetic proteins collagen proteins In some embodiments, the present disclosure refers to one or more polynucleotides encoding a full-length c / CLnn / Lznz / q / Yi collagen protein or any isoform or part thereof. The polynucleotides of the present disclosure can encode any collagen protein from any species known in the art, including, for example, human collagen proteins (see, for example, UniProt accession numbers P02452, P08123, P02461, P02462, P08572, P12109, Q02388, Q9UMD9. etc.), mouse collagen proteins (see, for example, UniProt accession numbers P11087, Q01149, P08121, P02463, P08122, Q04857, Q63870, Q07563, etc.), mouse collagen proteins chimpanzee (see, for example, UniProt accession numbers A0A2I3SM98, A0A2J8L483, H2QJ46, K7C8P4, K7C8W0, A0A2J8M8U9, H2QMJ5, H2Q2J4, etc.), rat collagen proteins (see, for example, UniProt accession numbers P02454, P02466, P13941, P02466, F1M6Q3, D3ZUL3, D3ZE04, D3ZE04, etc.), rabbit collagen proteins (see, for example, UniProt accession numbers G1T4A5, Q28668, G1T8J0, G1U9R7, G1T548, G1T380, G1T548, etc. ), etc. Methods for identifying orthologs / homologs of collagen proteins in additional species are known in the art and include, for example, the use of an amino acid sequence alignment program such as BLAST® or OrthoDB software. In some embodiments, a collagen polypeptide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at c / c i nn / ι znz / zi / Yl minus 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least %, at least 97 %, at least 98%, at least 99%, or 100% sequence identity to the sequence of any of the collagen polypeptides described herein or known in the art. In some embodiments, the present disclosure refers to one or more polynucleotides that encode a human collagen protein. A polynucleotide of the present disclosure can encode any human collagen protein known in the art, including, for example, a collagen alpha-1 (I) chain polypeptide (COL11) (see, for example, UniProt accession number P02452 ; SEQ. ID. NO.: 15), a collagen alpha-2(l) chain polypeptide (COL1-2) (see, for example, UniProt accession number P08123; SEQ. ID. NO.: 16) , a collagen alpha-1(II) chain polypeptide (COL2) (see, for example, UniProt accession number P02458), a collagen alpha-1(III) chain (COL3) polypeptide (see, for example, , UniProt accession number P2461; SEQ. ID. NO.: 17), a collagen alpha-1 (IV) chain polypeptide (COL4-1) (see, for example, UniProt accession number P02462; SEQ. ID NO: 18), a collagen alpha-2(IV) chain polypeptide (COL4-2) (see, for example, UniProt accession number P08572), a collagen alpha-3(IV) chain polypeptide collagen (COL4-3) (see, for example, UniProt accession number Q0 1955), a collagen alpha-4(IV) chain polypeptide (COL4-4) (see, for example, UniProt accession number P53420), a collagen alpha-5(IV) chain polypeptide (COL4-5 ) (see, for example, UniProt accession number 29400), a collagen alpha-6(IV) chain polypeptide (COL4-6) (see, for example, UniProt accession number Q14031), a collagen collagen alpha-1(V) (COL5-1) (see, for example, UniProt accession number P20908), an alpha-2(V) collagen (COL5-2) chain polypeptide (see, for example, UniProt accession number P05997), a collagen alpha-3(V) chain polypeptide (COL5-3) (see, for example, UniProt accession number P25940), a collagen alpha-1 (VI) chain polypeptide collagen (COL6-1) (see, for example, UniProt accession number P12109; I KNOW THAT. ID. NO.: 19), a collagen alpha-2(VI) chain polypeptide (COL6-2) (see, for example, UniProt accession number P12110), a collagen alpha-3(VI) chain polypeptide ( COL6-3) (see, for example, UniProt accession number P12111), a collagen alpha-4(VI) chain polypeptide (COL6-4), a collagen alpha-5(VI) chain polypeptide (COL6-5) (see, for example, UniProt accession number A8TX70 ), a collagen alpha-6(VI) chain polypeptide (COL6-6) (see, for example, UniProt accession number A6NMZ7), a collagen alpha-1 (VI) chain polypeptide (COL7) (see , for example, UniProt accession number Q02388; SEQ ID NO: 20), a collagen alpha-1 (VIII) chain polypeptide (COL8) (see, for example, UniProt accession number P27658), a collagen alpha-1 (IX) chain polypeptide (COL9-1) (see, for example, UniProt accession number P20849), a collagen alpha-2(IX) chain polypeptide (COL9-2) (see , for example, UniProt accession number Q14055), a collagen alpha-3(IX) chain polypeptide (COL9-3) (see, for example, UniProt accession number Q14050), an alpha-1 chain polypeptide (X) collagen (COL10) (see, for example, UniProt accession number Q03692), a polypeptide collagen alpha-1 (XI) chain polypeptide (COL11-1) (see, for example, UniProt accession number P12107), a collagen alpha-2 (XI) chain (COL11-2) polypeptide (see, for example, UniProt accession number P13942), a collagen alpha-1 (XII) chain polypeptide (COL12) (see, for example, UniProt accession number Q99715), an alpha-1 (XIII) chain polypeptide collagen (COL13) (see, for example, UniProt accession number Q5TAT6), an alpha-1 (XIV) chain polypeptide of collagen (COL14) (see, for example, UniProt accession number Q05707), a collagen polypeptide collagen alpha-1 (XV) chain (COL15) (see, for example, UniProt accession number P39059), collagen alpha-1 (XVI) chain (COL16) polypeptide (see, for example, accession number UniProt accession number Q07092), a collagen alpha-1(XVII) chain polypeptide (COL17) (see, for example, UniProt accession number Q9UMD9; I KNOW THAT. ID. NO.: 21), a collagen alpha-1 (XVIII) chain polypeptide (COL18) (see, for example, UniProt accession number P39060), a collagen alpha-1 (XIX) chain polypeptide (COL19) (see, for example, UniProt accession number Q14993), a collagen alpha-1 (XX) chain polypeptide (COL20) (see, for example, UniProt accession number Q9P218), an alpha-1 chain polypeptide (XXI) collagen (COL21) (see, for example, UniProt accession number Q96P44), an alpha-1 chain polypeptide (XXII) of collagen (COL22) (see, for example, UniProt accession number Q8NFW1) , a collagen alpha-1 (XXIII) chain polypeptide (COL23) (see, for example, UniProt accession number Q86Y22), a collagen alpha-1 (XXIV) chain polypeptide (COL24) (see, for example, , UniProt accession number Q17RW2), a collagen alpha-1 (XXV) chain polypeptide (COL25) (see, for example, UniProt accession number Q9BXS0), a collagen alpha-1 (XXVI) chain polypeptide (COL26) (see, for example eg, UniProt accession number Q96A83), a collagen (COL27) alpha-1 (XXVII) chain polypeptide (see, for example, UniProt accession number Q8IZC6), an alpha-1 (XXVIII) chain polypeptide of collagen (COL28) (see, for example, UniProt accession number Q2UY09), etc. In some embodiments, a polynucleotide of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100 % sequence identity to the sequence encoding any of the human collagen polypeptides described herein or known in the art. Methods for identifying orthologs / homologs of human collagen or collagen-like polypeptides are known in the art and include, for example, the use of an amino acid sequence alignment program such as BLAST® or OrthoDB software. In some embodiments, a polynucleotide of the present disclosure encodes a human COL1-1 protein. In some embodiments, a polynucleotide encoding a COL1-1 protein is a polynucleotide encoding a c / CLnn / Lznz / q / Yi polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85% , at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95% , at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the sequence of SEQ. ID. NO.: 15. In some embodiments, a polynucleotide encoding a human C0L1-1 protein is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 15. In some embodiments, a polynucleotide encoding a COL1-1 protein is a polynucleotide encoding an N-terminal truncation, an O-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 15. The N-terminal truncations, O-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 600, at least 700, at least 800, at least 900, at least 1000, at least 1100, at least 1200, at least 1300, at least 1400, but less than 1464 consecutive amino acids of SEQ. ID. NO.: 15. In some embodiments, a polynucleotide of the present disclosure encodes a human COL1-2 protein. In some embodiments, a polynucleotide encoding a COL1-2 protein is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87 %, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97 %, at least 98%, at least 99%, or 100% sequence identity to the sequence of SEQ. ID. NO.: 16. In some embodiments, a polynucleotide encoding a human COL1-2 protein is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 16. In some embodiments, a polynucleotide encoding a COL1-2 protein is a polynucleotide encoding an N-terminal truncation, a C-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 16. The N-terminal truncations, O-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 600, at least 700, at least 800, at least 900, at least 1000, at least 1100, at least 1200, at least 1300, but less than 1366 consecutive amino acids of SEQ. ID. NO.: 16. In some embodiments, a polynucleotide of the present disclosure encodes a human COL3 protein. In some embodiments, a polynucleotide encoding a COL3 protein is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the sequence of SEQ. ID. NO.: 17. In some embodiments, a polynucleotide encoding a human COL3 protein is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 17. c / c i nn / ι znz / zi / Yl In some embodiments, a polynucleotide encoding a COL3 protein is a polynucleotide encoding an N-terminal truncation, a C-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 17. The N-terminal truncations, O-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 600, at least 700, at least 800, at least 900, at least 1000, at least 1100, at least 1200, at least 1300, at least 1400, but less than 1466 consecutive amino acids of SEQ. ID. NO.: 17. In some embodiments, a polynucleotide of the present disclosure encodes a human COL4-1 protein. In some embodiments, a polynucleotide encoding a COL4-1 protein is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87 %, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97 %, at least 98%, at least 99%, or 100% sequence identity to the sequence of SEQ. ID. NO.: 18. In some embodiments, a polynucleotide encoding a human COL4-1 protein is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 18. In some embodiments, a polynucleotide encoding a COL4-1 protein is a polynucleotide encoding an N-terminal truncation, a C-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 18. The N-terminal truncations, C-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 600, at least 700, at least 800, at least 900, at least 1000, at least 1100, at least 1200, at least 1300, at least 1400, at least 1500, at least 1600, but less than 1669 consecutive amino acids of SEQ. ID. NO.: 18. In some embodiments, a polynucleotide of the present disclosure encodes a human COL6-1 protein. In some embodiments, a polynucleotide encoding a COL6-1 protein is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87 %, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97 %, at least 98%, at least 99%, or 100% sequence identity to the sequence of SEQ. ID. NO.: 19. In some embodiments, a polynucleotide encoding a human COL6-1 protein is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 19. In some embodiments, a polynucleotide encoding a COL6-1 protein is a polynucleotide encoding an N-terminal truncation, an O-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 19. The N-terminal truncations, O-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 600, at least 700, at least 800, at least 900, at least 1000, but less than 1028 consecutive amino acids of SEQ. ID. NO.: 19. c / CLnn / Lznz / q / Yi In some embodiments, a polynucleotide of the present disclosure encodes a human COL7 protein. In some embodiments, a polynucleotide encoding a COL7 protein is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the sequence of SEQ. ID. NO.: 20. In some embodiments, a polynucleotide encoding a human COL7 protein is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 20. In some embodiments, a polynucleotide encoding a COL7 protein is a polynucleotide encoding an N-terminal truncation, an O-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 20. The N-terminal truncations, C-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 600, at least 700, at least 800, at least 900, at least 1000, at least 1100, at least 1200, at least 1300, at least 1400, at least 1500, at least 1600, at least 1700, at least 1800, at least 1900, at least 2000, at least 2100, at least 2200, at least 2300, at least 2400, at least 2500, at least 2600, at least 2700, at least 2800, at least 2900, but less than 2944 consecutive amino acids of SEQ. ID. NO.: 20. In some embodiments, a polynucleotide of the present disclosure encodes a human COL17 protein. In some embodiments, a polynucleotide encoding a COL17 protein is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the sequence of SEQ. ID. NO.: 21. In some embodiments, a polynucleotide encoding a human COL17 protein is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 21. In some embodiments, a polynucleotide encoding a COL17 protein is a polynucleotide encoding an N-terminal truncation, an O-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 21. The N-terminal truncations, O-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 600, at least 700, at least 800, at least 900, at least 1000, at least 1100, at least 1200, at least 1300, at least 1400, but less than 1497 consecutive amino acids of SEQ. ID. NO.: 21. In some embodiments, one or more human collagen proteins of the present disclosure (eg, a first human collagen protein, another human collagen protein, a further human collagen protein, and / or a second human collagen protein) comprises a amino acid sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least c / CLnn / Lznz / q / Yi %, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence selected from SEQ. ID. NO.: 15-21. In some embodiments, one or more human collagen proteins of the present disclosure (eg, a first human collagen protein, another human collagen protein, a further human collagen protein, and / or a second human collagen protein) comprises a selected sequence of SEQ. ID. NO.: 15-21. In some embodiments, one or more human collagen proteins of the present disclosure (eg, a first human collagen protein, another human collagen protein, a further human collagen protein, and / or a second human collagen protein) comprises a amino acid sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence selected from SEQ. ID. NO.: 15-17. In some embodiments, one or more human collagen proteins of the present disclosure (eg, a first human collagen protein, another human collagen protein, a further human collagen protein, and / or a second human collagen protein) comprises a selected sequence of SEQ. ID. NO.: 15-17. fibronectin proteins In some embodiments, the present disclosure refers to one or more polynucleotides encoding a full-length fibronectin protein or any isoform or part thereof. A polynucleotide of the present disclosure may encode any fibronectin protein from any suitable species known in the art, including, for example, a human fibronectin protein (see, for example, UniProt accession number P02751), a mouse fibronectin protein (see, for example, UniProt accession number P11276), a chimpanzee fibronectin protein (see, for example, UniProt accession number P11276), a rat fibronectin protein (see, for example, UniProt accession number P04937) , a rabbit fibronectin protein (see, for example, UniProt accession number P04937), etc. Methods for identifying orthologs / homologs of fibronectin proteins in additional species are known to those skilled in the art. In some embodiments, a fibronectin protein of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89% , at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the sequence of any of the fibronectin proteins described herein or known in the art. In some embodiments, a polynucleotide of the present disclosure encodes a human fibronectin protein. In some embodiments, a polynucleotide encoding a human fibronectin protein is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87 %, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97 %, at least 98%, at least 99%, or 100% sequence identity to the sequence of SEQ. ID. NO.: 53. In some embodiments, a polynucleotide encoding a human fibronectin protein is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 53. c / CLnn / Lznz / q / Yi In some embodiments, a polynucleotide encoding a human fibronectin protein is a polynucleotide encoding an N-terminal truncation, a C-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 53. The N-terminal truncations, C-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 600, at least 700, at least 800, at least 900, at least 1000, at least 1100, at least 1200, at least 1300, at least 1400, at least 1500, at least 1600, at least 1700, at least 1800, at least 1900, at least 2000, at least 2100, at least 2200, at least 2300, at least 2400, but less than 2477 consecutive amino acids from SEQ. ID. NO.: 53. Elastin and associated proteins Elastic fibers in the extracellular matrix provide elastic properties to the tissue. Elastic fibers typically contain two morphologically distinct components: mature elastin fibers and microfibrils, which contain mainly fibrillin and are associated with other proteins, such as microfibril-associated glycoproteins (MAGPs), fibulins, and elastin proteins. located at the elastin-microfibril interface (EMILIN). Elastin and its soluble precursor, tropoelastin, belong to the major structural proteins in the body. In some embodiments, the present disclosure refers to one or more polynucleotides encoding an elastin or elastin-associated protein, including a tropoelastin, a fibrillin, a microfibril-associated glycoprotein, a fibulin, or a protein located at the elastin interface and microfibrils. In some embodiments, the present disclosure refers to one or more polynucleotides that encode a full-length elastin protein or any isoform or part thereof. A polynucleotide of the present disclosure can encode any elastin protein from any suitable species known in the art, including, for example, a human elastin protein (see, for example, UniProt accession number P15502), a mouse elastin protein (see, for example, UniProt accession number P15502), a chimpanzee elastin protein (see, for example, UniProt accession number H2QUQ6), a rat elastin protein (see, for example, UniProt accession number Q99372) , etc. Methods for identifying orthologs / homologs of elastin proteins in additional species are known to those skilled in the art. In some embodiments, an elastin protein of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89% , at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the sequence of any of the elastin proteins described herein or known in the art. In some embodiments, a polynucleotide of the present disclosure encodes a human elastin protein. In some embodiments, a polynucleotide encoding a human elastin protein is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87 %, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97 %, at least 98%, at least 99%, or 100% sequence identity to the sequence of SEQ. ID. NO.: 54. In some embodiments, a polynucleotide encoding c / CLnn / Lznz / q / Yi for a human elastin protein