Class i lanthipeptides with Anti-viral function

Abstract

Here, the inventors use genomics to discover a new family of lanthipeptides from Actinobacteria dedicated to anti-phage defense. They demonstrate that a specific family of metabolic pathways that produce unknown class I lanthipeptides are encoded near known anti-phage defense systems or within mobile genetic elements, indicating their anti-phage function. Furthermore, the inventors show that the heterologous expression of these pathways in Streptomyces albus (a model strain of Actinobacteria) confers anti-phage defense. The experimental results show that different lanthipeptides of this family confer a selective protection against phages, without compromising the cell viability. The inventors also have identified a specific regulatory system that controls the expression of "defensive lanthipeptides" in Actinobacteria and use this to demonstrate their anti-phage function in a native strain. Finally, the inventors explore the anti-phage mechanism of action of these compounds. Thus the present invention relates to a new class of anti-phage natural peptides.

Description

[0001] CLASS I LANTHIPEPTIDES WITH ANTI-VIRAL FUNCTION FIELD OF THE PRESENT INVENTION: The present invention is in the field of medicine, in particular microbiology. BACKGROUND OF THE PRESENT INVENTION: Infectious diseases caused by viruses constitute a major threat to global health and natural ecosystems as they affect all living organisms. The emergence of new viruses such as SARS- CoV-2 and the prevalence of chronic viral infections calls for the urgent development of newantiviral compounds. Bacteria have long been harnessed as a prolific source of specializedcompounds, known as natural products (NPs), that have shaped modern medicine, such as antibiotics and anticancer drugs [1,2]. Bacteria are also affected by viral infections from bacteriophages (or phages), and have evolved an array of defenses against them, known as anti- phage defense systems [3]. Recently we discovered that bacteria produce antiviral molecules that not only protect them against phages, but also protect humans from viral infections [4]. Our discovery unveiled a potential repository of natural antiviral compounds produced by bacterial defense systems. This leads to the exciting possibility that bacteria could represent a source of novel antivirals of pharmaceutical value. Recent studies have unveiled the untapped metabolic potential of bacteria, with millions of molecules yet to be discovered [5–7]. While some NPs have been identified for their role in protecting bacteria against viral infections, their involvement in anti-phage defense has been largely overlooked. Ribosomally synthesised and post-translationally modified peptides (RiPPs) are a widespread and vast superfamily of NPs, with a myriad of bioactivities and diverse therapeutic applications [8,9]. Lanthipeptides represent the largest and most diverse class of RiPPs and are defined by the presence of thioether cross-linked amino acids, lanthionine (Lan) and / or methyllanthionine (MeLan), which are synthetized post- translationally by a set of specialized enzymes. While the number of discovered lanthipeptides has increased in recent years, little is known about the diversity of their biological functions and ecological relevance. Actinobacteria are a phylum of Gram-positive bacteria that are particularly known for harboring a vast biosynthetic potential for producing lanthipeptides, which remains to be uncovered

[0010] . SUMMARY OF THE PRESENT INVENTION: The present invention is defined by the claims. In particular, the present invention relates to a family of class I lanthipeptides with anti-viral function. DETAILED DESCRIPTION OF THE PRESENT INVENTION:Here, the inventors use genomics to discover a new family of lanthipeptides fromActinobacteria dedicated to anti-phage defense. They demonstrate that a specific family ofmetabolic pathways that produce unknown class I lanthipeptides are encoded near known anti- phage defense systems or within mobile genetic elements, indicating their anti-phage function.Furthermore, the inventors show that the heterologous expression