is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 54. In some embodiments, a polynucleotide encoding a human elastin protein is a polynucleotide encoding an N-terminal truncation, a C-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 54. The N-terminal truncations, O-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 600, at least 700, but less than 786 consecutive amino acids of SEQ. ID. NO.: 54. lumican proteins In some embodiments, the present disclosure refers to one or more polynucleotides encoding a full-length lumican protein or any isoform or part thereof. A polynucleotide of the present disclosure can encode any lumican protein from any suitable species known in the art, including, for example, a human lumican protein (see, for example, UniProt accession number P51884), a mouse lumican protein (see, for example, UniProt accession number P51885), a chimpanzee lumican protein (see, for example, UniProt accession number H2Q6L3), a rat lumican protein (see, for example, UniProt accession number H2Q6L3), a rat lumican protein rabbit (see, for example, UniProt accession number 046379), etc. Methods for identifying orthologs / homologs of lumican proteins in additional are known to those skilled in the art. In some embodiments, a lumican protein of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the sequence of any of the lumican proteins described herein or known in the art. In some embodiments, a polynucleotide of the present disclosure encodes a human lumican protein. In some embodiments, a polynucleotide encoding a human lumican protein is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87% , at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97% , at least 98%, at least 99% or 100% sequence identity to the sequence of SEQ. ID. NO.: 55. In some embodiments, a polynucleotide encoding a human lumican protein is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 55. In some embodiments, a polynucleotide encoding a human lumican protein is a polynucleotide encoding an N-terminal truncation, an O-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 55. The N-terminal truncations, C-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, but less than 338 consecutive amino acids of SEQ. ID. NO.: 55. c / CLnn / Lznz / q / YL Vitronectin and vitronectin receptor proteins In some embodiments, the present disclosure refers to one or more polynucleotides encoding a full-length vitronectin or vitronectin receptor protein or any isoform or part thereof. A polynucleotide of the present disclosure may encode any vitronectin or vitronectin receptor protein from any suitable species known in the art, including, for example, a human vitronectin or vitronectin receptor protein (see, for example, UniProt accession numbers P04004 and P06756), a mouse vitronectin or vitronectin receptor protein (see, for example, UniProt accession numbers P29788 and P43406), a chimpanzee vitronectin or vitronectin receptor protein (see, for example, UniProt accession numbers H2QCH3 and H2R6C3), a rat vitronectin or vitronectin receptor protein (see, for example, UniProt accession number Q7TQ11), a rabbit vitronectin or vitronectin receptor protein (see, for example, UniProt accession number P22458), etc Methods for identifying orthologs / homologs of vitronectin proteins or vitronectin receptors in additional species are known to those skilled in the art. In some embodiments, a vitronectin or vitronectin receptor protein of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the sequence of any of the vitronectin or vitronectin receptor proteins described herein or known in the art. In some embodiments, a polynucleotide of the present disclosure encodes a human vitronectin protein. In some embodiments, a polynucleotide encoding a human vitronectin protein is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87 %, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97 %, at least 98%, at least 99%, or 100% sequence identity to the sequence of SEQ. ID. NO.: 56. In some embodiments, a polynucleotide encoding a human vitronectin protein is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 56. In some embodiments, a polynucleotide encoding a human vitronectin protein is a polynucleotide encoding an N-terminal truncation, a C-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 56. N-terminal truncations, O-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, but less than 478 consecutive amino acids of SEQ. ID. NO.: 56. laminin proteins In some embodiments, the present disclosure refers to one or more polynucleotides encoding a full-length laminin protein or any isoform or part thereof. A polynucleotide of the present disclosure may encode any laminin protein from any suitable species known in the art, including, for example, a human laminin protein (see, for example, UniProt accession numbers P25391, c / CLnn / Lznz / q / Yi Ρ24043, Q16787, Q16363, 015230, Ρ07942, Ρ55268, Q13751, Ρ11047, Q13753, and Q9Y6N6), a mouse laminin protein (see, for example, UniProt accession numbers Q61789, Q61087, and Q61092), a chimpanzee laminin protein (see, for example, UniProt accession numbers H2QEC7, H2R041, and H2Q0R2), a rat laminin protein (see, for example, UniProt accession numbers D3ZN05, F1LPI5, and F1LRH4), a rabbit laminin protein (see, for example, example, UniProt accession number G1SY40 and A0A0B5JSH0), etc. Methods for identifying orthologs / homologs of laminin proteins in additional species are known to those skilled in the art. In some embodiments, a laminin protein of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89% , at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the sequence of any of the laminin proteins described herein or known in the art. In some embodiments, a polynucleotide of the present disclosure encodes a human laminin protein, such as a human laminin alpha-1 subunit (LamA1) polypeptide (see, for example, UniProt accession number P25391), a human laminin alpha-1 subunit polypeptide (LamA1), 2 of human laminin (LamA2) (see, for example, UniProt accession number P24043), a human laminin (LamA3) alpha-3 subunit polypeptide (see, for example, UniProt accession number Q16787), a subunit polypeptide human laminin alpha-4 (LamA4) (see, for example, UniProt accession number Q16363), a human laminin alpha-5 (LamA5) subunit polypeptide (see, for example, UniProt accession number 015230), a polypeptide human beta-1 (LamB1) subunit polypeptide (see, for example, UniProt accession number P07942), a human beta-2 (LamB2) subunit polypeptide (see, for example, UniProt accession number P55268), a human beta-3 (LamB3) human (see, for example, UniProt accession number Q13751), a human gamma-1 subunit (LamC1) polypeptide (see, for example, UniProt accession number P11047), a human gamma-2 (LamC2) subunit polypeptide (see, for example, UniProt accession number Q13753), a gamma subunit polypeptide -3 (LamC3) human (see, for example, UniProt accession number Q9Y6N6), etc. In some embodiments, a polynucleotide of the present disclosure encodes a human LamA3 polypeptide. In some embodiments, a polynucleotide encoding a human LamA3 polypeptide is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87 %, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97 %, at least 98%, at least 99%, or 100% sequence identity to the sequence of SEQ. ID. NO.: 57. In some embodiments, a polynucleotide encoding a human LamA3 polypeptide is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 57. In some embodiments, a polynucleotide encoding a human LamA3 polypeptide is a polynucleotide encoding an N-terminal truncation, a C-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 57. The N-terminal truncations, the O-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 750, al c / CLnn / Lznz / q / Yi minus 1000, at least 1250 , at least 1500, at least 1750, at least 2000, at least 2250, at least 2500, at least 2750, at least 3000, at least 3250, but less than 3333 consecutive amino acids of SEQ. ID. NO.: 57. In some embodiments, a polynucleotide of the present disclosure encodes a human LamB3 polypeptide. In some embodiments, a polynucleotide encoding a human LamB3 polypeptide is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87 %, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97 %, at least 98%, at least 99%, or 100% sequence identity to the sequence of SEQ. ID. NO.: 58. In some embodiments, a polynucleotide encoding a human LamB3 polypeptide is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 58. In some embodiments, a polynucleotide encoding a LamB3 polypeptide is a polynucleotide encoding an N-terminal truncation, a C-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 58. The N-terminal truncations, C-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 600, at least 700, at least 800, at least 900, at least 1000, at least 1100, but less than 1172 consecutive amino acids of SEQ. ID. NO.: 58. In some embodiments, a polynucleotide of the present disclosure encodes a human LamC2 polypeptide. In some embodiments, a polynucleotide encoding a human LamC2 polypeptide is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87 %, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97 %, at least 98%, at least 99%, or 100% sequence identity to the sequence of SEQ. ID. NO.: 59. In some embodiments, a polynucleotide encoding a human LamC2 polypeptide is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 59. In some embodiments, a polynucleotide encoding a LamC2 polypeptide is a polynucleotide encoding an N-terminal truncation, an O-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 59. N-terminal truncations, O-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 600, at least 700, at least 800, at least 900, at least 1000, at least 1100, but less than 1193 consecutive amino acids of SEQ. ID. NO.: 59. Neuromodulatory proteins In some embodiments, the present disclosure refers to one or more polynucleotides that encode a full-length neuromodulatory protein or any isoform or part thereof. A polynucleotide of the present disclosure can encode any neuromodulatory protein from any species known in the art, including, for example, c / CLnn / Lznz / q / Yi, a clostridium botulinum protein (see, for example, UniProt accession numbers PODPIO, Q45894, P0DPI1, P10844 and B1INP5), etc. Methods for identifying orthologs / homologs of neuromodulatory proteins in additional species are known to those skilled in the art. In some embodiments, a neuromodulatory protein of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the sequence of any of the neuromodulatory proteins described herein or known in the art. In some embodiments, a polynucleotide of the present disclosure encodes a clostridium bolutinum neuromodulatory protein. In some embodiments, a polynucleotide of the present disclosure encodes a clostridium botulinum neurotoxin type A protein. In some embodiments, a polynucleotide encoding a clostridium botulinum neurotoxin type A protein is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86% , at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% , at least %, at least 98%, at least 99% or 100% sequence identity to the sequence of SEQ. ID. NO.: 60. In some embodiments, a polynucleotide encoding a clostridium botulinum neurotoxin type A protein is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 60. In some embodiments, a clostridium botulinum neurotoxin type A protein of the present disclosure comprises an alanine to valine mutation at a position corresponding to position 27 of SEQ. ID. NO.: 60. In some embodiments, a polynucleotide encoding a clostridium botulinum neurotoxin type A protein is a polynucleotide encoding an N-terminal truncation, an O-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 60. The N-terminal truncations, O-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 600, at least 700, at least 800, at least 900, at least 1000, at least 1100, at least 1200, but less than 1296 consecutive amino acids of SEQ. ID. NO.: 60. In some embodiments, a polynucleotide of the present disclosure encodes a clostridium botulinum neurotoxin type B protein. In some embodiments, a polynucleotide encoding a clostridium botulinum neurotoxin type B protein is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86% , at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% , at least %, at least 98%, at least 99% or 100% sequence identity to the sequence of SEQ. ID. NO.: 61. In some embodiments, a polynucleotide encoding a clostridium botulinum neurotoxin type B protein is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 61. In some embodiments, a polynucleotide encoding a clostridium botulinum neurotoxin type B protein is c / CLnn / Lznz / q / Yi, a polynucleotide encoding an N-terminal truncation, a C-terminal truncation, or a fragment of the amino acid sequence. from SEQ. ID. NO.: 61. The N-terminal truncations, C-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 600, at least 700, at least 800, at least 900, at least 1000, at least 1100, at least 1200, but less than 1291 consecutive amino acids of SEQ. ID. NO.: 61. fibrillin proteins In some embodiments, the present disclosure refers to one or more polynucleotides encoding a full-length fibrillin protein or any isoform or part thereof. A polynucleotide of the present disclosure can encode any fibrillin protein from any suitable species known in the art, including, for example, a human fibrillin protein (see, for example, UniProt accession numbers P35555, P35556, and Q75N90), a protein mouse fibrillin (see, for example, UniProt accession numbers Q61554 and Q61555), a chimpanzee fibrillin protein (see, for example, UniProt accession numbers A0A2I3RTE4 and K7CZX0), a rat fibrillin protein (see, for example, example, UniProt accession number G3V9M6 and F1M5Q4), a rabbit fibrillin protein (see, for example, UniProt accession number G1SKM2, G1SUS5 and G1T1H4), etc. Methods for identifying fibrillin protein orthologs / homologs in additional species are known to those skilled in the art. In some embodiments, a fibrillin protein of the present disclosure comprises a sequence with at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89% , at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to the sequence of any of the fibrillin proteins described herein or known in the art. In some embodiments, a polynucleotide of the present disclosure encodes a human fibrillin protein. In some embodiments, a polynucleotide of the present disclosure encodes a human fibrillin-1 protein. In some embodiments, a polynucleotide encoding a human fibrillin-1 protein is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86%, at at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least at least 97%, at least 98%, at least 99%, or 100% sequence identity to the sequence of SEQ. ID. NO.: 62. In some embodiments, a polynucleotide encoding a human fibrillin-1 protein is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 62. In some embodiments, a polynucleotide encoding a fibrillin-1 protein is a polynucleotide encoding an N-terminal truncation, an O-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 62. N-terminal truncations, O-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 750, at least 1000, at least 1250, at least 1500, at least 1750, at least 2000, at least 2250, at least 2500, at least 2750, but c / CLnn / Lznz / q / Yi less than 2871 consecutive amino acids of SEQ. ID. NO.: 62. In some embodiments, a polynucleotide of the present disclosure encodes a human fibrillin-2 protein. In some embodiments, a polynucleotide encoding a human fibrillin-2 protein is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86%, at at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least at least 97%, at least 98%, at least 99%, or 100% sequence identity to the sequence of SEQ. ID. NO.: 63. In some embodiments, a polynucleotide encoding a human fibrillin-2 protein is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 63. In some embodiments, a polynucleotide encoding a fibrillin-2 protein is a polynucleotide encoding an N-terminal truncation, a C-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 63. The N-terminal truncations, C-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 750, at least 1000, at least 1250, at least 1500, at least 1750, at least 2000, at least 2250, at least 2500, at least 2750, but less than 2912 consecutive amino acids of SEQ. ID. NO.: 63. In some embodiments, a polynucleotide of the present disclosure encodes a human fibrillin-3 protein. In some embodiments, a polynucleotide encoding a human fibrillin-3 protein is a polynucleotide encoding a polypeptide comprising an amino acid sequence with at least 75%, at least 80%, at least 85%, at least 86%, at at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least at least 97%, at least 98%, at least 99%, or 100% sequence identity to the sequence of SEQ. ID. NO.: 64. In some embodiments, a polynucleotide encoding a human fibrillin-3 protein is a polynucleotide encoding a polypeptide comprising the amino acid sequence of SEQ. ID. NO.: 64. In some embodiments, a polynucleotide encoding a fibrillin-3 protein is a polynucleotide encoding an N-terminal truncation, an O-terminal truncation, or a fragment of the amino acid sequence of SEQ. ID. NO.: 64. The N-terminal truncations, O-terminal truncations or fragments may comprise at least 10, at least 12, at least 14, at least 16, at least 18, at least 20, at least 30, at least 40, at least 50, at least 75, at least 100, at least 200, at least 300, at least 400, at least 500, at least 750, at least 1000, at least 1250, at least 1500, at least 1750, at least 2000, at least 2250, at least 2500, at least 2750, but less than 2809 consecutive amino acids of SEQ. ID. NO.: 64. Examples of cosmetic polypeptides In some embodiments, one or more cosmetic proteins of the present disclosure (eg, a first cosmetic protein, another cosmetic protein, a further cosmetic protein, and / or a second cosmetic protein) comprises an amino acid sequence with at least 80%, at at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least least 99% or 100% c / CLnn / Lznz / q / Yi sequence identity to an amino acid sequence selected from SEQ. ID. NO.: 15-21 or 53-64. In some embodiments, one or more cosmetic proteins of the present disclosure (eg, a first cosmetic protein, another cosmetic protein, a further cosmetic protein, and / or a second cosmetic protein) comprise a sequence selected from SEQ. ID. NO.: 15-21 or 53-64. In some embodiments, one or more cosmetic proteins of the present disclosure (for example, a first cosmetic protein, another cosmetic protein, a further cosmetic protein, and / or a second cosmetic protein) comprises an amino acid sequence with at least 80%, at at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least least 99% or 100% sequence identity to an amino acid sequence selected from SEQ. ID. NO.: 15-21, 53-54 or 57-59. In some embodiments, one or more cosmetic proteins of the present disclosure (eg, a first cosmetic protein, another cosmetic protein, a further cosmetic protein, and / or a second cosmetic protein) comprise a sequence selected from SEQ. ID. NO.: 15-21, 53-54 or 57-59. first polynucleotides In some embodiments, the present disclosure refers to a recombinant nucleic acid comprising a first polynucleotide encoding a first polypeptide comprising a first cosmetic protein. The first cosmetic protein can be any of the cosmetic proteins described herein or known in the art, including, for example, a collagen protein, a fibronectin, an elastin, a lumican, a vitronectin / vitronectin receptor, a laminin , a neuromodulator, a fibrillin, etc. In some embodiments, the first cosmetic protein is a structural extracellular matrix protein (eg, collagen, elastin, fibronectin, laminin, fibrillin, etc.). In some embodiments, the first cosmetic protein is a collagen, elastin, fibronectin, or laminin (eg, a human collagen, elastin, fibronectin, or laminin). In some embodiments, a recombinant nucleic acid of the present disclosure comprises a copy of the first polynucleotide. In some embodiments, a recombinant nucleic acid of the present disclosure comprises two or more (eg, two or more, three or more, four or more, five or more, ten or more, etc.) copies of the first polynucleotide. In some embodiments, a recombinant nucleic acid of the present disclosure comprises two copies of the first polynucleotide. In some embodiments, the first cosmetic protein is a first human collagen protein. The first human collagen protein can be any of the human collagen proteins described herein or known in the art. In some embodiments, the first human collagen protein is selected from COL1-1, COL1-2, COL2, COL3, COL4-1, COL4-2, COL4-3, COL4-4, COL4-5, COL4-6, COL5. -1, COL5-2, COL5-3, COL6-1, COL6-2, COL6-3, COL6-4, COL6-5, COL6-6, COL7, COL8, COL9-1, COL9-2, COL9-3 , COL10, COL11-1, COL11-2, COL12, COL13, COL14, COL15, COL16, COL17, COL18, COL19, COL20, COL21, COL22, COL23, COL24, COL25, COL26, COL27 or COL28. In some embodiments, the first human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-1, COL4-2, COL6-1, COL7, or COL17. In some embodiments, the first human collagen protein is COL1-1. In some embodiments, the first human collagen protein is COL1-2. In some c / CLnn / Lznz / q / Yi modalities, the first human collagen protein is C0L3. In some embodiments, the first human collagen protein is COL4-1. In some embodiments, the first human collagen protein is COL4-2. In some embodiments, the first human collagen protein is COL6-1. In some embodiments, the first human collagen protein is C0L7. In some embodiments, the first human collagen protein is not C0L7. In some embodiments, the first human collagen protein is C0L17. In some embodiments, the first polypeptide consists essentially of the first cosmetic protein. In some embodiments, the first polypeptide consists of the first cosmetic protein. In some embodiments, the first polypeptide is the first cosmetic protein. chimeric polyeptides In some embodiments, the first polypeptide is a chimeric polypeptide comprising the first cosmetic protein. In some embodiments, the first polypeptide is a chimeric polypeptide comprising the first cosmetic protein and another cosmetic protein. In some embodiments, the chimeric polypeptide comprises a linker polypeptide that links the first cosmetic protein and the other cosmetic protein. In some embodiments, the chimeric polypeptide comprises, from the n-terminus to the c-terminus, the first cosmetic protein-the linker polypeptide-the other cosmetic protein. The first cosmetic protein and / or the other cosmetic protein can be any of the cosmetic proteins described herein or known in the art, including, for example, a collagen protein, a fibronectin, an elastin, a lumican, a vitronectin / a vitronectin receptor, a laminin, a neuromodulator, a fibrillin, etc. In some embodiments, the first cosmetic protein and / or the other cosmetic protein is a structural extracellular matrix protein (eg, collagen, elastin, fibronectin, laminin, fibrillin, etc.). In some embodiments, the first cosmetic protein and / or the other cosmetic protein is a collagen, elastin, fibronectin, or laminin (eg, a human collagen, elastin, fibronectin, or laminin). In some embodiments, the first cosmetic protein and the other cosmetic protein are the same. In some embodiments, the first cosmetic protein and the other cosmetic protein are different. In some embodiments, the linker polypeptide is a cleavable linker polypeptide. Any cleavable linker polypeptide known in the art can be used for the chimeric polypeptides of the present disclosure, including, for example, a T2A linker, a P2A linker, an E2A linker, and an F2A linker, etc. In some embodiments, the linker polypeptide is a T2A linker polypeptide. An example of a nucleic acid sequence encoding a T2A linker polypeptide is provided as SEQ. ID. NO.: 24. An exemplary amino acid sequence of a T2A linker polypeptide is provided as SEQ. ID. NO.: 28. In some embodiments, the linker polypeptide is a P2A linker polypeptide. An example of a nucleic acid sequence encoding a P2A linker polypeptide is provided as SEQ. ID. NO.: 25. An exemplary amino acid sequence of a P2A linker polypeptide is provided as SEQ. ID. NO.: 29. In some embodiments, the binding polypeptide is an E2A linker polypeptide. An example of a nucleic acid sequence encoding an E2A linker polypeptide is provided as SEQ. ID. NO.: 26. An example amino acid sequence of an E2A linker polypeptide is provided as SEQ. ID. NO.: 30. In some embodiments, the linker polypeptide is an F2A linker polypeptide. An example of a nucleic acid sequence encoding a c / CLnn / Lznz / q / Yi linker polypeptide F2A is provided as SEQ. ID. NO.: 27. An exemplary amino acid sequence of an F2A linker polypeptide is provided as SEQ. ID. NO.: 31. In some embodiments, the linker polypeptide comprises a sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95% , at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to an amino acid sequence selected from SEQ. ID. NO.: 28-31. In some embodiments, the linker polypeptide comprises a sequence selected from SEQ. ID. NO.: 28 to 31. In some embodiments, the first cosmetic protein is a first collagen protein (eg, a first human collagen protein) and the other cosmetic protein is another collagen protein (eg, another human collagen protein). An example of a nucleic acid sequence encoding a chimeric polypeptide comprising a first human collagen protein, a linker polypeptide, and another human collagen protein is provided in SEQ. ID. NO.: 32. In some embodiments, the first cosmetic protein is a first human collagen protein and the other cosmetic protein is another human collagen protein. The other human collagen protein can be any of the human collagen proteins described herein or known in the art. In some embodiments, the other human collagen protein is selected from COL1-1, COL1-2, COL2, COL3, COL4-1, COL4-2, COL4-3, COL4-4, COL4-5, COL4-6, COL5 -1, COL5-2, COL5-3, COL6-1, COL6-2, COL6-3, COL6-4, COL6-5, COL6-6, COL7, COL8, COL9-1, COL9-2, COL9-3 , COL10, COL11-1, COL11-2, COL12, COL13, COL14, COL15, COL16, COL17, COL18, COL19, COL20, COL21, COL22, COL23, COL24, COL25, COL26, COL27 or COL28. In some embodiments, the other human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-1, COL4-2, COL6-1, COL7, or COL17. In some embodiments, the other human collagen protein is COL1-1. In some embodiments, the other human collagen protein is COL1-2. In some embodiments, the other human collagen protein is COL3. In some embodiments, the other human collagen protein is COL4-1. In some embodiments, the other human collagen protein is COL4-2. In some embodiments, the other human collagen protein is COL6-1. In some embodiments, the other human collagen protein is COL7. In some embodiments, the other human collagen protein is not COL7. In some embodiments, the other human collagen protein is COL17. In some embodiments, the first human collagen protein and the other human collagen protein are the same. In some embodiments, the first human collagen protein and the other human collagen protein are different. In some embodiments, the first human collagen protein is COL1-1 and the other human collagen protein is selected from COL1-2, COL3, COL4-1, COL4-2, COL6-1, COL7, or COL17. In some embodiments, the first human collagen protein is COL1-1 and the other human collagen protein is COL1-2. In some embodiments, the first human collagen protein is COL1-1 and the other human collagen protein is COL3. In some embodiments, the first human collagen protein is COL1-2 and the other human collagen protein is COL1-1, COL3, COL4-1, COL4-2, COL6-1, COL7, or COL17. In some embodiments, the first human collagen protein is COL1-2 and the other human collagen protein is COL1-1. In some embodiments, the first human collagen protein is COL3 and the other human collagen protein is c / CLnn / Lznz / q / Yi selected from C0L1-1, C0L1-2, C0L4-1, COL4-2, C0L6-1 , C0L7 or C0L17. In some embodiments, the first human collagen protein is C0L4-1 and the other human collagen protein is COL1-1, COL1-2, COL3, COL4-2, COL6-1, COL7, or COL17. In some embodiments, the first human collagen protein is COL4-1 and the other human collagen protein is COL4-2. In some embodiments, the first human collagen protein is COL6-1 and the other human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-1, COL4-2, COL7, or COL17. In some embodiments, the first human collagen protein is COL7 and the other human collagen protein is COL1-1, COL1-2, COL3, COL4-1, COL4-2, COL6-1, or COL17. In some embodiments, the first human collagen protein is COL17 and the other human collagen protein is COL1-1, COL1-2, COL3, COL4-1, COL4-2, COL6-1, or COL7. In some embodiments, the first cosmetic protein is a first laminin protein (eg, a first human laminin protein) and the other cosmetic protein is another laminin protein (eg, another human laminin protein). In some embodiments, the first cosmetic protein is a first human laminin protein and the other cosmetic protein is another human laminin protein. The other human laminin protein can be any of the human laminin proteins described herein or known in the art. In some embodiments, the first human laminin protein is a human LamA3 polypeptide and the other human laminin protein is a human LamB3 polypeptide. In some embodiments, the first human laminin protein is a human LamA3 polypeptide and the other human laminin protein is a human LamC2 polypeptide. In some embodiments, the first human laminin protein is a human LamB3 polypeptide and the other human laminin protein is a human LamC2 polypeptide. In some embodiments, the first polynucleotide encodes a monocistronic mRNA. In some embodiments, the monocistronic mRNA comprises an open reading frame (ORF) that encodes the first polypeptide. In some embodiments, the first polynucleotide encodes a polycistronic mRNA. In some embodiments, the polycistronic mRNA comprises an open reading frame (ORF) that encodes the first polypeptide. polycistronic mRNA In some embodiments, the first polynucleotide encodes a polycistronic mRNA. In some embodiments, the polycistronic mRNA comprises an open reading frame (ORF) that encodes the first polypeptide. In some embodiments, the first polynucleotide encodes a polycistronic mRNA comprising: 1) a first open reading frame (ORF) encoding the first polypeptide and 2) a second open reading frame (ORF) encoding an additional cosmetic protein. In some embodiments, the polycistronic mRNA further comprises an intraribosome entry site (IRES) that separates the first ORF and the second ORF. In some embodiments, the polycistronic mRNA comprises, from 5' to 3', the first ORF encoding the first polypeptide-the IRES-the second ORF encoding the additional cosmetic protein. The first polypeptide can be any of the first polypeptides described herein. The additional cosmetic protein can be any of the cosmetic proteins described herein or known in the art, including, for example, a collagen protein, a fibronectin, an elastin, a lumican, a vitronectin / vitronectin receptor, a laminin , a neuromodulator, a fibrillin, etc. In some embodiments, the c / CLnn / Lznz / q / Yi additional cosmetic protein is a structural extracellular matrix protein (eg, collagen, elastin, fibronectin, laminin, fibrillin, etc.). In some embodiments, the additional cosmetic protein is a collagen, elastin, fibronectin, or laminin (eg, human collagen, elastin, fibronectin, or laminin). Any suitable IRES known in the art can be used for the polycistronic mRNAs of the present disclosure, including, for example, a virus-derived IRES (eg, an IRES derived from a poliovirus, rhinovirus, encephalomyocarditis virus (EMCV), foot-and-mouth disease virus, hepatitis C virus, classical swine fever virus, rous sarcoma virus, human immunodeficiency virus, Cricket's palsy virus, Kaposi's sarcoma-associated herpes virus, etc.), an IRES derived from Cellular mRNA (for example, an IRES derived from growth factor mRNA, such as fibroblast growth factor 2, platelet-derived growth factor B, and vascular endothelial growth factor; an IRES derived from transcription factor mRNA , such as NF-kB repression factor, antennapedia, and ultrabithorax; an IRES derived from oncogenic mRNA, such as c-myc, pim-1, and protein kinase p58PITSLRE, etc.), a synthetic IRES (for example, an IRES C P148) and others (see, for example, Mokrejs et al. (2007) A Bioinformatical Approach to the Analysis of Viral and Cellular Internal Ribosome Entry Sites. Columbus F publishers. New Messenger RNA Research Communications. Hauppauge, NY: Nova Science Publishers; pp. 133-166). In some embodiments, the IRES is a CP148 IRES. An example of a nucleic acid sequence encoding a CP148 IRES is provided as SEQ. ID. NO.: 22. In some modalities, the IRES is an IRES EMCV. An example of a nucleic acid sequence encoding an EMCV IRES is provided as SEQ. ID. NO.: 23. In some embodiments, the nucleic acid sequence encoding the IRES comprises a sequence with at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94 %, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to a nucleic acid sequence selected from SEQ. ID. NO.: 22 or SEQ. ID. NO.: 23. In some embodiments, the nucleic acid sequence encoding the IRES comprises the sequence SEQ. ID. NO.: 22 or SEQ. ID. NO.: 23. In some embodiments, the first polypeptide is a first collagen protein (eg, a first human collagen protein) and the additional cosmetic protein is an additional collagen protein (eg, an additional human collagen protein). An example of a nucleic acid encoding a polycistronic mRNA comprising a first ORE, an IRES, and a second ORF is provided as SEQ. ID. NO.: 33 or SEQ. ID. NO.: 34. The additional human collagen protein can be any of the human collagen proteins described herein. In some embodiments, the additional human collagen protein is selected from COL1-1, COL1-2, COL2, COL3, COL4-1, COL4-2, COL4-3, COL4-4, COL4-5, COL4-6, COL5. -1, COL5-2, COL5-3, COL6-1, COL6-2, COL6-3, COL6-4, COL6-5, COL6-6, COL7, COL8, COL9-1, COL9-2, COL9-3 , COL10, COL11-1, COL11-2, COL12, COL13, COL14, COL15, COL16, COL17, COL18, COL19, COL20, COL21, COL22, COL23, COL24, COL25, COL26, COL27 or COL28. In some embodiments, the additional human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-1, COL4-2, COL6-1, COL7, or COL17. In some embodiments, the additional human collagen protein is COL1-1. In some embodiments, the additional human collagen protein is COL1-2. In some embodiments, the additional human collagen protein is COL3. In some embodiments, the additional human collagen protein is COL4-1. c / CLnn / Lznz / q / YL In some embodiments, the additional human collagen protein is COL4-2. In some embodiments, the additional human collagen protein is COL6-1. In some embodiments, the additional human collagen protein is COL7. In some embodiments, the additional human collagen protein is not C0L7. In some embodiments, the additional human collagen protein is COL17. In some embodiments, the first human collagen protein and the additional human collagen protein are the same. In some embodiments, the first human collagen protein and the additional human collagen protein are different. In some embodiments, the first human collagen protein is C0L1-1 and the additional human collagen protein is selected from C0L1-2, C0L3, COL4-1, COL4-2, COL6-1, C0L7, or C0L17. In some embodiments, the first human collagen protein is C0L1-1 and the additional human collagen protein is COL1-2. In some embodiments, the first human collagen protein is COL1-1 and the additional human collagen protein is COL3. In some embodiments, the first human collagen protein is COL1-2 and the additional human collagen protein is selected from COL1-1, COL3, COL4-1, COL4-2, COL6-1, COL7, or COL17. In some embodiments, the first human collagen protein is COL1-2 and the additional human collagen protein is COL1-1. In some embodiments, the first human collagen protein is COL3 and the additional human collagen protein is selected from COL1-1, COL1-2, COL4-1, COL4-2, COL6-1, COL7, or COL17. In some embodiments, the first human collagen protein is COL4-1 and the additional human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-2, COL6-1, COL7, or COL17. In some embodiments, the first human collagen protein is COL4-1 and the additional human collagen protein is COL4-2. In some embodiments, the first human collagen protein is COL6-1 and the additional human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-1, COL4-2, COL7, or COL17. In some embodiments, the first human collagen protein is C0L7 and the additional human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-1, COL4-2, COL6-1, or COL17. In some embodiments, the first human collagen protein is C0L17 and the additional human collagen protein is selected from COL1-1, COL1-2, COL3, C0L4-1, COL4-2, COL6-1, or COL7. In some embodiments, the first polypeptide is a first collagen protein (eg, a first human collagen protein) and the additional cosmetic protein is an additional collagen protein (eg, an additional human collagen protein). In some embodiments, the first polypeptide is a first laminin protein (eg, a first human laminin protein) and the additional cosmetic protein is an additional laminin protein (eg, an additional human laminin protein). In some embodiments, the first polypeptide is a first human laminin protein and the additional cosmetic protein is an additional human laminin protein. The additional human laminin protein can be any of the human laminin proteins described herein or known in the art. In some embodiments, the first human laminin protein is a human LamA3 polypeptide and the additional human laminin protein is a human LamB3 polypeptide. In some embodiments, the first human laminin protein is a human LamA3 polypeptide and the additional human laminin protein is a human LamC2 polypeptide. In some embodiments, the first human laminin protein is a c / CLnn / Lznz / q / Yi polypeptide. Human LamB3 and the additional human laminin protein is a human LamC2 polypeptide. second polynucleotides In some embodiments, the present disclosure refers to a recombinant nucleic acid that further comprises a second polynucleotide encoding a second cosmetic protein. The second cosmetic protein can be any of the cosmetic proteins described herein or known in the art, including, for example, a collagen protein, a fibronectin, an elastin, a lumican, a vitronectin / vitronectin receptor, a laminin , a neuromodulator, a fibrillin, etc. In some embodiments, the second cosmetic protein is a structural extracellular matrix protein (eg, a collagen, an elastin, a fibronectin, a laminin, a fibrillin, etc.). In some embodiments, the second cosmetic protein is a collagen, elastin, fibronectin, or laminin (eg, a human collagen, elastin, fibronectin, or laminin). In some embodiments, the first and second cosmetic proteins are the same. In some embodiments, the first and second cosmetic proteins are different. In some embodiments, the recombinant nucleic acid comprises a copy of the second polynucleotide. In some embodiments, the recombinant nucleic acid comprises two or more (eg, two or more, three or more, four or more, five or more, ten or more, etc.) copies of the second polynucleotide. In some embodiments, the recombinant nucleic acid comprises two copies of the second polynucleotide. In some embodiments, the second cosmetic protein is a collagen protein. In some embodiments, the second cosmetic protein is a second human collagen protein. The second human collagen protein can be any of the human collagen proteins described herein. In some embodiments, the second human collagen protein is selected from COL1-1, COL1-2, COL2, COL3, COL4-1, COL4-2, COL4-3, COL4-4, COL4-5, COL4-6, COL5. -1, COL5-2, COL5-3, COL6-1, COL6-2, COL6-3, COL6-4, COL6-5, COL6-6, COL7, COL8, COL9-1, COL9-2, COL9-3 , COL10, COL11-1, COL11-2, COL12, COL13, COL14, COL15, COL16, COL17, COL18, COL19, COL20, COL21, COL22, COL23, COL24, COL25, COL26, COL27 or COL28. In some embodiments, the second human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-1, COL6-1, COL7, or COL17. In some embodiments, the second human collagen protein is COL1-1. In some embodiments, the second human collagen protein is COL1-2. In some embodiments, the second human collagen protein is COL3. In some embodiments, the second human collagen protein is COL4-1. In some embodiments, the second human collagen protein is COL4-2. In some embodiments, the second human collagen protein is COL61. In some embodiments, the second human collagen protein is COL7. In some embodiments, the second human collagen protein is not COL7. In some embodiments, the second human collagen protein is COL17. In some embodiments, the first polynucleotide encodes a first collagen protein and the second polynucleotide encodes a second collagen protein. In some embodiments, the first polynucleotide encodes a first human collagen protein and the second polynucleotide encodes a second human collagen protein. In some embodiments, the first human collagen protein (encoded by the first polynucleotide) and the second human collagen protein (encoded by the second polynucleotide) are the same. In some embodiments, the first human collagen protein (encoded by the first polynucleotide) and the second human c / CLnn / Lznz / q / Yi collagen protein (encoded by the second polynucleotide) are different. In some embodiments, the first human collagen protein is COL1-1 and the second human collagen protein is selected from COL1-2, COL3, COL4-1, COL4-2, COL6-1, COL7, or COL17. In some embodiments, the first human collagen protein is C0L1-1 and the second human collagen protein is COL1-2. In some embodiments, the first human collagen protein is COL1 -1 and the second human collagen protein is COL3. In some embodiments, the first human collagen protein is C0L1-2 and the second human collagen protein is selected from COL1-1, C0L3, COL4-1, COL4-2, COL6-1, C0L7, or C0L17. In some embodiments, the first human collagen protein is COL1-2 and the second human collagen protein is C0L1-1. In some embodiments, the first human collagen protein is C0L3 and the second human collagen protein is selected from COL1-1, COL1-2, COL4-1, COL4-2, COL6-1, COL7, or C0L17. In some embodiments, the first human collagen protein is COL4-1 and the second human collagen protein is selected from COL1-2, COL1-2, COL3, COL4-2, COL6-1, COL7, or COL17. In some embodiments, the first human collagen protein is COL4-1 and the second human collagen protein is COL4-2. In some embodiments, the first human collagen protein is COL6-1 and the second human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-1, COL4-2, COL7, or COL17. In some embodiments, the first human collagen protein is C0L7 and the second human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-1, COL4-2, COL6-1, or COL17. In some embodiments, the first human collagen protein is COL17 and the second human collagen protein is selected from COL1-1, COL1-2, COL3, COL4-1, COL4-2, COL6-1, or COL7. In some embodiments, the first polynucleotide encodes a first laminin protein (eg, a first human laminin protein) and the second polynucleotide encodes a second laminin protein (eg, a second human laminin protein). In some embodiments, the first polynucleotide encodes a first human laminin polypeptide and the second polynucleotide encodes a second human laminin protein. The second human laminin protein can be any of the human laminin proteins described herein or known in the art. In some embodiments, the first human laminin protein is a human LamA3 polypeptide and the second human laminin protein is a human LamB3 polypeptide. In some embodiments, the first human laminin protein is a human LamA3 polypeptide and the second human laminin protein is a human LamC2 polypeptide. In some embodiments, the first human laminin protein is a human LamB3 polypeptide and the second human laminin protein is a human LamC2 polypeptide. recombinant nucleic acids In some embodiments, the present disclosure refers to recombinant nucleic acids comprising any one or more polynucleotides described herein. In some embodiments, the recombinant nucleic acid comprises a copy of the first polynucleotide. In some embodiments, the recombinant nucleic acid comprises two copies of the first polynucleotide. In some embodiments, the recombinant nucleic acid comprises a copy of the first polynucleotide and a copy of the second polynucleotide. In some embodiments, the recombinant nucleic acid comprises one copy of the first polynucleotide and two copies of the second polynucleotide. In some c / CLnn / Lznz / q / Yi embodiments, the recombinant nucleic acid comprises two copies of the first polynucleotide and one copy of the second polynucleotide. In some embodiments, the recombinant nucleic acid comprises two copies of the first polynucleotide and two copies of the second polynucleotide. In some embodiments, the recombinant nucleic acid is a vector (eg, an expression vector, a display vector, etc.). In some embodiments, the vector is a DNA vector or an RNA vector. In general, vectors suitable for maintaining, propagating and / or expressing polynucleotides can be used to produce one or more polypeptides in a subject. Examples of suitable vectors may include, for example, plasmids, cosmids, episomes, transposons, and viral vectors (for example, adenoviral vectors, adeno-associated viral vectors, vaccinia viral vectors, Sindbis viral vectors, measles vectors, viral vectors herpes, lentiviral vectors, retroviral vectors, etc.). In some embodiments, the vector is a herpes viral vector. In some embodiments, the vector is capable of autonomous replication in a host cell. In some embodiments, the vector is not capable of autonomous replication in a host cell. In some embodiments, the vector can integrate into host DNA. In some embodiments, the vector cannot integrate into a host DNA (eg, it is found in the episome). Methods for making vectors with one or more polynucleotides of interest are known to those skilled in the art and these include, for example, chemical synthesis or artificial manipulation of isolated nucleic acid segments (for example, through genetic alteration techniques). In some embodiments, a recombinant nucleic acid of the present disclosure is a herpes simplex virus (HSV) amplicon. Herpes virus amplicons, including structural features and methods for making them, are generally known to those skilled in the art (see, for example, de Silva S. and Bowers W. Herpes Virus Amplicon Vectors.” Viruses 2009, 1 , 594-629). In some embodiments, the herpes simplex virus amplicon is an HSV-1 amplicon. In some embodiments, the herpes simplex virus amplicon is a hybrid HSV-1 amplicon. Examples of HSV-1 hybrid amplicons may include, but are not limited to, HSV / AAV hybrid amplicons, HSV / EBV hybrid amplicons, HSV / EBV / RV hybrid amplicons, and / or YAS\ÍISIeep¡ng hybrid amplicons. Beauty. In some embodiments, the amplicon is a hybrid HSV / AAV amplicon. In some modalities, the amplicon is a hybrid amplicon of HSVISIeeping Beauty. In some embodiments, a recombinant nucleic acid of the present disclosure is a recombinant herpes virus genome. The recombinant herpes virus genome may be a recombinant genome of any member of the Herpesviridae family of DNA viruses known in the art, including, for example, a herpes simplex virus recombinant genome, a varicella zoster virus recombinant genome , a recombinant human cytomegalovirus genome, a recombinant herpesvirus 6A genome, a recombinant herpesvirus 6B genome, a recombinant herpesvirus 7 genome, a recombinant Kaposi sarcoma-associated herpesvirus genome, and any combination or any derivative thereof. In some embodiments, the recombinant herpesvirus genome comprises one or more (for example, one or more, two or more, three or more, four or more, five or more, six or more, seven or more, eight or more , nine or more, ten or more, etc.) inactivating mutations. In some embodiments, the inactivating mutation(s) is found in one or more (for example, one or more, two or more, three or more, four or more, five or more, six or more, seven or more, eight or more). more, nine or more, ten or c / CLnn / Lznz / q / Yi more) herpes virus genes. In some embodiments, the recombinant herpesvirus genome is attenuated (eg, compared to a corresponding wild-type herpesvirus genome). In some embodiments, the recombinant herpes virus genome is replication competent. In some embodiments, the recombinant herpes virus genome is replication defective. In some embodiments, the recombinant nucleic acid is a recombinant herpes simplex virus (HSV) genome. In some embodiments, the recombinant herpes simplex virus genome is a recombinant herpes simplex virus type 1 (HSV-1) genome, a recombinant herpes simplex virus type 2 (HSV-2) genome, or any derivative thereof. In some embodiments, the recombinant herpes simplex virus genome is a recombinant HSV-1 genome. In some embodiments, the recombinant herpes simplex virus genome is replication competent. In some embodiments, the recombinant herpes simplex virus genome is replication defective. In some embodiments, the recombinant herpes simplex virus genome comprises one or more (for example, one or more, two or more, three or more, four or more, five or more, six or more, seven or more, eight or more, nine or more, ten or more, etc.) inactivating mutations. In some embodiments, the inactivating mutation(s) is found in one or more (for example, one or more, two or more, three or more, four or more, five or more, six or more, seven or more, eight or more). more, nine or more, ten or more) herpes simplex virus genes. As used herein, an "inactivating mutation" can refer to any mutation that generates a gene product or region (RNA or protein) with reduced, undetectable, or eliminated amount and / or function (for example, compared to with a corresponding sequence without the inactivating mutation). Examples of knockout mutations may include, but are not limited to, deletions, insertions, point mutations, and rearrangements in the transcriptional control sequences (promoters, enhancers, insulators, etc.) and / or coding sequences of a specific gene or region. . Any suitable method for measuring the amount of a gene product or region known in the art can be used, including, for example, qPCR, Northern blots, RNAseq, Western blots, ELISA, etc. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in at least one, at least two, at least three, at least four, at least five, at least six, at least seven, or all eight genes of the herpes simplex virus. herpes simplex virus infected cell protein (or infected cell polypeptide) (ICP) 0, ICP4, ICP22, ICP27, ICP47, thymidine kinase (tk), extensive unique region (UL) 41 and / or UL55. In some embodiments, the recombinant herpes simplex virus genome does not comprise an inactivating mutation in the ICP34.5 and / or ICP47 herpes simplex virus genes (eg, to prevent production of an immune-stimulating virus). In some embodiments, the recombinant herpes simplex virus genome does not comprise an inactivating mutation in the ICP34.5 herpes simplex virus gene (one or both copies). In some embodiments, the recombinant herpes simplex virus genome does not comprise an inactivating mutation in the ICP47 herpes simplex virus gene. In some embodiments, the recombinant herpes simplex virus genome does not comprise an inactivating mutation in the ICP34.5 (one or both copies) and ICP47 herpes simplex virus genes. In some embodiments, the recombinant herpes simplex virus genome is not oncolytic. In some embodiments, the recombinant herpes simplex virus genome comprises a c / CLnn / Lznz / q / Yi inactivating mutation in the ICPO gene (one or both copies). In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICPO gene (one or both copies) and further comprises an initiation mutation in the ICP4 (one or both copies), ICP22, ICP27 genes. , ICP47, UL41 and / or UL55. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICPO gene (one or both copies) and an inactivating mutation in the ICP4 gene (one or both copies). In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICPO gene (one or both couplets) and an inactivating mutation in the ICP22 gene. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICPO gene (one or both copies) and an inactivating mutation in the UL41 gene. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICPO gene (one or both copies), an inactivating mutation in the ICP4 gene (one or both copies), and an inactivating mutation in the ICP4 gene. the ICP22 gene. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICPO gene (one or both copies), an inactivating mutation in the ICP4 gene (one or both copies), and an inactivating mutation in the ICP4 gene. the UL41 gene. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICPO gene (one or both copies), an inactivating mutation in the ICP22 gene, and an inactivating mutation in the UL41 gene. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICPO gene (one or both copies), an inactivating mutation in the ICP4 gene (one or both copies), an inactivating mutation in the ICP22 gene and an inactivating mutation in the UL41 gene. In some embodiments, the inactivating mutation is a deletion of the coding sequence of the ICPO (one or both copies), ICP4 (one or both copies), ICP22 and / or UL41 genes. In some embodiments, the recombinant herpes simplex virus genome further comprises an inactivating mutation in the ICP27, ICP47 and / or UL55 genes. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP4 gene (one or both copies). In some embodiments, the recombinant herpes complex virus genome comprises an inactivating mutation in ICP4 (one or both copies) and further comprises an inactivating mutation in the ICPO (one or both couplets), ICP22, ICP27, ICP47 genes. , UL41 and / or UL55. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP4 gene (one or both copies) and an inactivating mutation in the ICP22 gene. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP4 gene (one or both copies) and an inactivating mutation in the UL41 gene. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP4 gene (one or both copies), an inactivating mutation in the ICP22 gene, and an inactivating mutation in the UL41 gene. In some embodiments, the knockout mutation is a deletion of the coding sequence of the ICP4 (one or both copies), ICP22 and / or UL41 genes. In some embodiments, the recombinant herpes simplex virus genome further comprises an inactivating mutation in the ICPO, ICP27, ICP47 and / or UL55 genes. In some embodiments, the recombinant herpes simplex virus genome comprises a c / CLnn / Lznz / q / Yi inactivating mutation in the ICP22 gene. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP22 gene and further comprises an inactivating mutation in the ICPO (one or both copies), ICP4 (one or both copies), ICP27 genes. , ICP47, UL41 and / or UL55. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP22 gene and an inactivating mutation in the UL41 gene. In some embodiments, the knockout mutation is a deletion of the coding sequence of the ICP22 and / or UL41 genes. In some embodiments, the recombinant herpes simplex virus genome further comprises an inactivating mutation in the ICPO (one or both copies), ICP4 (one or both copies), ICP27, ICP47, and / or UL55 genes. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP27 gene. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP27 gene and further comprises an inactivating mutation in the ICPO (one or both copies), ICP4 (one or both copies), ICP22 genes. , ICP47, UL41 and / or UL55. In some embodiments, the inactivating mutation is a deletion of the coding sequence of the ICP27 gene. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP47 gene. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP47 gene and further comprises an inactivating mutation in the ICPO (one or both copies), ICP4 (one or both copies), ICP22 genes. , ICP27, UL41 and / or UL55. In some embodiments, the inactivating mutation is a deletion of the coding sequence of the ICP47 gene. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the UL41 gene. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the UL41 gene and further comprises an inactivating mutation in the ICPO (one or both copies), ICP4 (one or both copies), ICP22 genes. , ICP27, ICP47 and / or UL55. In some embodiments, the inactivating mutation is a deletion of the coding sequence of the UL41 gene. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the UL55 gene. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the UL55 gene and further comprises an inactivating mutation in the ICPO (one or both copies), ICP4 (one or both copies), ICP22 genes. , ICP27, ICP47 and / or UL41. In some embodiments, the inactivating mutation is a deletion of the coding sequence of the UL55 gene. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation (eg, a deletion) in the internal repeat (splice) region in the internal long repeat (IRL) regions and Internal Short Repeat (IRS) In some embodiments, inactivation (eg, deletion) of the junction region removes one copy in each of the ICP4 and ICPO genes. In some embodiments, inactivation (eg, deletion) of the junction region further inactivates (eg, deletes) the promoter of the ICP22 and ICP47 genes. If desired, expression of one or both of these genes can be restored by insertion of an immediate early promoter into the recombinant herpes simplex virus genome (see, for example, HUI et al., (1995). Nature 375( 6530): 411-415, Goldsmith et al (1998) J Exp Med c / c i nn / ι znz / zi / Yl· 187(3): 341-348). Without wishing to be bound by theory, it is believed that inactivation (eg, deletion) of the junction region may contribute to the stability of the recombinant herpes simplex virus genome and / or allow the recombinant herpes simplex virus genome to receive more transgenes and / or larger transgenes. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP4 (one or both copies), ICP22 and ICP27 genes. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP4 (one or both copies), ICP27 and UL55 genes. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICP4 (one or both copies), ICP22, ICP27, ICP47 and UL55 genes. In some embodiments, the inactivating mutation in the ICP4 (one or both copies), ICP27 and / or UL55 genes is a deletion of the coding sequence of the ICP4 (one or both copies), ICP27 and / or UL55 genes . In some embodiments, the inactivating mutation in the ICP22 and ICP47 genes is a deletion in the promoter region of the ICP22 and ICP47 genes (for example, the ICP22 and ICP47 coding sequences are intact, but their transcription is not detected). is active). In some embodiments, the recombinant herpes simplex virus genome comprises a coding sequence deletion of the ICP4 (one or more copies), ICP27, and UL55 genes, as well as a deletion in the promoter region of the IPC22 and UL55 genes. ICP47. In some embodiments, the recombinant herpes simplex virus genome further comprises an inactivating mutation in the ICPO and / or UL41 genes. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICPO gene (one or both copies). In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICPO (one or both copies) and ICP4 (one or both copies) genes. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICPO (one or both copies), ICP4 (one or both copies) and ICP22 genes. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICPO (one or both copies), ICP4 (one or both copies), ICP22 and ICP27 genes. In some embodiments, the recombinant herpes simplex virus genome comprises an inactivating mutation in the ICPO (one or both copies), ICP4 (one or both copies), ICP22, ICP27, and UL55 genes. In some embodiments, the inactivating mutation in the ICPO (one or both copies), ICP4 (one or both copies), ICP22, ICP27, and / or UL55 genes comprises a deletion of the coding sequence of the ICPO, ICP4 genes. (one or both copies), ICP22, ICP27 and / or UL55. In some embodiments, the recombinant herpes simplex virus genome further comprises an inactivating mutation in the ICP47 and / or UL41 genes. In some embodiments, a recombinant herpes simplex virus genome comprises one or more polynucleotides of the present disclosure at one, two, three, four, five, six, seven, or more viral gene loci. Examples of suitable viral loci may include, but are not limited to, the ICPO (one or both copies), ICP4 (one or both copies), ICP22, ICP27, ICP47, tk, UL41, and UL55 herpes simplex viral gene loci. . In some embodiments, a recombinant herpes simplex virus genome comprises one or more polynucleotides of the present disclosure at one or both viral loci of the ICP4 gene (eg, a recombinant virus with a first polynucleotide encoding c / c i nn / ι znz / zi / Yl a first human collagen protein at one or both of the ICP4 loci; a recombinant virus with a second polynucleotide encoding a second human collagen protein at one or both of the ICP4 loci, etc.) . In some embodiments, a recombinant herpes simplex virus genome comprises one or more polynucleotides of the present disclosure at the viral ICP22 gene locus (for example, a recombinant virus with a first polynucleotide encoding a first human collagen protein in the ICP22 gene locus). ICP22 locus; a recombinant virus with a second polynucleotide encoding a second human collagen protein at the ICP22 locus, etc.). In some embodiments, a recombinant herpes simplex virus genome comprises one or more polynucleotides of the present disclosure at the UL41 gene viral locus (eg, a recombinant virus with a first polynucleotide encoding a first human collagen protein at the UL41 gene locus). UL41 locus; a recombinant virus with a second polynucleotide encoding a second human collagen protein at the UL41 locus, etc.). In some embodiments, a recombinant herpes simplex virus genome comprises one or more polynucleotides of the present disclosure at one or both of the ICP4 gene viral loci and one or more polynucleotides of the present disclosure at the ICP22 viral locus (eg, a recombinant virus with a first polynucleotide encoding a first human collagen protein at one or both of the ICP4 loci and a second polynucleotide encoding a second human collagen protein at the ICP22 locus; a recombinant virus with a second polynucleotide encoding encoding a second human collagen protein at one or both of the ICP4 loci and a first polynucleotide encoding a first human collagen protein at the ICP22 locus, etc.). In some embodiments, a recombinant herpes simplex virus genome comprises one or more polynucleotides of the present disclosure at one or both of the viral ICP4 gene loci and one or more polynucleotides of the present disclosure at the UL41 locus (eg, a recombinant virus with a first polynucleotide encoding a first human collagen protein at one or both of the ICP4 loci and a second polynucleotide encoding a second human collagen protein at the UL41 locus; a recombinant virus with a second polynucleotide encoding a second human collagen protein at one or both of the ICP4 loci and a first polynucleotide encoding a first human collagen protein at the UL41 locus, etc.). In some embodiments, a recombinant herpes simplex virus genome comprises one or more polynucleotides of the present disclosure at one or both of the ICP4 gene viral loci and one or more polynucleotides of the present disclosure at the ICP22 viral locus and one or more polynucleotides of the present disclosure at the UL41 viral locus (for example, a recombinant virus with a first polynucleotide encoding a first human collagen protein at one or both of the ICP4 loci and a second polynucleotide encoding a second collagen protein at the ICP22 and UL41 loci; a recombinant virus with a second polynucleotide encoding a second human collagen protein at one or both of the ICP4 loci and a first polynucleotide encoding a first human collagen protein at the ICP22 loci and UL41, etc.). In some embodiments, the recombinant herpes virus genome (for example, a recombinant herpes simplex virus genome) is genetically altered to reduce or eliminate the expression of one or more toxic herpes simplex genes (such as one or both copies of the herpes simplex gene). HSV ICPO gene, one or both copies of the HSV ICP4 gene, the ICP22 gene and / or the UL41 gene). In some embodiments, the herpes simplex virus herpes virus genome (for example, a recombinant herpes simplex virus genome) is genetically altered to reduce the cytotoxicity of the c / CLnn / Lznz / q / Yi recombinant genome (for example, by introduced into a target cell), compared to a corresponding wild type herpes virus genome (eg, a wild type herpes simplex virus genome). In some embodiments, the cytotoxicity (eg, in human keratinocyte and / or fibroblast cells) of the recombinant virus genome (eg, a recombinant herpes simplex virus genome) is reduced by at least about 5%, at least about 10%, at least about 15%, at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about of 45%, at least about 50%, at least about 55%, at least about 60%, at least about 65%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 90%, at least about 95%, or at least about 99%, compared to a corresponding wild-type herpesvirus genome (for example, by measuring relative cytotoxicity of a recombinant herpes simplex virus genome of AICP4 (one or both copies) with resp ecto to a wild-type herpes simplex virus genome in human keratinocytes or fibroblasts (cell lines or primary cells); measuring the relative cytotoxicity of a recombinant herpes simplex virus genome of ΔΙΟΡ4 (one or both copies) / AICP22 relative to a wild-type herpes simplex virus genome in human fibroblasts or keratinocytes (cell lines or primary cells), etc.) . In some embodiments, the cytotoxicity (eg, in human keratinocyte and / or fibroblast cells) of the recombinant herpes virus genome (eg, a recombinant herpes simplex virus genome) is reduced by at least about 1.5-fold, at least about 2 times, at least about 3 times, at least about 4 times, at least about 5 times, at least about 6 times, at least about 7 times, at least about 8 times, at least about least about 9 times, at least about 10 times, at least about 15 times, at least about 20 times, at least about 25 times, at least about 50 times, at least about 75 times, at least about 100-fold, at least about 250-fold, at least about 500-fold, at least about 750-fold, at least about 1000-fold or more, compared to a corresponding wild-type herpesvirus genome (eg, measuring relative cytotoxicity iva of a recombinant herpes simplex virus genome of AICP4 (one or both copies) relative to a wild-type herpes simplex virus genome in human keratinocytes or fibroblasts (cell lines or primary cells); measuring the relative cytotoxicity of a recombinant AICP4 (one or both copies) / AICP22 herpes simplex virus genome relative to a wild-type herpes simplex virus genome in human fibroblasts or keratinocytes (cell lines or primary cells, etc.) . Methods for measuring cytotoxicity are known in the art, including, for example, through the use of vital dyes (formazan dyes), protease biomarkers, an MTT assay (or an assay using related tetrazolium salts such as water soluble tetrazolium, MTS, XTT, etc.), measurement of ATP content, etc. In some embodiments, the recombinant herpes virus genome (eg, a recombinant herpes simplex virus genome) is genetically altered to reduce its impact on host cell proliferation upon exposure of the target cell to the recombinant genome, in comparison with a corresponding wild type herpes virus genome (eg, a wild type herpes simplex virus genome). In some embodiments, the target cell is a human cell. In some embodiments, the target cell is a cell of the c / CLnn / Lznz / q / Yi epidermis and / or the dermis. In some embodiments, the target cell is a fibroblast and / or keratinocyte. In some embodiments, host cell proliferation (eg, human fibroblast and / or keratinocyte cells) upon exposure to the recombinant genome is at least about 5%, at least about 10%, at least about 15%, at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 45%, at least about 50%, at least about 50% least about 55%, at least about 60%, at least about 65%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 90%, at least about 95%, or at least about 99% faster compared to host cell proliferation upon exposure to a corresponding wild-type herpesvirus genome (for example, by measuring the relative cytotoxicity of a AICP4 recombinant herpes simplex virus genome (a or both copies) with respect to cell proliferation after exposure to a wild-type herpes simplex virus genome in human keratinocytes or fibroblasts (cell lines or primary cells); measuring relative cell proliferation after exposure to a recombinant herpes simplex virus genome of ΔΙΟΡ4 (one or both copies) / AICP22 relative to cell proliferation after exposure to a wild-type herpes simplex virus genome in human fibroblasts or keratinocytes (cell lines or primary cells), etc.). In some embodiments, host cell proliferation (eg, fibroblast and / or keratinocyte cells) upon exposure to the recombinant genome is at least about 1.5-fold, at least about 2-fold, at least about 3-fold, at least about 4 times, at least about 5 times, at least about 6 times, at least about 7 times, at least about 8 times, at least about 9 times, at least about 10 times, at least about 15 times, at least about 20 times, at least about 25 times, at least about 50 times, at least about 75 times, at least about 100 times, at least about 250 times, at least about 500-fold, at least about 750-fold, or at least about 1,000-fold faster compared to host cell proliferation upon exposure to a corresponding wild-type herpesvirus genome (for example, by measuring relative cytotoxicity tive of a recombinant herpes simplex virus genome of AICP4 (one or both copies) with respect to cell proliferation upon exposure to a wild-type herpes simplex virus genome in human keratinocytes or fibroblasts (cell lines or primary cells); measuring relative cell proliferation after exposure to a recombinant herpes simplex virus genome of AICP4 (one or both copies) / AICP22 relative to cell proliferation after exposure to a wild-type herpes simplex virus genome in human fibroblasts or keratinocytes (cell lines or primary cells), etc.). Methods for measuring cell proliferation are known to those skilled in the art, including, for example, through the use of a KI67 cell proliferation assay, a BrdU cell proliferation assay, etc. A vector (eg, herpes virus vector) can include one or more polynucleotides of the present disclosure in a form suitable for expression of the polynucleotide in a host cell. Vectors can include one or more regulatory sequences, operably linked to the polynucleotide to be expressed (eg, as described above). In some embodiments, a recombinant nucleic acid of the present disclosure (for example, a recombinant herpes simplex virus c / CLnn / Lznz / q / Yi genome) comprises one or more of the polynucleotides described herein, inserted in either orientation. in recombinant nucleic acid. If the recombinant nucleic acid comprises two or more polynucleotides described herein (eg, two or more, three or more, etc.), the polynucleotides can be inserted in the same or opposite orientations from one another. Without wishing to be bound by theory, the incorporation of two polynucleotides (eg, two transgenes) into a recombinant nucleic acid (eg, a vector) in an antisense orientation can help to avoid read-through and ensure correct expression of each. polynucleotide. IV. Virus Certain aspects of the present disclosure refer to viruses comprising any of the recombinant polynucleotides and / or nucleic acids described herein. In some embodiments, the virus has the ability to infect one or more target cells of a subject (eg, a human). In some embodiments, the virus is suitable for delivery of the recombinant polynucleotides and / or nucleic acids into one or more target cells of a subject (eg, a human subject). In some embodiments, the target cell(s) is one or more human cells. In some embodiments, the target cell(s) is one or more cells of the skin (eg, one or more cells of the epidermis, dermis, and / or subcutis). In some embodiments, the cell(s) are selected from keratinocytes, melanocytes, Langerhans cells, Merkel cells, mast cells, fibroblasts, and / or adipocytes. In some embodiments, the cell(s) are keratinocytes. In some embodiments, the cell(s) reside in the stratum corneum, granulosa layer, spiny cell layer, basal layer, and / or basement membrane. In some embodiments, the target cell(s) is one or more epidermal cells. Any suitable virus known in the art may be used, including, for example, adenovirus, adeno-associated virus, retrovirus, lentivirus, sendai virus, herpes virus (for example, a herpes simplex virus), vaccinia virus, and / or any virus hybrid of these. In some modalities, the virus is attenuated. In some embodiments, the virus is replication defective. In some embodiments, the virus is replication competent. In some embodiments, the virus is modified to alter its tissue tropism relative to the tissue tropism of an unmodified wild type virus. In some embodiments, the virus has less toxicity compared to a corresponding wild type virus. Methods for producing a virus comprising recombinant nucleic acids are known to those skilled in the art. In some embodiments, the virus is a member of the Herpesviridae family of DNA viruses including, for example, a herpes simplex virus, a varicella zoster virus, a human cytomegalovirus, a herpes virus 6A, a herpes virus 6B, a herpes virus 7 and a herpes virus associated with Kaposi's sarcoma, etc. In some modalities, the herpes virus is attenuated. In some embodiments, the herpes virus is replication defective. In some embodiments, the herpes virus is replication competent. In some embodiments, the herpes virus has less toxicity compared to a corresponding wild type herpes virus. In some modalities, the herpes virus is not oncolytic. In some embodiments, the virus is a herpes simplex virus. Herpes simplex viruses comprising recombinant nucleic acids can be produced via a process described, for example, in WO2015 / 009952 and / or c / CLnn / Lznz / q / Yi WO2017 / 176336. In some modalities, the herpes simplex virus is attenuated. In some embodiments, the herpes simplex virus is replication competent. In some forms, the herpes simplex virus is replication defective. In some embodiments, the herpes simplex virus is a herpes simplex virus type 1 (HSV-1), a herpes simplex virus type 2 (HSV-2) or any derivative thereof. In some embodiments, the herpes simplex virus is a herpes simplex virus type 1 (HSV-1). In some modalities, HSV-1 is attenuated. In some embodiments, HSV-1 has less toxicity compared to a corresponding wild type HSV-1. In some modalities, HSV-1 is not oncolytic. In some embodiments, the herpes simplex virus is modified to alter its tissue tropism relative to the tissue tropism of an unmodified wild-type herpes simplex virus. In some embodiments, the herpes simplex virus comprises a modified envelope. In some embodiments, the modified envelope comprises one or more (eg, one or more, two or more, three or more, four or more, etc.) herpes simplex virus motant glycoproteins. Examples of herpes simplex virus glycoproteins may include, but are not limited to, the gB, gC, gD, gH, and gL glycoproteins. In some embodiments, the modified envelope alters the tissue tropism of the herpes simplex virus relative to a wild-type herpes simplex virus. In some embodiments, the transduction efficiency (in vitro and / or in vivo) of a virus of the present disclosure (eg, a herpes virus) relative to one or more target cells (eg, one or more fibroblasts and / or human keratinocytes) is at least about 25%. For example, the transduction efficiency of the virus with respect to one or more target cells may be at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 45%, at least about 50%, at least about 55%, at least about 60%, at least about 65%, at least about 70%, at least about 75%, at least about of 80%, at least about 85%, at least about 90%, at least about 95%, at least about 99%, at least about 99.5% or more. In some embodiments, the virus is a herpes simplex virus and the transduction efficiency of the virus with respect to one or more target cells (eg, one or more human fibroblasts and / or keratinocytes) is from about 85% to about 100%. In some embodiments, the virus is a herpes simplex virus and the transduction efficiency of the virus with respect to one or more target cells (eg, one or more human fibroblasts and / or keratinocytes) is at least about 85%, at least about 86%, at least about 87%, at least about 88%, at least about 89%, at least about 90%, at least about 91%, at least about 92%, to least about 93%, at least about 94%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99 or 100% . Methods for measuring the efficiency of viral transduction in vitro or in vivo are known to those skilled in the art, including, for example, qPCR analysis, deep sequencing, Western blotting, fluorometric analysis (such as fluorescent in situ hybridization (FISH) English), fluorescent reporter gene expression, immunofluorescence, FACS), etc. V. Formulations and compositions Certain aspects of the present disclosure refer to formulations and compositions (eg, pharmaceutical formulations and compositions) comprising any of the recombinant nucleic acids (for example, c / CLnn / Lznz / q / Yi a recombinant herpesvirus genome) and / or virus (for example, a herpes virus comprising a recombinant genome described herein (as a herpes simplex virus