of these pathways inStreptomyces albus (a model strain of Actinobacteria) confers anti-phage defense. Theexperimental results show that different lanthipeptides of this family confer a selectiveprotection against phages, without compromising the cell viability. The inventors also haveidentified a specific regulatory system that controls the expression of “defensive lanthipeptides” in Actinobacteria and use this to demonstrate their anti-phage function in a native strain. Finally,the inventors explore the anti-phage mechanism of action of these compounds. This workreveals a new class of anti-phage NPs, and the first account of a family of RiPPs dedicated to anti-phage defense. Main definitions:As used herein, the terms “peptide”, “polypeptide”, and “protein” are used interchangeablyherein to refer to polymers of amino acids of any length. The terms also encompass an amino acid polymer that has been modified; for example, disulfide bond formation, glycosylation, lipidation, phosphorylation, or conjugation with a labeling component. As used herein, the term “lanthipeptide” has its general meaning in the art and refers to a peptide that contains one or more thioether bridges formed by the post-translational modification of certain amino acid residues. The thioether bridges are derived from the dehydration of serine or threonine residues and the subsequent cyclization with cysteine residues, resulting in lanthionine or methyllanthionine rings. Lanthipeptides are a subclass of ribosomally synthesized and post-translationally modified peptides (RiPPs). Lanthipeptides are classified into four classes based on the biosynthetic enzymes involved in their production. Class I and II lanthipeptides are synthesized by lanthionine synthetases (LanB / C and LanM , respectively), class III lanthipeptides are synthesized by lanthipeptidases (LanL), and class IVlanthipeptides are synthesized by radical SAM enzymes (LanKC). In the context oflanthipeptide biosynthesis, a precursor peptide refers to the initial translated polypeptide chain that serves as the starting point for the biosynthesis of the mature, bioactive lanthipeptidemolecule. The precursor peptide consists of two main components: the core peptide and theleader peptide. As used herein, the term “core peptide” of a lanthipeptide refers to the centralstructural framework of the compound and serves as the scaffold onto which post-translationalmodifications are added, ultimately yielding the mature, bioactive form of the lanthipeptide. The core peptide often contains conserved motifs and regions essential for maintaining theoverall structural integrity of the lanthipeptide molecule. The residues that are modified post-translationally in lanthipeptides are predominantly serine (Ser), threonine (Thr), and cysteine(Cys) residues within the core peptide sequence. As used herein, the term “leader peptide”refers to the N-terminal segment attached to the core peptide. It serves as a recognition sequence for the biosynthetic machinery responsible for the post-translational modifications of the core peptide. Following the completion of post-translational modifications, the leader peptide isoften cleaved to release the mature lanthipeptide from the precursor form.As used herein, the term “polynucleotide” as used herein refers to polymers of nucleotides of any length, including ribonucleotides, deoxyribonucleotides, analogs thereof, or mixtures thereof. This term refers to the primary structure of the molecule. Thus, the term includes triple-,double- and single-stranded deoxyribonucleic acid (“DNA”), as well as triple-, double- andsingle-stranded ribonucleic acid (“RNA”). It also includes modified, for example by alkylation, and / or by capping, and unmodified forms of the polynucleotide. As used herein, the term "encoding" refers to the inherent property of specific sequences of nucleotides in a polynucleotide, such as, for example, a gene, a cDNA, or an mRNA, to serve as templates for synthesis of other polymers and macromolecules in biological processes having either a defined sequence of nucleotides (e.g., rRNA, tRNA and mRNA) or a defined sequence of amino acids and the biological properties