comprising a recombinant herpes virus genome) and a carrier or excipient (for example, a carrier or excipient pharmaceutically acceptable.) In some embodiments, the composition or formulation is a cosmetic composition or formulation (eg, a skin care product). In some embodiments, the composition or formulation comprises any one or more of the viruses (eg, herpes viruses) described herein. In some embodiments, the composition or formulation comprises between about 104 and about 1012 plaque forming units (PFU) / mL of virus. For example, the composition or formulation may comprise of about 104a about 1012, about 105a about 1012, about 106a about 1012, about 107a about 1012, about 108a about 1012, about 109a about 1012, around 1010a around 1012, around 1011a around 1012, around 104a around 1011, around 105a around 1011, around 106a around 1011, around 107a around 1011, around 108a around 1011 , around 109a around 1011, around 1010a around 1011, around 104a around 1010, around 105a around 1010, around 106a around 1010, around 107a around 1010, around 108a around 1010, around 109a around 1010, around 104a around 109, around 105a around 109, around 106a around 109, around 107a around 109, around 1 08a around 109, around 104a around 108, around 105a around 108, around 106a around 108, around 107a around 108, around 104a around 107, around 105a around 107, around 106a about 107, about 104a about 106, about 105a about 106o about 104a about 105PFU / mL of the virus. In some embodiments, the composition or formulation comprises about 104, about 105, about 106, about 107, about 108, about 109, about 101°, about 1011 or about 1012 PFU / mL of virus. The formulations and compositions (eg, pharmaceutical formulations and compositions) described herein can be prepared by mixing the active ingredient(s) (such as a virus or recombinant nucleic acid) to the desired degree of purity with one or more acceptable excipients or carriers. . Acceptable carriers or excipients (for example, pharmaceutically acceptable carriers or excipients) are generally nontoxic to recipients at the doses and concentrations employed and may include, but are not limited to: buffers (such as phosphate, citrate, acetate, and other organic acids ); antioxidants (such as ascorbic acid and methionine); preservatives (such as octadecyldimethylbenzylammonium chloride, benzalkonium chloride, benzethonium chloride, phenolic, butyl, or benzyl alcohol, alkylparabens, catechol, resorcinol, cyclohexanol, 3-pentanol, and m-cresol); amino acids (such as glycine, glutamine, asparagine, histidine, arginine, or lysine); low molecular weight polypeptides (less than about 10 residues); proteins (such as serum albumin, gelatin, or immunoglobulins); polyols (such as glycerol, eg, formulations including 10% glycerol); hydrophilic polymers (such as polyvinylpyrrolidone); monosaccharides, disaccharides, and other carbohydrates (including glucose, mannose, or dextrins); chelating agents (such as EDTA); sugars (such as sucrose, mannitol, trehalose, or sorbitol); salt-forming counterions (such as sodium); metal complexes (such as c / CLnn / Lznz / q / Yi Zn protein complexes); liposomes (eg, cationic lipids); nanoparticle carriers; and / or non-ionic surfactants (such as polyethylene glycol (PEG)). A complete review of carriers can be found in REMINGTON'S PHARMACEUTICAL SCIENCES (Mack Pub. Co, N.J. 1991). In some embodiments, the composition or formulation comprises one or more lipid carriers (eg, cationic lipids). In some embodiments, the composition or formulation comprises one or more nanoparticle carriers. Nanoparticles are submicron (less than about 1000 nm) drug delivery vehicles, which can carry encapsulated drugs (such as synthetic small molecules, proteins, peptides, cells, viruses, and nucleic acid-based biotherapeutics for rapid or controlled release. Various molecules (eg, proteins, peptides, recombinant nucleic acids, etc.) can be efficiently encapsulated in nanoparticles using processes known in the art.In some embodiments, a molecule "encapsulated" in a nanoparticle can refer to a molecule (such as a virus) contained in the nanoparticle or attached to and / or associated with the surface of the nanoparticle or any combination of these The nanoparticles for use in the compositions or formulations described herein can be any type of biocompatible nanoparticle known in the art. technique, including, for example, nanoparticles comprising poly(lactic acid ), poly(glycolic acid), PLGA, PLA, PGA and any combination of these (see, for example, Vauthier et al. Adv Drug Del Rev. (2003) 55: 51948; US2007 / 0148074, US2007 / 0092575, US2006 / 0246139, US5753234, US7081483 and WO2006 / 052285). In some embodiments, the carrier or excipient (for example, a pharmaceutically acceptable carrier or excipient) may be adapted or suitable for any route of administration known in the art, including, for example, intravenous, intramuscular, subcutaneous, dermal, intranasal administration. , intratracheal, sublingual, buccal, topical, oral, transdermal, intradermal, intraperitoneal, intraorbital, intravitreal, subretinal, transmucosal, intraarticular, by superficial injection, by implant, by inhalation, intrathecal, intraventricular, and / or intranasal. In some embodiments, the carrier or excipient (eg, pharmaceutically acceptable carrier or excipient) is adapted or suitable for topical, transdermal, subcutaneous, and / or intradermal administration. In some embodiments, the carrier or excipient is adapted or suitable for topical, transdermal, and / or intradermal administration. In some embodiments, the carrier or excipient is adapted or suitable for superficial injection. Examples of carriers or excipients adapted or suitable for use in topical, transdermal, subcutaneous, superficial and / or intradermal application / administration may include, but are not limited to, ointments, oils, pastes, creams, aerosols, suspensions, emulsions, ointments greases, gels, powders, liquids, lotions, solutions, aerosols, patches (eg, transdermal patches or microneedle patches), adhesive tapes, a needle or array of microneedles, and inhalers. In some embodiments, the carrier or excipient (eg, pharmaceutically acceptable carrier or excipient) comprises one or more (eg, one or more, two or more, three or more, four or more, five or more, etc.) of an ointment, an oil, a paste, a cream, an aerosol, a suspension, an emulsion, a fatty ointment, a gel, a powder, a liquid lotion, a solution, an aerosol, an adhesive tape and an inhaler. In some embodiments, the carrier comprises a patch (eg, a patch that adheres to the skin), such as a transdermal patch or a microneedle patch. In some embodiments, the carrier comprises a microneedle or a c / CLnn / Lznz / q / Yi array of microneedles. Methods for making and using suitable microneedle arrays for composition delivery are generally known in the art (Kim Y. et al. Microneedles for drug and vaccine delivery”. Advanced Drug Delivery Reviews 2012, 64 (14): 1547-68). . In some embodiments, the formulation or composition (eg, pharmaceutical formulation or composition) is adapted or suitable for any route of administration known in the art, including, for example, intravenous, intramuscular, subcutaneous, dermal, oral, intranasal, intratracheal, sublingual, buccal, topical, transdermal, intradermal, intraperitoneal, intraorbital, intravitreal, subretinal, transmucosal, intraarticular, by superficial injection, by implant, by inhalation, intrathecal, intraventricular, and / or intranasal. In some embodiments, the composition or formulation is adapted or suitable for cutaneous, topical, subcutaneous transdermal, and / or intradermal administration. In some embodiments, the pharmaceutical formulation or composition is adapted or suitable for topical, transdermal, and / or intradermal administration. In some embodiments, the composition or formulation is adapted or suitable for intradermal administration. In some embodiments, the composition or formulation is adapted or suitable for superficial injection. In some embodiments, the formulation or composition (eg, pharmaceutical formulation or composition) further comprises one or more additional components. Examples of additional components may include, but are not limited to, binding agents (eg, pregelatinized corn starch, polyvinylpyrrolidone or hydroxypropyl methylcellulose, etc.); fillers (eg lactose and other sugars, microcrystalline cellulose, pectin, gelatin, calcium sulfate, ethyl cellulose, polyacrylates or calcium hydrogen phosphate, etc.); lubricants (for example, magnesium stearate, talc, silica, colloidal silicon dioxide, stearic acid, metal stearates, hydrogenated vegetable oils, corn starch, polyethylene glycols, sodium benzoate, sodium acetate, etc.); disintegrants (eg starch, sodium starch glycolate, etc.); wetting agents (eg sodium lauryl sulfate, etc.); saline solutions; alcohols; polyethylene glycols; jelly; lactose; amylase; magnesium stearate; talcum powder; silicic acid; viscous paraffin; hydroxymethylcellulose; polyvinylpyrrolidone; sweeteners; flavorings; flavoring agents; dyes; moisturizers; Sunscreens; antibacterial agents; agents capable of stabilizing polynucleotides or preventing their degradation, and the like. In some embodiments, the composition or formulation comprises a hydroxypropyl methylcellulose gel. In some embodiments, the composition or formulation comprises a phosphate buffer. In some embodiments, the composition or formulation comprises glycerol (for example, at about 1%, about 2%, about 3%, about 4%, about 5%, about 6%, about 7%, about 8%, about 9%, about 10%, about 15%, etc.). Formulations and compositions (eg, pharmaceutical formulations and compositions) for use in administration in vivo are generally sterile. Sterility can be easily achieved, for example, by filtration through sterile filtration membranes. In some embodiments, any of the recombinant nucleic acids, viruses, and / or compositions or formulations described herein can be used for delivery of one or more polynucleotides encoding a collagen protein (for example, a human collagen protein such as collagen 3) in one or more cells of a c / CLnn / Lznz / q / Yi subject (eg, one or more collagen-deficient cells). In some embodiments, any of the recombinant nucleic acids, viruses, and / or compositions or formulations described herein can be used in therapy. In some embodiments, any of the recombinant nucleic acids, viruses, and / or compositions or formulations described herein may be used in the treatment of a cosmetic or cosmetic condition that benefits from the expression of a collagen polypeptide (for example , an aesthetic or cosmetic condition associated with a collagen deficiency (such as aged and / or UV-damaged skin)). In some embodiments, any of the recombinant nucleic acids, viruses, and / or compositions or formulations described herein can be used in the treatment of dermatological aging (eg, as described below). In some embodiments, any of the recombinant nucleic acids, viruses, and / or compositions or formulations described herein can be used in the preparation or manufacture of a medicament. In some embodiments, any of the recombinant nucleic acids, viruses, and / or compositions or formulations described herein may be used in the preparation or manufacture of a medicament useful for the delivery of one or more polynucleotides encoding a collagen protein ( eg, a human collagen protein such as collagen 3) in one or more cells of a subject (eg, one or more collagen-deficient cells). In some embodiments, any of the recombinant nucleic acids, viruses, and / or compositions or formulations described herein may be used in the preparation or manufacture of a medicament useful for the treatment of a cosmetic or aesthetic condition that benefits from the expression of a collagen polypeptide (eg, an aesthetic or cosmetic condition associated with a deficiency of collagen (such as aged and / or UV-damaged skin)). In some embodiments, any of the recombinant nucleic acids, viruses, and / or compositions or formulations described herein may be used in the preparation or manufacture of a medicament useful for the treatment of dermatological aging (for example, as described below). ). SAW. methods Certain aspects of the present disclosure refer to a method of enhancing, increasing, increasing, and / or supplementing the levels of one or more extracellular dermal matrix proteins in a subject (eg, in one or more cells of a subject), comprising administering to the subject any of the recombinant nucleic acids, viruses, medicaments and / or compositions described herein. In some embodiments, the subject is a human. Other aspects of the present description refer to a method for stabilizing or improving the structure and / or organization of the extracellular dermal matrix in a subject, which comprises administering to the subject any of the recombinant nucleic acids, viruses, drugs and / or compositions that are described herein. In some embodiments, the subject is a human. Other aspects of the present disclosure refer to a method for enhancing, increasing, increasing and / or supplementing the levels of one or more human collagen proteins in a subject (for example, in one or more cells of a subject), comprising administering to the subject any of the recombinant nucleic acids, viruses, drugs and / or compositions described herein. In some embodiments, the subject is a human. c / CLnn / Lznz / q / Yi In some embodiments, administration of the recombinant nucleic acid, virus, drug, and composition to the subject increases collagen levels (eg, COL1 -1, C0L1-2, C0L3, C0L1-1 and C0L1-2, C0L1- 1 and C0L3, etc.) (transcript or protein levels) in one or more cells of the subject by at least about 10% compared to the endogenous levels of the collagen(s) in one or more corresponding untreated cells (for example , one or more cells before treatment, one or more uninfected cells during treatment, etc.) from the subject. For example, administration of the recombinant nucleic acid, virus, drug, and / or composition can increase collagen levels (transcript or protein levels) in one or more cells of the subject by at least about 10%, at least about 15%, at least around 20%, at least around 25%, at least around 30%, at least around 40%, at least around 50%, at least around 60%, at least around 70%, at least around 80% , at least about 90%, at least about 95%, at least about 99% or more, as compared to the endogenous levels of the collagen(s) in one or more corresponding untreated cells of the subject. In some embodiments, administration of the recombinant nucleic acid, virus, drug, and composition to the subject increases collagen levels (transcript or protein levels) in one or more cells of the subject by at least about 2-fold compared to the endogenous levels of the collagen(s) in one or more corresponding untreated cells (eg, one or more cells prior to treatment, one or more uninfected cells during treatment, etc.) of the subject. For example, administration of the recombinant nucleic acid, virus, drug, and / or composition can increase collagen levels (transcript or protein levels) in one or more cells of the subject by at least about 2-fold, at least about 3 times, at least around 4 times, at least around 5 times, at least around 6 times, at least around 7 times, at least around 8 times, at least around 9 times, at least around 10 times, at least around 15 times , at least around 20 times, at least around 25 times, at least around 50 times, at least around 75 times, at least around 100 times, at least around 250 times, at least around 500 times, at least around 750 times, at least around less than about 1000 times or more compared to the endogenous levels of the collagen(s) in one or more corresponding untreated cells of the subject. Methods for measuring transcript or protein levels in a sample are known to those skilled in the art, including, for example, via qPCR, RNAseq, ELISA, Western blotting, mass spectrometry, etc. Other aspects of the present disclosure refer to a method of potentiating, augmenting, augmenting, and / or supplementing a subject's soft tissue, which comprises administering to the subject any of the described recombinant nucleic acids, viruses, drugs, and / or compositions at the moment. In some embodiments, the subject is a human. In some embodiments, the recombinant nucleic acids, viruses, drugs, and / or compositions are injected into a subject's soft tissue. In some embodiments, the subject's skin is aged skin. In some embodiments, the subject's skin is damaged from ultraviolet light exposure (eg, from the sun, from a tanning bed, etc.). In some embodiments, the subject's skin is wrinkled. In some embodiments, the recombinant nucleic acids, viruses, drugs, and / or compositions can be used in a method of repairing and / or augmenting a subject's soft tissue. In some modalities, "tissue repair" refers to restoration of tissue architecture and / or function and encompasses tissue regeneration and replacement. In some modalities, soft tissue repair or augmentation refers to procedures that c / CLnn / Lznz / q / YL are used to restore the youthful appearance of skin (for example, compared to "aged" skin whose appearance is due to defects as a result of chronological aging or other physical, chemical or UV damage). In some embodiments, the recombinant nucleic acids, viruses, drugs, and / or compositions are useful in soft tissue cosmetic applications, such as to fill in wrinkles, lines, folds, scars, and to enhance dermal tissue (eg, give a more pulpy effect to thin lips, filling in furrows in the eyes and / or sunken cheeks, etc.). Other aspects of the present description refer to a method for improving the quality, condition and / or appearance of the skin in a subject in need thereof, which comprises administering to the subject any of the recombinant nucleic acids, viruses, drugs and / or or compositions described herein. In some embodiments, the subject is a human. In some embodiments, the skin condition is one or more of sun damage, aging, UV exposure, rough texture, sagging skin, and / or wrinkles. Improvement in skin quality, condition and / or appearance (eg compared to pre-treatment) can be assessed using any suitable method or scale known in the art, eg FACE Q, GAIS, etc In some embodiments, the subject's skin is aged skin. In some embodiments, the subject's skin is damaged from ultraviolet light exposure (eg, from the sun, from a tanning bed, etc.). In some embodiments, the subject's skin is wrinkled. Other aspects of the present description refer to a method for reducing the appearance of one or more superficial depressions in the skin of a subject in need thereof, which comprises administering to the subject any of the recombinant nucleic acids, viruses, drugs and / or compositions that are described herein. In some embodiments, the subject is a human. In some embodiments, administration of the recombinant nucleic acid, virus, drugs, and / or composition reduces the appearance of one or more superficial pits in the subject's skin for at least about three months, at least about six months, at least around nine months or at least around 12 months. In some embodiments, the appearance of one or more pits in the subject's skin is reduced after administration of the composition compared to the appearance of the pit(s) in the subject's skin prior to ad...