resulting therefrom. Thus, a gene, cDNA, or RNA, encodes a protein if transcription and translation of mRNA corresponding to that gene produces the protein in a cell or other biological system. Both the coding strand, the nucleotide sequence of which is identical to the mRNA sequence and is usually provided in sequence listings, and the non-coding strand, used as the template for transcription of a gene or cDNA, can be referred to as encoding the protein or other product of that gene or cDNA. Unless otherwise specified, a "polynucleotide sequence encoding an amino acid sequence" includes all nucleotide sequences that are degenerate versions of each other and that encode the same amino acid sequence. As used herein, the term "virus" refers to a microscopic infectious agent that can only replicate inside the living cells of other organisms. Viruses can infect all types of life forms, from animals and plants to microorganisms, including bacteria and archaea. A virus consists of a nucleic acid genome (either DNA or RNA) enclosed in a protein coat called a capsid. Some viruses also have an outer lipid envelope. Viruses are able to alter the genetic material of their hosts and cause various diseases in humans and animals. As used herein, the term "bacteriophage" refers to a type of virus that infects and replicates within bacteria. Bacteriophages are composed of a nucleic acid (either DNA or RNA) inside a protein capsid, and sometimes have a tail structure that helps them attach to and inject their genetic material into the bacterial cell. Bacteriophages are ubiquitous in nature and can be found in various environments where bacteria are present. Lanthipeptides of the present inventionThe first object of the present invention relates to a lanthipeptide which production is encodedby one or more biosynthetic gene cluster dedicated to anti-phage defense, and that belong to anidentified clade of class I lanthipeptide BGCs encoded in Actinobacterial genomesTypically, the lanthipeptide of the present invention is characterized by 1, 2, 3 or 4 thioetherbridges. In some embodiments, the lanthipeptide of the present invention has a length of at least 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60 or 65 amino acids.In some embodiments, the lanthipeptides of the present invention can exhibit one or morefurther post-translational modifications, including, but not limited to glycosylations, (e.g., N-linked or O-linked glycosylations), myristylations, palmitylations, methylations, acetylations,acylations and phosphorylations (e.g., serine / threonine or tyrosine).In some embodiments, the lanthipeptide of the present invention comprises a core peptide ofconsensus formula (I), (II), (III), (IV), (V), or (VI): TXDXCXXXCXXXC (I) (SEQ ID NO:1)TXDXCGXXCXXXC (II) (SEQ ID NO:2)TXDXCGXXCXXXXC (III) (SEQ ID NO:3)TXDXCGXXCXXXXXXC (IV) (SEQ ID NO:4)TXDXCGXGXTXXXXC (V) (SEQ ID NO:5)SXXGCGSTCXXXXC (VI) (SEQ ID NO:6)CXXDXCXXTXXXXG (VII) (SEQ ID NO:7)wherein X represents any amino acid residue. In some embodiments, the lanthipeptide of the present invention comprises a core peptide as described in Table A: Table A: Formulas per type. Type Formula of type Consensus formula1 TXDXCGXXCXXXXXXC TXDXCGXXCXXXXXXC (II)2 TXDXCXXTCXXXC (SEQ ID NO :8) TXDXCXXXCXXXC (I)3 TXDXCGXXCX(X)XACXXS (SEQ ID NO : 9 TXDXCGXXCXXXXC (III)and SEQ ID NO: 10) 4TXDXCGSGXTXXXXC (SEQ ID NO :11) TXDXCGXGXTXXXXC (IV)5 TDXGCXTXXXDC (SEQ ID NO :12) TDXXCXTXXXXC (V)(SEQ IDNO:20) 6TDDXCXXXCX(X)XCXT (SEQ ID NO:13 and TXDXCXXXCXXXC (I)SEQ ID NO:14) 7SDGGCXXTCGXXXCXS (SEQ ID NO :15) SXXGCXXTCXXXXC (VI)(SEQ IDNO:21) 8TXDXCXXXCXSXC (SEQ ID NO :16) TXDXCXXXCXXXC (I)9 CXXDXCXXTXXXXG CXXDXCXXTXXXXG (VII)10 TDDNCGTTCXSTCTT (SEQ ID NO :17) TXDXCXXXCXXXC (I)11 TDDGCGTTCSTSCXTSSXXXS (SEQ ID TXDXCXXXCXXXC (I)NO :18)12 CXTXDGCAXXCXSSCXS (SEQ ID NO :19) TXDXCXXXCXXXC (I)In some embodiments, the lanthipeptide of the present invention comprises a core peptide oftype (1) and is selected from the group consisting of:AALLRSTDDGCGSTCSGTACTSFGGNV (SEQ ID NO :22)AALQQSTSDNCGSTCTGTACISYTGDPV (SEQ ID NO :23)ACATDDGCGHTCELSACHSQR (SEQ ID NO :24)ACQTDDGCGHTCELSACHSQR (SEQ ID NO :25)ACSTSDGCGSSCGTSACATSSYDPA (SEQ ID NO :26)AKLSCDTDDGCGQTCSTSACNSQANNPS (SEQ ID NO :27)AKLSCDTSDGCGQTCSTSACNSQANNPA (SEQ ID NO :28)AKLSCDTSDGCGQTCSTSACNSQANNPS (SEQ ID NO :29)AMACQTDDGCGSTCEISACHSQK (SEQ ID NO :30)AVGEDGFRLEFAVIESAVPLAKLGCNTSDGCGHTCQGSACNSQ ANNPS (SEQ IDNO :31)CDTSDNCGATCGTSACNSGSLDPS (SEQ ID NO :32)CNTDDGCGDTCNTSACNTSSYDPA (SEQ ID NO :33)DLLRDTSDNCGSSCSGTACTSFVGDPA (SEQ ID NO :34)DLLRDTSDNCGSTCSGTACASFTGDPA (SEQ ID NO :35)DLMRDTSDNCGSTCSGTACTSYVGDPA (SEQ ID NO :36)DMRVVESTTPLVEMMCSTDDGCGVSCGTSACSTGSNDPS (SEQ ID NO :37)DSLPLAKMSCNTDDNCGGSTCGS (SEQ ID NO :38)DTSDGCGNTCSTSACSTNSADPF (SEQ ID NO :39)EEEFVLDMRVVESTTPLVAMMCSTSDGCGSTCSTSACSTSSND PF (SEQ IDNO :40)ETMAPLMVDCDTSDGCGSTCETSACTSGTASPA (SEQ ID NO :41)EVFMCNTNDGCGSTCSGSACSTSSYDPR (SEQ ID NO :42)EVFMCNTNDGCGSTCSTSACSTSSYDPR (SEQ ID NO :43)FMCNTNDGCGSTCSTSACSTSSYDPR (SEQ ID NO :44)GGLLLSTSDNCGSTCDGTACTSAMAYPA (SEQ ID NO :45)GKLMCDTGDGCGSTCQGSACNSYIDDPF (SEQ ID NO :46)IAIMMCDTSDGCGNSCSTSACNTSSNDPS (SEQ ID NO :47)IAIMMCDTSDGCGNSCSTSACSTSSNDPV (SEQ ID NO :48)IAIMMCDTSDGCGQSCSTSACSTSSNDPS (SEQ ID NO :49)ITMCSTDDNCGSTCKPSACASNSADPF (SEQ ID NO :50)IVIMMCDTSDGCGQSCSTSACSTSSNDPS (SEQ ID NO :51)LLRDTNDNCGSTCSGSACASGGGNVG (SEQ ID NO :52)LLRSTSDNCGSTCDGTACVSFASDPA (SEQ ID NO :53)LLRSTSDNCGSTCDGTACVSFVSDPA (SEQ ID NO :54)LQRSTSDNCGSTCSGTACNTSMSDVS (SEQ ID NO :55)LRCDTDDGCGNTCQGSACASFTNNPV (SEQ ID NO :56)LRCDTSDGCGNTCQTSACSSFTNNPV (SEQ ID NO :57)LRCDTSDGCGSTCATSACNSATNNPF (SEQ ID NO :58)LRCTTGDGCGETCSGSACTTSAYDPRD (SEQ ID NO :59)LVIMMCDTSDGCGATCSTSACSTGSNDPF (SEQ ID NO :60)LVIMMCDTSDGCGDTCNTSACSTGSNDPF (SEQ ID NO :61)LVIMMCDTSDGCGNTCGTSACSTGSNDPF (SEQ ID NO :62)LVIMMCDTSDGCGNTCSTSACSTGSNDPF (SEQ ID NO :63)LVIMMCDTSDGCGSSCSTSACSTASNDPS (SEQ ID NO :64)LVIMMCDTSDGCGSTCSTSACSSGSNDPF (SEQ ID NO :65)LVIMMCDTSDGCGSTCSTSACSTGSNDPF (SEQ ID NO :66)LVIMMCDTSDGCGSTCSTSACTTFSNDPL (SEQ ID NO :67)LVIMSCDTSDGCGDTCNTSACASGSNDPF (SEQ ID NO :68)LVITMCDTSDGCGSTCSTSACTTFSNDPY (SEQ ID NO :69)MACSTSDNCGGSTCGSACTSHVTQPL (SEQ ID NO :70)MADCDTSDGCGSTCATTACISNANDPF (SEQ ID NO :71)MCDTSDGCGNTCSTSACTTFSNDPY (SEQ ID NO :72)MCDTSDGCGSTCSTSACTTFSNDPY (SEQ ID NO :73)MCSTSDGCGNSCSTSACTTKASEPL (SEQ ID NO :74)MCSTSDGCGNTCSTSACSSSSYDPF (SEQ ID NO :75)MCSTSDGCGSSCSTSACTTKASEPL (SEQ ID NO :76)MEDCDTSDGCGNTCSTSACTTSSNDPS (SEQ ID NO :77)MGNCSTSDGCGSTCQTSACNSGVANPV (SEQ ID NO :78)MLCSTGDGCGSSCSTSACTTNVADPS (SEQ ID NO :79)MSCDTEDNCGNTTCGSACTSQVAQAPF (SEQ ID NO :80)MSCDTSDGCGGTTCGSACTSQVAQTPY (SEQ ID NO :81)MSCDTSDNCGGTTCGSACTSHVATPL (SEQ ID NO :82)MSCDTSDNCGGTTCGSACTSQVAQNPF (SEQ ID NO :83)PLAKLGCNTSDGCGHTCQGSACNSQANNPS (SEQ ID NO :84)QTDDGCGQTCQISACHSQR (SEQ ID NO :85)SCDTSDGCGSTCSTSACSTGSNNPF (SEQ ID NO :86)SFLRSTDDGCGSTCSNGSTACASSVNDPS (SEQ ID NO :87)SLLRDTDDGCGSTCSNGATACTSLSGDAA (SEQ ID NO :88)SLLRSTDDGCGSTCSNGSTACASSVNDHS (SEQ ID NO :89)SLLRSTDDGCGSTCSNGSTACASSVNDPS (SEQ ID NO :90)TDDNCGSTCGGTACASGP (SEQ ID NO :91)TMCSTGDGCGATCRPSACNSVSSDPF (SEQ ID NO :92)TMGCQTDDGCGTTCQISACHSQK (SEQ ID NO :93)TRSTDDNCGSTCSGSACASGGGNV (SEQ ID NO :94)TSDGCGSSCSGSACTSFTDDPV (SEQ ID NO :95)VAMMCDSSDGCGSTCSTSACSTNSNDPA (SEQ ID NO :96)VIESSTPLVIMMCSTSDGCGSTCSTSACSTSSYDPA (SEQ ID NO :97)VIESSYPIAALACDTNDGCGSTCASACNSSAADPA (SEQ ID NO :98)VIMACSTSDGCGSTCNTSACATSSYDPA (SEQ ID NO :99)VIMMCDTSDGCGQSCSTTACTTSSLDPS (SEQ ID NO :100)VIMMCSTSDGCGNTCDTSACSTSAYDPR (SEQ ID NO :101)VIMMCSTSDGCGSSCSTSACATKSSDPV (SEQ ID NO :102)VIMMCSTSDGCGSSCSTSACTTKSCDPV (SEQ ID NO :103)VITMCATDDNCGSTCQPSACSSISDDPS (SEQ ID NO :104)VVEATTSLVVMMCDTGDGCGSTCSTSACSTSSNDPS (SEQ ID NO :105)VVEVTTPLVIMMCSTSDGCGNTCGTSACSTSSYDPR (SEQ ID NO :106)VVLMCDTDDGCGSTCSNSACATGSNDPS (SEQ ID NO :107)VVMACSTSDGCGETCSTSACSTSSYDPA (SEQ ID NO :108)VVMACSTSDGCGQTCSTSACSTSSYDPA (SEQ ID NO :109)VVMACSTSDGCGSTCSTSACNTSSYDPA (SEQ ID NO :110)VVMMCSTSDGCGATCNTSACNTSSYDPN (SEQ ID NO :111)VVMMCSTSDGCGSSCSTSACATKSSDPT (SEQ ID NO :112)VVMMCSTSDGCGSSCSTSACTTKSCDPV (SEQ ID NO :113)AAHPFGKLQCATGDGCGSTCSGGASACSSFVEDPA (SEQ ID NO :114)AAHPIGKLMCSTGDGCGSTCSGSSSACSSFIEDPA (SEQ ID NO :115)AEHPYGKLMCSTGDGCGPTCQGGASACNSFVEDS (SEQ ID NO :116)ATHPIGRLMCTTSDGCGNTCTNGASSCNSLLRDPE (SEQ ID NO :117)ATYSNGNNQCSTNDGCGQTCENGASACNSSIDDPDHNH (SEQ ID NO :118)CPTDDGCGATCENGASACDSFVEEPA (SEQ ID NO :119)CPTDDGCGNTCAGADSSCNSAADNPF (SEQ ID NO :120)CPTNDGCGETCKDGASACQSVANNVF (SEQ ID NO :121)DCPTDDGCGNTCAGSDSSCNSFADDPS (SEQ ID NO :122)DCPTDDGCGNTCSGNDSSCNSFADDPS (SEQ ID NO :123)DSPLTVFMCPTSDGCGDTCLRTPSE (SEQ ID NO :124)FSCATSDGCGNTCANGASACNSFTDDPA (SEQ ID NO :125)GDCPTDDGCGNTCSGNASSCNSTFDDPS (SEQ ID NO :126)GGPDNCPTDDGCGNTCQNGASACDSFIDDPV (SEQ ID NO :127)GKLACTTNDGCGNTCQNGASACNSFVGDPF (SEQ ID NO :128)GKLLCATNDGCGNTCANGASACTSFTEDPA (SEQ ID NO :129)GKLMCATNDGCGQTCANGASACSSFIEDPA (SEQ ID NO :130)GKLMCNTGDGCGNTCAGSASACNSYVGDPV (SEQ ID NO :131)GKLMCNTGDGCGNTCAGTASACNSYVGDPF (SEQ ID NO :132)GKLMCNTGDGCGNTCQGSASACNSYVSDPV (SEQ ID NO :133)GKLMCNTGDGCGNTCQGTASACNSYVSDPV (SEQ ID NO :134)GKLMCSTGDGCGNTCANGASACGSFIEDPA (SEQ ID NO :135)GKLMCSTGDGCGPTCQGGASACNSFVEDSA (SEQ ID NO :136)GKLMCSTGDGCGSTCATNASACSSFIEDPA (SEQ ID NO :137)GKLMCSTGDGCGSTCATNSSACNSFVEDPA (SEQ ID NO :138)GKLMCSTGDGCGSTCSGGSSACSSFIEDPA (SEQ ID NO :139)GKLMCSTGDGCGSTCSGGSSACSSFVEDPA (SEQ ID NO :140)GKLMCSTGDGCGSTCSNGASACNSFVEDPA (SEQ ID NO :141)GKLMCSTGDGCGTTCATGASACGSFTEDPA (SEQ ID NO :142)GKLMCSTGDGCGTTCATNSSACNSFVEDPA (SEQ ID NO :143)GKLMCSTSDGCGGTCQGGSSACSSYIEDPA (SEQ ID NO :144)GKLMCTTGDGCGTTCATGSSACNSFVEDPA (SEQ ID NO :145)GKLMCTTSDGCGTTCANGSSACSSFVEDPA (SEQ ID NO :146)GKLQCSTGDGCGSTCSGGASACSSFVEDPA (SEQ ID NO :147)GKLTCTTGDGCGNTCAGTASACNSYVGDPV (SEQ ID NO :148)GLMDCPTDDGCGNTCSGNDSSCNSFTDDPS (SEQ ID NO :149)GNCPTDDGCGDTCSGNASACNSTFDDPS (SEQ ID NO :150)GNCPTDDGCGNTCAGNDSTCNSTFDDPS (SEQ ID NO :151)GNCPTDDGCGNTCSGNASTCNSAFDDPS (SEQ ID NO :152)GNLGDCPTDDGCGNTCENGASACDSFIDDPV (SEQ ID NO :153)GNTNDCPTDDGCGDTCQDGASACDSFIDDPA (SEQ ID NO :154)GQADCPTDDGCGNTCAGSASSCNSSMNALA (SEQ ID NO :155)GRTPCPTDDGCGNTCSGSSSACNSAMNALS (SEQ ID NO :156)GSNCPTDDGCGITCANGASACTSEGNNQF (SEQ ID NO :157)HGYGHLMCSTGDGCGTTCQTGASACGSFTEDPA (SEQ ID NO :158)LACSTGDGCGSTCANGASSCNSSAEYPA (SEQ ID NO :159)LACTTSDGCGNTCQNGASACNSFVGDPF (SEQ ID NO :160)LMCDTGDGCGSTCSNGASACDSAAGDPA (SEQ ID NO :161)LMCSTGDGCGSTCATGASACASFTEDPA (SEQ ID NO :162)LMCSTGDGCGSTCATGASACGSFTEDPA (SEQ ID NO :163)LMCSTGDGCGSTCATGSSACNSFVEDPA (SEQ ID NO :164)LMCSTGDGCGTTCATGASACGSFTEDPA (SEQ ID NO :165)LMCSTGDGCGTTCATGASACNSSTEEPS (SEQ ID NO :166)LMCSTGDGCGTTCATNSSACNSFVEDPA (SEQ ID NO :167)LMCSTSDGCGNTCGGNASSCSSLVRDPE (SEQ ID NO :168)MCPTSDGCGNTCVNGASACQSSIEDAA (SEQ ID NO :169)MCSTGDGCGTTCATGASACGSFTEDPA (SEQ ID NO :170)MGDCPTDDGCGNTCAGNDSACNSFADDPS (SEQ ID NO :171)MGDCPTDDGCGNTCAGSDSSCNSFADDPS (SEQ ID NO :172)MGDCPTDDGCGNTCEGDASSCGSFADDPS (SEQ ID NO :173)MGDCPTDDGCGNTCEGEASACNSFADDPS (SEQ ID NO :174)MGDCPTDDGCGNTCVGNDSACNSFADDPS (SEQ ID NO :175)NCPTSDGCGDTCANGASSCVSSIEDAA (SEQ ID NO :176)NCPTSDGCGDTCANGASSCVSSIEDAG (SEQ ID NO :177)NCPTSDGCGDTCANGASSGWPAIAAAAAQSAPRRGDSHAWLSP RRCL (SEQ IDNO :178)SNDCPTDDGCGNTCSNGASACTSQNNNQF (SEQ ID NO :179)SNNCPTDDGCGDTCKNDASACTSESNHGF (SEQ ID NO :180)SSNCPTDDGCGNSCANGASACISHNNNQF (SEQ ID NO :181)SVKVVLAAHPLGRLMCSTNDGCGQTCSGGASSCSSLVRDPE (SEQ ID NO :182)TGDCPTDDGCGDSCKDGASACDSFIGDPS (SEQ ID NO :183)TGDGCGNTCQQGASACNSFVGDPA (SEQ ID NO :184)TGDGCGQTCATGASACGSFTEDPA (SEQ ID NO :185)TGDGCGSTCSNGASACDSAAGDPA (SEQ ID NO :186)TGDGCGTTCATGASACGSFTEDPA (SEQ ID NO :187)TGDGCGTTCATGSSACNSFVEDPA (SEQ ID NO :188)TSDGCGNTCANGASSCNSYIEDPS (SEQ ID NO :189)TSDGCGNTCQNGASACNSYVADPF (SEQ ID NO :190)TSDGCGSTCNDGASACNSSIEPPLS (SEQ ID NO :191)TVFMCPTSDGCGNTCENGASACQSSIEDAA (SEQ ID NO :192)TVFMCPTSDGCGNTCVNGASACQSSIEDAA (SEQ ID NO :193)YADCPTDDGCGNTCANGASACDSYIGDPA (SEQ ID NO :194)YNFDCPTSDGCGNTCANGASSCVSTIEDAA (SEQ ID NO :195)YNFNCPTSDGCGNTCANGASSCASTIEDAA (SEQ ID NO :196)MCSTSDGCGSTCSTSACSTSSNDPF (SEQ ID NO :197)MCSTSDGCGSTCSTSACSTSSNDPA (SEQ ID NO :198)GTPGRACDTSDNCPPTC (SEQ ID NO :199)In some embodiments, the lanthipeptide of the present invention comprises a core peptide oftype (2) and is selected from the group consisting of: AALLRSTDDGCGATCAGTACVSFGGNV (SEQ ID NO :200)AALLRSTDDGCGSTCSGTACASFGGNV (SEQ ID NO :201)ALLQNTEDNCGQTCESACPATGC (SEQ ID NO :202)DLYQLTNDNCGTTCETACTSCPK (SEQ ID NO :203)DTGEWDLDVSFIEAGDSVKHLIYMTNDNCGQTCASACVSCP (SEQ ID NO :204)EATSDNCTSTRASACVTCT (SEQ ID NO :205)EDNCGRTCESACPATGC (SEQ ID NO :206)ELLRLTDDGCGATCESACNSCP (SEQ ID NO :207)ELMNQTSDNCGSSNESACVGCFTE (SEQ ID NO :208)ELMRPTDDGCGHTCESACNSCPE (SEQ ID NO :209)EMMRLTDDGCGSTCESACNSCA (SEQ ID NO :210)GGTVEHIIKMTEDNCGSTCESACTSC (SEQ ID NO :211)GTVIGELLNSTSDGCGSTGASACAGCVTD (SEQ ID NO :212)HIIKMTGDNCGTTCQSACTTC (SEQ ID NO :213)HLIRLTNDGCNSTCATACTSCP (SEQ ID NO :214)IGIEDLDITFIEAGGTVDHIIKMTNDGCGSTCQSACTSC (SEQ ID NO :215)IIKMTDDGCGSTCQSACNSC (SEQ ID NO :216)IIRLTGDNCGSTCQSACVSCP (SEQ ID NO :217)IKMTEDGCGSTCASACTSC (SEQ ID NO :218)IKMTEDNCGGTCASACTSC (SEQ ID NO :219)IKMTEDNCGSTCASACTSC (SEQ ID NO :220)IKMTEDNCGSTCESACTSC (SEQ ID NO :221)IKMTEDSCGSTCESACTSC (SEQ ID NO :222)IKMTQDNCGTTCESACTSC (SEQ ID NO :223)IPELLRSTSDNCGKTCASACTSCKQD (SEQ ID NO :224)IPELLRSTSDNCGKTCSSACTSCKQN (SEQ ID NO :225)IQMTEDGCGSTCASACTSC (SEQ ID NO :226)IRMTEDNCGNTCESACTSC (SEQ ID NO :227)KILYDSSGGCGATCQSSCASCS (SEQ ID NO :228)KILYDTSDGCGSTCASACTSCS (SEQ ID NO :229)KILYDTSDGCGSTCQSACTSCR (SEQ ID NO :230)KMTGDNCGTTCESACTSC (SEQ ID NO :231)LDALLNLTGDNCGGTCASACTSCP (SEQ ID NO :232)LDALLNLTGDNCGTTCESACTSC (SEQ ID NO :233)LDDLLNLTGDGCGTTCQSACTSCP (SEQ ID NO :234)LGSVLYDTSDNCGHTCESACSSCP (SEQ ID NO :235)LLIQLTGDGCGSTCQSACVSCP (SEQ ID NO :236)LLRITSDNCGKTCQSACTSCRS (SEQ ID NO :237)LLRSTSDNCGGTCASACTSCKS (SEQ ID NO :238)LLRSTSDNCGKTCASACTSCKQD (SEQ ID NO :239)LLRSTSDNCGKTCASACTSCQS (SEQ ID NO :240)LMNKTSDNCGSTSESACAGCITD (SEQ ID NO :241)LMNSTSDNCGSTNESACAGCITD (SEQ ID NO :242)LMNTTSDNCGSTNESACAGCITD (SEQ ID NO :243)LMRATDDGCGSTCASACTSCK (SEQ ID NO :244)LMRSTSDNCGKTCASACTSCKS (SEQ ID NO :245)LRLTDDGCGATCESACNSCP (SEQ ID NO :246)LTDDGCGSTCASACTSCS (SEQ ID NO :247)LYDTGDNCGQTCQSACNSCP (SEQ ID NO :248)LYDTSDGCGTTCASACTSCR (SEQ ID NO :249)LYDTSDNCGHTCQSACVSCM (SEQ ID NO :250)MNSTSDNCGSTDESACAGCVID (SEQ ID NO :251)MRLTDDNCGSTCESACNSCP (SEQ ID NO :252)QLIQLTGDGCGSTCATACVSCP (SEQ ID NO :253)QLIRLTDDGCNSTCATACVSCP (SEQ ID NO :254)QLIRLTGDGCNSTCATACTSCP (SEQ ID NO :255)QLIRLTGDGCNSTCATACVSCP (SEQ ID NO :256)QLIRLTNDGCGSTCASACTSCP (SEQ ID NO :257)QLIRLTNDGCGSTCQSACTSCP (SEQ ID NO :258)QLIRLTNDGCGTTCQSACTSCP (SEQ ID NO :259)QLIRLTNDGCNSTCASACVSCP (SEQ ID NO :260)QLIRLTNDGCNSTCATACTSCP (SEQ ID NO :261)QLIRLTNDGCNSTCATACVSCP (SEQ ID NO :262)QLIRLTNDGCNSTCGTACVSCP (SEQ ID NO :263)QLIRLTSDGCGSTCATACTSCP (SEQ ID NO :264)QLIRLTSDGCNSTCATACTSCP (SEQ ID NO :265)QLIRLTSDGCNSTCATACVSCP (SEQ ID NO :266)QLIRLTSGGCNSTCATACVSCP (SEQ ID NO :267)QLIRMTDDGCNSTCATACISCGT (SEQ ID NO :268)QLIRMTDDGCNSTCATACNSCP (SEQ ID NO :269)QLIRMTDDGCNSTCATACTSCP (SEQ ID NO :270)QLIRMTDDGCNSTCATACTSCPA (SEQ ID NO :271)QLIRMTDDGCNSTCATACTSCPS (SEQ ID NO :272)QLIRMTDDGCNSTCGTACVSCGS (SEQ ID NO :273)QLIRMTDDGCNSTCGTACVSCGT (SEQ ID NO :274)QLIRMTNDGCNSTCATACTSCPA (SEQ ID NO :275)QLIRMTNDGCNSTCATACVSCP (SEQ ID NO :276)RILYDTSDGCGQTCESACNSCG (SEQ ID NO :277)SPTEDNCGQTCESACPQTGC (SEQ ID NO :278)VAADQLIQLTGDGCGSTCASACVSCP (SEQ ID NO :279)VAELMNSTSDGCTSTGASACVTCVIS (SEQ ID NO :280)VDDILRMTDDNCGQTCESACTSCP (SEQ ID NO :281)VDHIIKMTNDGCGSTCQSACTSC (SEQ ID NO :282)VEELMRPTDDGCGHTCESACNSCPE (SEQ ID NO :283)VPELMRSTDDNCGSTCASACTTCSKK (SEQ ID NO :284)AALLRSTDDGCGSTCEGSACASGGGNV (SEQ ID NO :285)ADHLIRLTDDGCGQTCESACNSSCP (SEQ ID NO :286)CESACSPSCTDNGN (SEQ ID NO :287)DLMRLTDDGCGTTCESACPAQSGC (SEQ ID NO :288)DWELDITFIESGESVDKLIYMTNDGCGKTCQSACSTTCPA (SEQ ID NO :289)DWELDITFVESGESVDKLIYMTNDGCGKTCQSACSTTCPA (SEQ ID NO :290)ELLSLTDDNCGTTCESACTTTCP (SEQ ID NO :291)ELMRPTDDGCGQTCESACMQTCP (SEQ ID NO :292)ELMRPTDDGCGSTCESACTPTCP (SEQ ID NO :293)GRHCHSNDGCGHTCDSACAASCTDGDD (SEQ ID NO :294)GVDKLIYMTNDGCGKTCQSACTSCPK (SEQ ID NO :295)HLINMTDDGCGHTCEKSTCISAA (SEQ ID NO :296)HLINMTDDGCGHTCEKSTCISSA (SEQ ID NO :297)HLINMTDDGCGNTCAGSTCISAA (SEQ ID NO :298)HLINMTDDGCGQTCEKSTCISAA (SEQ ID NO :299)HLINMTDDGCGQTCEKSTCISAT (SEQ ID NO :300)HLINMTDDGCGSTCEKSTCITSA (SEQ ID NO :301)HLINMTDDGCGTTCEKSTCISAA (SEQ ID NO :302)HLINMTDDGCGTTCEKSTCITAA (SEQ ID NO :303)INPTDDGCGTSCPDSCTPS (SEQ ID NO :304)ISVTDDGCGTTCPKACTTGSR (SEQ ID NO :305)IYMTNDGCGKTCQSACSTTCP (SEQ ID NO :306)IYMTNDGCGSTCQSACSTTCP (SEQ ID NO :307)KLIQMTDDGCGKTCQSACSTTCP (SEQ ID NO :308)KLIRMTDDGCGATCQSACSTTCP (SEQ ID NO :309)KLIRMTDDGCGTSCQSACPATCP (SEQ ID NO :310)KLIRMTDDGCGTTCQSACSPTCP (SEQ ID NO :311)KLIRMTDDGCGTTCQSACSTTCP (SEQ ID NO :312)LDELMRLTDDNCGTTCQSACSTTCA (SEQ ID NO :313)LINLTDDGCGSTCASPCATAMG (SEQ ID NO :314)LINLTDDGCGSTCPKACATNCG (SEQ ID NO :315)LINLTDDGCGTSCPTTCVTSTSA (SEQ ID NO :316)LINLTDDGCGTSCPTTCVTSTSD (SEQ ID NO :317)LVEELIRMTDDGCGTTCQSACPNTCPGD (SEQ ID NO :318)LWGMTDDGCGQTCQSACAPSCTARKGT (SEQ ID NO :319)MTNDGCGKTCQSACSTTCPK (SEQ ID NO :320)QVWNSGTNCHTDDGCGQTCESACSNSCTDGG (SEQ ID NO :321)RDGEQAGADDWELDIKFIEAGDAVKHLIYMTNDQCGTTCQSAC TNTCPS (SEQ IDNO :322)RERACQTDDGCGHTCEKSACTTTA (SEQ ID NO :323)RLIHMTNDGCGQTCQSACSTTCP (SEQ ID NO :324)RLIQMTDDGCGQTCESACQQTCP (SEQ ID NO :325)RLIQMTDDGCGQTCESACQSTCP (SEQ ID NO :326)RLIQMTDDGCGQTCESACSATCP (SEQ ID NO :327)RLIQMTDDGCGQTCESACSSSCP (SEQ ID NO :328)RLIQMTDDGCGQTCESACSTTCP (SEQ ID NO :329)RLIQMTDDGCGQTCQSACSTTCP (SEQ ID NO :330)RLIQMTDDGCGSTCESACNATCP (SEQ ID NO :331)RLIQMTDDGCGSTCQSACSTTCP (SEQ ID NO :332)RLIRMTDDGCGETCESACSTTCP (SEQ ID NO :333)RLIRMTDDGCGKTCESACTTTCP (SEQ ID NO :334)RLIRMTDDGCGKTCQSACPNTC (SEQ ID NO :335)RLIRMTDDGCGKTCQSACSSTCP (SEQ ID NO :336)RLIRMTDDGCGQTCESACSATCP (SEQ ID NO :337)RLIRMTDDGCGQTCQSACSTTCP (SEQ ID NO :338)RLIRMTDDGCGTTCETACSTTCP (SEQ ID NO :339)RLIRMTDDGCGTTCQSACSTTCP (SEQ ID NO :340)RLIRMTDDGCGVTCESACSTTCP (SEQ ID NO :341)RLIRMTDDGCGVTCQSACSTTCP (SEQ ID NO :342)SINLTDDGCGTTCEGACCTSGSD (SEQ ID NO :343)SLVNMTNDGCGTTCEKDTCISGA (SEQ ID NO :344)SLVTMTDDGCGSTCQGSTCISSV (SEQ ID NO :345)TDDGCDHTCEKSACTTTA (SEQ ID NO :346)TDDGCGHTCEKSACTTTD (SEQ ID NO :347)TNDGCGKTCQSACSPSCTNNG (SEQ ID NO :348)TNDGCGQTCESACTPSCTQNG (SEQ ID NO :349)TNDGCGQTCETACTQSCTDNG (SEQ ID NO :350)TNDGCGQTCQSACAPSCTDNG (SEQ ID NO :351)TNDGCGQTCQTACTNSCTRRTVG (SEQ ID NO :352)TWNSGRTCNSNDGCGHTCQSACANSCTDGE (SEQ ID NO :353)VLVNMTDDGCGTTCAKTTCISAA (SEQ ID NO :354)WSMTNDGCGKTCETACTPSCTDNG (SEQ ID NO :355)WSMTNDGCGSTCQSACTQSCTNSGGGG (SEQ ID NO :356)ALLNDTGDGCGSTCQSACANSTCIGG (SEQ ID NO :357)ALLNDTGDGCGSTCQSACSNSTCIGG (SEQ ID NO :358)ALLNDTGDGCGSTCQSACSNSTCISGG (SEQ ID NO :359)DLMRNTDDNCGQTCQSACSNSTCG (SEQ ID NO :360)DLMRSTDDNCGATCQSACSNSTC (SEQ ID NO :361)DTGDGCGATCQSACSNSTCIG (SEQ ID NO :362)ELMSSTDDGCGETCASACSNSTCIA (SEQ ID NO :363)IADLMRNTDDNCGQTCQSACSNSTC (SEQ ID NO :364)IAELMSSTDDGCGQTCASACSNSTCVA (SEQ ID NO :365)LDALLNLTGDNCGTTCESACSTTCA (SEQ ID NO :366)LDELMRLTDDGCGHTCQSACPNSGC (SEQ ID NO :367)LDSLLNLTGDNCGSTCESACSTSCS (SEQ ID NO :368)LGSLLNDTSDNCTSTCASACSNSTCIGG (SEQ ID NO :369)LGWLLNDTSDNCTSTCNSACSNSTCIGG (SEQ ID NO :370)LKDTDDGCGSTCQSACSNSTCIAG (SEQ ID NO :371)LLNDTDDNCTSTCQSACSNSTCIGG (SEQ ID NO :372)LLNDTGDGCGATCQSACSNSTCIGG (SEQ ID NO :373)LLNDTGDGCGSTCQSACANSTCVSG (SEQ ID NO :374)LLNDTGDGCGSTCQSACSNSTCISG (SEQ ID NO :375)LLNDTGDGCTATCQSACSNSTCG (SEQ ID NO :376)LLNDTGDGCTSTCQSACSNSTCIGG (SEQ ID NO :377)LLNKTSDQCGSTNQSACVTCIGD (SEQ ID NO :378)LLNSTSDNCTSTCQSACSNSTCVA (SEQ ID NO :379)LLNSTSDNCTSTCQSACSNSTCVAN (SEQ ID NO :380)LMRNTDDNCGQTCQSACSNSTC (SEQ ID NO :381)LMRSTDDNCGATCQSACSNSTC (SEQ ID NO :382)LNDASDNCGSTCQSACSNSTCIGG (SEQ ID NO :383)LNDTGDGCGQTCESACSNSTCE (SEQ ID NO :384)LNDTGDGCGQTCESACSNSTCG (SEQ ID NO :385)LNDTGDGCGQTCQSACSNSTCE (SEQ ID NO :386)LNDTGDGCGQTCQSACSNSTCIG (SEQ ID NO :387)LNDTGDGCTSTCKSACSNSTCIA (SEQ ID NO :388)LNDTGDGCTSTCQSACSNSTCG (SEQ ID NO :389)LNDTGDNCTSTCQSACSNSTCIGS (SEQ ID NO :390)LNDTSDGCTSTCQSACSNSTCIGG (SEQ ID NO :391)LNDTSDGCTSTCQSACSNSTCVGG (SEQ ID NO :392)LNDTSDNCGSTCQSACSNSTCIGG (SEQ ID NO :393)LNDTSDNCGSTCQSACSNSTCIGS (SEQ ID NO :394)LNDTSDNCTATCSSACSNSTCIGG (SEQ ID NO :395)LNDTSDNCTSTCASACSNSTCIGG (SEQ ID NO :396)LNDTSDNCTSTCQSACTNSTCIGG (SEQ ID NO :397)LRSNTDDGCGQTCESACSNSTC (SEQ ID NO :398)LVNDTSDNCTSTCESACSNSTCE (SEQ ID NO :399)SDFDLRIETVASAPVLGSLLNDTSDNCGSTCQSACSNSTCIGG (SEQ IDNO :400)TTGDGCGQTCQSACVNTGV (SEQ ID NO :401)VAELMRNTDDGCTSTCESACTNSTCIV (SEQ ID NO :402)VAGLLNDTGDGCGSTCQSACSNSTCISG (SEQ ID NO :403)VAGLLNDTSDGCTATCQSACSNSTCISG (SEQ ID NO :404)VASLLNDTGDGCTSTCQSACSNSTCIGG (SEQ ID NO :405)VGMLLNDTGDGCGQTCESACSNSTCE (SEQ ID NO :406)VNDDGLVPCDTSDGCGSTCASACTNSGL (SEQ ID NO :407)ALLNDTGDGCGSSCQSACSNSTCIGG (SEQ ID NO :408)LDSLLNLTGDNCGSTCESACSTTCP (SEQ ID NO :409)LMGNTDDNCGVSCQSACSNSNCE (SEQ ID NO :410)LNDTGDGCTATCESACSNSTCE (SEQ ID NO :411)LNDTSDGCTSTCQSACSNSTCIGS (SEQ ID NO :412)LNDTSDNCTSTCESACSNSTCIGG (SEQ ID NO :413)SDFDLRIETVASLPVLGSLLNDTSDNCGSTCQSACSNSTCIGG (SEQ ID NO :414)VAGLLNDTGDGCGATCQSACSNSTCIGS (SEQ ID NO :415)VAGLLNDTGDGCTSTCQSACSNSTCIGG (SEQ ID NO :416)In some embodiments, the