Claims

CLAIMS The following is claimed:

1. A recombinant herpesvirus genome comprising a first polynucleotide encoding a first polypeptide comprising a first cosmetic protein.

2. The recombinant herpesvirus genome of claim 1, wherein the recombinant herpesvirus genome comprises two or more copies of the first polynucleotide.

3. The recombinant herpesvirus genome of claim 1 or claim 2, wherein the recombinant herpesvirus genome exhibits competent replication.

4. The recombinant herpesvirus genome of claim 1 or claim 2, wherein the recombinant herpesvirus genome has defective replication.

5. The recombinant herpesvirus genome of any of claims 1-4, wherein the recombinant herpesvirus genome is selected from the group consisting of a recombinant herpes simplex virus genome, a recombinant varicella zoster virus genome, a recombinant human cytomegalovirus genome, a recombinant herpesvirus 6A genome, a recombinant herpesvirus 6B genome, a recombinant herpesvirus 7 genome, a recombinant herpesvirus Kaposi sarcoma-associated herpesvirus genome, and any derivatives thereof.

6. The recombinant herpesvirus genome of any of claims 1-5, wherein the recombinant herpesvirus genome is a recombinant herpes simplex virus genome.

7. The recombinant herpesvirus genome of claim 6, wherein the recombinant herpes simplex virus genome is a recombinant herpes simplex virus type 1 (HSV-1) genome, a recombinant herpes simplex virus type 2 (HSV-2) genome, or any derivative thereof.

8. The recombinant herpesvirus genome of claim 6 or claim 7, wherein the recombinant herpes simplex virus genome is a recombinant herpes simplex virus type 1 (HSV-1) genome.

9. The recombinant herpesvirus genome of any of claims 6-8, wherein the recombinant herpes simplex virus genome comprises an inactivation mutation.

10. The recombinant herpesvirus genome of claim 9, wherein the inactivation mutation is located in a gene of the herpes simplex virus.

11. The recombinant herpesvirus genome of claim 10, wherein the inactivation mutation is a deletion from the coding sequence of the herpes simplex virus gene.

12. The recombinant herpesvirus genome of claim 10 or claim 11, wherein the herpes simplex virus gene is selected from the group consisting of infected cell protein (ICP) 0, ICP4, ICP22, ICP27, ICP47, thymidine kinase (tk), single extensive region (UL) 41 and UL55.

13. The recombinant herpesvirus genome of claim 12, wherein the recombinant herpes simplex virus genome comprises an inactivation mutation in one or both copies of the ICP4 gene.

14. The recombinant herpesvirus genome of claim 12 or claim 13, wherein the recombinant herpes simplex virus genome comprises an inactivation mutation in the ICP22 gene. c / CLnn / Lznz / q / Yi 129 15. The recombinant herpesvirus genome of any of claims 12-14, wherein the recombinant herpes simplex virus genome comprises an inactivation mutation in the UL41 gene.

16. The recombinant herpesvirus genome of any of claims 12-15, wherein the recombinant herpes simplex virus genome comprises an inactivation mutation in one or both copies of the ICPO gene.

17. The recombinant herpesvirus genome of any of claims 12-16, wherein the recombinant herpes simplex virus genome comprises an inactivation mutation in the ICP27 gene.

18. The recombinant herpesvirus genome of any of claims 6-17, wherein the recombinant herpes simplex virus genome comprises the first polynucleotide within one or both of the viral ICP4 gene loci.

19. The recombinant herpesvirus genome of any of claims 1-18, wherein the first cosmetic protein is selected from the group consisting of a first collagen protein, a first fibronectin protein, a first elastin protein, a first lumican protein, a first vitronectin protein, a first vitronectin receptor protein, a first laminin protein, a first neuromodulator protein, and a first fibrillin protein.

20. The recombinant herpesvirus genome of any of claims 1-19, wherein the first cosmetic protein comprises a sequence having at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with an amino acid sequence selected from the group consisting of SEQ. ID. NO.: 15-21 and 53-64.

21. The recombinant herpesvirus genome of any of claims 1-20, wherein the first cosmetic protein is an extracellular structural matrix protein.

22. The recombinant herpesvirus genome of any of claims 19-21, wherein the first collagen protein is a human collagen protein.

23. The recombinant herpesvirus genome of any of claims 19-22, wherein the first collagen protein is selected from the group consisting of an alpha-1 chain polypeptide (I) of collagen (COL1-1), an alpha-2 chain polypeptide (I) of collagen (COL1-2), an alpha-1 chain polypeptide (II) of collagen (COL2), an alpha-1 chain polypeptide (III) of collagen (COL3), an alpha-1 chain polypeptide (IV) of collagen (COL4-1), an alpha-2 chain polypeptide (IV) of collagen (COL4-2), an alpha-3 chain polypeptide (IV) of collagen (COL4-3), an alpha-4 chain polypeptide (IV) of collagen (COL4-4), an alpha-5 chain polypeptide (IV) of collagen (COL4-5), an alpha-6 chain polypeptide (IV) of collagen (COL4-6), an alpha-1 chain polypeptide (V) of collagen (COL5-1), an alpha-2 chain polypeptide (V) of collagen (COL5-2), an alpha-3 chain polypeptide (V) of collagen (COL5-3), an alpha-1 chain polypeptide (VI) of collagen (COL6-1),an alpha-2(VI) chain polypeptide of collagen (COL6-2), an alpha-3(VI) chain polypeptide of collagen (COL6-3), an alpha-4(VI) chain polypeptide of collagen (COL6-4), an alpha-5(VI) chain polypeptide (COL6-5), an alpha-6(VI) chain polypeptide of collagen (COL6-6), an alpha-1(VIII) chain polypeptide (COL8), an alpha-1(IX) chain polypeptide of collagen (COL9-1), an alpha-2(IX) chain polypeptide of collagen (COL9-2), an alpha-3(IX) chain polypeptide of collagen (COL9-3), an alpha-1(X) chain polypeptide of collagen (COL10), an alpha-1(XI) chain polypeptide of collagen (COL11-1), an alpha-2(XI) chain polypeptide of collagen (COL11-2), an alpha-1 chain polypeptide (XII) of collagen (COL12), an alpha-1 chain polypeptide (XIII) of collagen (COL13), an alpha-1 chain polypeptide (XIV) of collagen (COL14), an alpha-1 chain polypeptide (XV) of collagen (COL15), an alpha-1 chain polypeptide (XVI) of collagen (COL16),an alpha-1 (XVII) collagen chain polypeptide (COL17), an alpha-1 (XVIII) collagen chain polypeptide (COL18), an alpha-1 (XIX) collagen chain polypeptide (COL19), an alpha-1 (XX) collagen chain polypeptide (COL20), an alpha-1 (XXI) collagen chain polypeptide (COL21), an alpha-1 (XXII) collagen chain polypeptide (COL22), an alpha-1 (XXIII) collagen chain polypeptide (COL23), an alpha-1 (XXIV) collagen chain polypeptide (COL24), an alpha-1 (XXV) collagen chain polypeptide (COL25), an alpha-1 (XXVI) collagen chain polypeptide (COL26), an alpha-1 (XXVII) collagen chain polypeptide (COL27), and an alpha-1 (XXVIII) collagen chain polypeptide (COL28).

24. The recombinant herpesvirus genome of any of claims 19-23, wherein the first human collagen protein is selected from the group consisting of COL1-1, COL1-2, COL3, COL4-1, COL4-2, COL6-1 and COL17.

25. The recombinant herpesvirus genome of any of claims 19-24, wherein the first human collagen protein comprises a sequence having at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with the amino acid sequence of SEQ. ID. NO.:

17.

26. The recombinant herpesvirus genome of any of claims 1-25, wherein the first cosmetic protein is not a collagen alpha-1 chain polypeptide (Vil) (COL7).

27. The recombinant herpesvirus genome of any of claims 1-26, wherein the first polypeptide essentially consists of or comprises the first cosmetic protein.

28. The recombinant herpesvirus genome of any of claims 1-26, wherein the first polypeptide comprises: (a) the first cosmetic protein, (b) another cosmetic protein and (c) a linker polypeptide linking (a) to (b).

29. The recombinant herpesvirus genome of claim 28, wherein the linker polypeptide is a cleavable linker polypeptide.

30. The recombinant herpesvirus genome of claim 28 or claim 29, wherein the linker polypeptide comprises a sequence having at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with an amino acid sequence selected from the group consisting of SEQ. ID. NO.: 28-31.

31. The recombinant herpesvirus genome of any of claims 28-30, wherein the first cosmetic protein and the other cosmetic protein are different.

32. The recombinant herpesvirus genome of any of claims 1-31, wherein the first polynucleotide encodes a polycistronic mRNA comprising: (a) a first open reading frame (ORE) encoding c / CLnn / Lznz / q / Yi 131 the first polypeptide, (b) a second ORF encoding an additional cosmetic protein, and (c) an interior ribosome entry site (IRES) separating (a) from (b).

33. The recombinant herpesvirus genome of claim 32, wherein the nucleic acid sequence encoding the IRES has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with a nucleic acid sequence selected from SEQ. ID. NO.: 22 or SEQ. ID. NO.:

23.

34. The recombinant herpesvirus genome of claim 32 or claim 33, wherein the first cosmetic protein and the additional cosmetic protein are different.

35. The recombinant herpesvirus genome of any of claims 1-34, wherein the recombinant herpesvirus genome further comprises a second polynucleotide encoding a second cosmetic protein.

36. The recombinant herpesvirus genome of claim 35, wherein the first and second cosmetic proteins are different.

37. The recombinant herpesvirus genome of any of claims 1-36, wherein the recombinant herpesvirus genome exhibits lower cytotoxicity upon introduction into a target cell compared to a corresponding wild-type herpesvirus genome.

38. The recombinant herpesvirus genome of claim 37, wherein the target cell is a cell of the epidermis and / or dermis.

39. The recombinant herpesvirus genome of claim 37 or claim 38, wherein the target cell is a human cell.

40. The recombinant herpesvirus genome of any of claims 37-39, wherein the target cell is a fibroblast.

41. A herpes virus comprising the recombinant herpes virus genome of any of claims 1-40.

42. The herpes virus of claim 41, wherein the herpes virus exhibits competent replication.

43. The herpes virus of claim 41, wherein the herpes virus exhibits defective replication.

44. The herpes virus of any of claims 41-43, wherein the herpes virus exhibits lower cytotoxicity compared to a corresponding wild herpes virus.

45. The herpes virus of any of claims 41-44, wherein the herpes virus is selected from the group consisting of a herpes simplex virus, a varicella zoster virus, a human cytomegalovirus, a herpesvirus 6A, a herpesvirus 6B, a herpesvirus 7, and a herpesvirus associated with Kaposi's sarcoma.

46. ​​The herpes virus of any of claims 41-45, wherein the herpes virus is a herpes simplex virus.

47. The herpes virus of claim 46, wherein the herpes simplex virus is herpes simplex virus type 1 (HSV-1), herpes simplex virus type 2 (HSV-2), or any derivative thereof. c / CLnn / Lznz / q / Yi 132 48. A composition comprising: (a) the recombinant herpesvirus genome of any of claims 1-40 or the herpesvirus of any of claims 41-47, and (b) an excipient.

49. The composition of claim 48, wherein the composition is sterile.

50. The composition of claim 48 or claim 49, wherein the composition is suitable for topical, transdermal, subcutaneous, intradermal, oral, intranasal, intratracheal, sublingual, buccal, rectal, vaginal, urethral, ​​inhaled, intravenous, intra-arterial, intramuscular, intracardiac, intraosseous, intraperitoneal, transmucosal, intravitreal, subretinal, intra-articular, periarticular, local or epicutaneous administration.

51. The composition of any of claims 48-50, wherein the composition is suitable for intradermal administration.

52. The composition of any of claims 48-51, wherein the composition is suitable for surface injection.

53. The composition of any of claims 48-52, wherein the composition is a cosmetic composition.

54. The composition of any of claims 48-53, wherein the composition is a skin care product.

55. The herpes virus of any of claims 41-47 or the composition of any of claims 48-54 for use as a medicament.

56. The herpes virus of any of claims 41-47 or the composition of any of claims 48-54 for use in therapy.

57. The use of the herpes virus of any of claims 41-47 or the composition of any of claims 48-54 in the preparation of a medicament for treating one or more signs or symptoms of dermatological aging.

58. A method for enhancing, boosting, increasing and / or supplementing the levels of one or more extracellular dermal matrix proteins in a subject, wherein the method comprises administering to the subject an effective amount of the herpes virus of any of claims 41-47 or the composition of any of claims 48-54.

59. A method for enhancing, boosting, increasing and / or supplementing the levels of one or more collagen proteins in a subject, wherein the method comprises administering to the subject an effective amount of the herpes virus of any of claims 41-47 or the composition of any of claims 48-54.

60. A method for enhancing, augmenting, increasing and / or supplementing the soft tissue of a subject, wherein the method comprises administering to the subject an effective amount of the herpes virus of any of claims 41-47 or the composition of any of claims 48-54.

61. The method of claim 60, wherein the composition is injected into the subject's soft tissue.

62. A method for improving the condition, quality, and / or appearance of the skin in a subject in need, wherein the method comprises administering to the subject an effective quantity of the herpes virus of any of claims 41-47 or the composition of any of claims 48-54. c / CLnn / Lznz / q / Yi 133 63. The method of claim 62, wherein the composition is administered to one or more points of sun damage or other UV exposure, rough texture, sagging skin, wrinkles, or any combination thereof.

64. A method for reducing the occurrence of one or more superficial depressions in the skin of a subject in need, wherein the method comprises administering to the subject an effective amount of the herpes virus of any of claims 41-47 or the composition of any of claims 48-54.

65. The method of claim 64, wherein the superficial depression(s) in the skin are selected from the group consisting of nasolabial folds, crow's feet, frown lines, expression lines, scars, glabellar lines, eyelid ptosis, tear troughs, nasojugal lines, bunny lines, mid-cheek ptosis, marionette lines, blackhead marks, smile lines, laugh lines, chin creases, neck wrinkles, platysma of the neck, and any combination thereof.

66. A method for increasing and / or improving at least one of the texture, smoothness, elasticity, or tension of the skin of a subject in need, wherein the method comprises administering to the subject an effective amount of the herpes virus of any of claims 41-47 or the composition of any of claims 48-54.

67. The method of any of claims 62-66, wherein the subject's skin is aged skin.

68. The method of any of claims 62-67, wherein the subject's skin is damaged as a result of exposure to ultraviolet light.

69. The method of any of claims 62-68, wherein the subject's skin is wrinkled.

70. A method for reducing one or more dermatological signs of aging in a subject in need, wherein the method comprises administering to the subject an effective amount of the herpes virus of any of claims 41-47 or the composition of any of claims 48-54.

71. The method of claim 70, wherein the reduction of one or more dermatological signs of aging is achieved by: (a) treating, reducing and / or preventing lines and / or wrinkles, (b) reducing the size of skin pores, (c) improving skin thickness, firmness and / or resilience, (d) improving the smoothness, suppleness and / or silkiness of the skin, (e) improving skin tone, radiance and / or clarity, (f) improving collagen and / or procollagen production, (g) improving skin texture and / or promoting retexturization, (h) improving the appearance of skin contours, (i) restoring skin radiance and / or luminosity, (j) improving the deteriorated appearance of skin due to aging and / or menopause, (k) improving skin hydration, (l) increasing skin elasticity and / or resilience, (m) treatment, reduction and / or prevention of sagging skin, (n) improvement of skin firmness, (o) reduction of pigmentation,(p) discolored skin and / or scarring, (p) improvement of the optical properties of the skin by light reflection or diffraction, or (q) any combination of these.

72. The method of any one of claims 58-71, wherein the subject is a human being.

73. The method of any of claims 58-72, wherein the composition or the herpes virus is administered to the subject topically, transdermally, subcutaneously, epicutaneously, intradermally, orally, sublingually, buccally, rectally, vaginally, intraurethrally, intravenously, intra-arterially, intramuscularly, intraosseously, intracardially, intraperitoneally, transmucosally, intravitreally, subretinally, intra-articularly, periarticularly, locally, or by inhalation.

74. The method of any of claims 58-73, wherein the composition or the herpes virus is administered to the subject intradermally.

75. The method of any of claims 58-74, wherein the composition or the herpes virus is administered by surface injection.