lanthipeptide of the present invention comprises a core peptide oftype (3) and is selected from the group consisting of: AAAACATDDGCGSTCPSACSGSSV (SEQ ID NO :417)ADTILMCSTNDTCGSSCPSACTTS (SEQ ID NO :418)DLDIRLIETSDEAESLINLTEDNCGSSCPNACTGSY (SEQ ID NO :419)INLTDDGCGSSCPSACATSASD (SEQ ID NO :420)INLTDDGCGSSCPSACTTSTAD (SEQ ID NO :421)INLTDDGCGSSCPSACTTSTSD (SEQ ID NO :422)LINLTDDGCGSSCPSACTTSASD (SEQ ID NO :423)LMCSTGDGCGSSCPSACTTS (SEQ ID NO :424)LMCSTGDTCGSSCPSACTTS (SEQ ID NO :425)MLVASTDDNCGSSCPNACTTSSS (SEQ ID NO :426)SDDGCGSSCPSACTSTAN (SEQ ID NO :427)TTDTESPFADLDITFLETGPSAALLVASTDDNCGSSCPNACTTSSS (SEQ IDNO :428)ATETVLMCSTGDTCGSSCPSACTTS (SEQ ID NO :429)FIEGTPASETVLMCTTGDTCGSSCPSACTTS (SEQ ID NO :430)LMCGTGDTCGSSCPSACTTS (SEQ ID NO :431)NTSLRCGTGDTCGSSCPSACTTS (SEQ ID NO :432)SETVLMCSTGDTCGSSCPSACTTS (SEQ ID NO :433)TSLRCGTGDTCGSSCPSACTTS (SEQ ID NO :434)TVAEADPFGLDISFIEGTPATETVLMCTTGDTCGSSCPSACVT S (SEQ IDNO :435)TVLMCSTGDTCGSSCPSACSGSTV (SEQ ID NO :436)TVLMCSTGDTCGSSCPSACTTS (SEQ ID NO :437)TVLMCSTGDTCGSSCPSACVTS (SEQ ID NO :438)TVLMCTTGDTCGSSCPSACTTS (SEQ ID NO :439)TVLTCTTGDTCGSSCPSACVTS (SEQ ID NO :440)TWLRCGTGDTCGSSCPSACTTS(SEQ ID NO :441)VSDDGLVPCGTGDGCGSTCASACANSGV (SEQ ID NO :442)YIVRSCDTSDTCGSTCYSACASS (SEQ ID NO :443)AADTVLMCSTGDNCGSSCPSACTTS (SEQ ID NO :444)ANETVLMCGTGDNCGSSCPSACTTS (SEQ ID NO :445)ASESVLMCTTGDNCGSSCPSACGGSSVE (SEQ ID NO :446)ASETVLMCSTSDNCGSSCGSACTTS (SEQ ID NO :447)ATETALMCGTGDNCGSSCPSACTTS (SEQ ID NO :448)ATETVLMCGTGDNCGSSCPSACTTS (SEQ ID NO :449)DLMRNTDDNCGSSCQSACSNSTC (SEQ ID NO :450)DLMRNTDDNCGTSCQSACSNSTCG (SEQ ID NO :451)DQSDPFGLDITFIENTPASESVLMCSTGDNCGSSCPSACTTS (SEQ IDNO :452)ESETVLMCGTGDNCGSSCPSACATS (SEQ ID NO :453)ITMCATDDNCGSTCKPSACSTSSDNPS (SEQ ID NO :454)LLCGTGDNCGSSCPSACTTS (SEQ ID NO :455)LLCSTGDNCGSSCPSACTTS (SEQ ID NO :456)LMCSTGDNCGSSCPSACTTS (SEQ ID NO :457)LMCSTGDNCGTSCPSACPTS (SEQ ID NO :458)LMCSTGDNCGTSCPSACTTS (SEQ ID NO :459)LMCSTSDNCGSSCPSACTTS (SEQ ID NO :460)LMCTTGDNCGTSCPSACTTS (SEQ ID NO :461)LMGNTDDNCGSSCQSACSNSDCE (SEQ ID NO :462)LMTNTDDNCGSTCQSACSNSSC (SEQ ID NO :463)SALMCSTGDNCGTSCPSACANSGS (SEQ ID NO :464)TELLCSTGDNCGSSCPSACTTS (SEQ ID NO :465)TILMCGTGDNCGSSCPSACSGSTV (SEQ ID NO :466)TMLMCSTGDNCGSSCPSACTTS (SEQ ID NO :467)TVLLCSTGDNCGSSCPSACTTS (SEQ ID NO :468)TVLMCGTGDNCGSSCPSACTTS (SEQ ID NO :469)TVLMCSTGDNCGASCPSACATS (SEQ ID NO :470)TVLMCSTGDNCGSSCPSACTTS (SEQ ID NO :471)TVLTCSTGDNCGSSCPSACSGSTV (SEQ ID NO :472)VAALMRDTSDNCGSTCPSACASGGGKVG (SEQ ID NO :473)VITMCATDDNCGTTCKPSACSTSSDNPS (SEQ ID NO :474)In some embodiments, the lanthipeptide of the present invention comprises a core peptide oftype (4) and is selected from the group consisting of: ASPSAPTGDCTDDNCGSGNTASDACVTNG (SEQ ID NO :475)ASPTAPTGDCTDDNCGSGNTGSEACVTNG (SEQ ID NO :476)ATGSDDCTSDKCGSGETGSDACTTNG (SEQ ID NO :477)ATSTDDDCGSGDTGSSACTTTSN (SEQ ID NO :478)ATSTDDDCGSGNTGSDACTTNADE (SEQ ID NO :479)ATSTDDDCGSGNTGSDACTTNADVGGVR (SEQ ID NO :480)ATSTDDDCGSGNTGSDACTTNADVGVR (SEQ ID NO :481)ATSTDDECGSGNTESQACTTTSD (SEQ ID NO :482)ATSTDDNCGSGNTDSDACTTNADAGVR (SEQ ID NO :483)ATSTDDNCGSGNTGSNACTTNADIGGVR (SEQ ID NO :484)ATSTDDNCGSGNTRSDACTTKADGS (SEQ ID NO :485)AVASEDCTSDECGSGETSSDACTTNS (SEQ ID NO :486)FSTNTDDNCGSGNTGSNACTTKNN (SEQ ID NO :487)LTTDDECGSGETGTNACTTNADAS (SEQ ID NO :488)MSSEDCTSDNCGSGNTGSNACTTRA (SEQ ID NO :489)VIGADTSDNCGSGNTGSNACTTNC (SEQ ID NO :490)ASGYSTNTSDGCGSGNTGSNACTTRCDGGN (SEQ ID NO :491)ATGTDDNCGSGNTGSNACTTRCDASD (SEQ ID NO :492)ATGYATGTDDNCGSGNTGSNACTTRCDAGN (SEQ ID NO :493)ATNTDDDCGSGDTGTSACTTSADG (SEQ ID NO :494)GYATATDDGCGSGNTGSNACTTKCDGGN (SEQ ID NO :495)GYATATDDGCGSGNTGSNACTTRCDDGN (SEQ ID NO :496)GYATATDDGCGSGNTGSNACTTRCDGGN (SEQ ID NO :497)SGGYATSTNDGCGSGNTGSNACTTKCDGGN (SEQ ID NO :498)SGHATNTDDECGSGNTGTSACTT (SEQ ID NO :499)STGYATNTDDNCGSGNTGSNACTTRCDGSF (SEQ ID NO :500)YATATDDGCGSGNTGSNACTTKCDGGN (SEQ ID NO :501)YATSTNDGCGSGNTGSNACTTKSDGDN (SEQ ID NO :502)YSTNTSDGCGSGNTGSNAGTTRCDGGN (SEQ ID NO :503)AGGYATNTDDNCGSGNTGSNACSGGGK (SEQ ID NO :504)AGGYATSTDDNCGSGNTGSNACSGGGK (SEQ ID NO :505)AGGYATSTDDNCGSGNTGSNACSGGSK (SEQ ID NO :506)ASGYATNTDDGCGSGNTGSNACTGK (SEQ ID NO :507)ASGYATSTDDGCGSGNTGSNACSGGSK (SEQ ID NO :508)ASGYATSTDDGCGSGNTGSNACTGK (SEQ ID NO :509)ASGYATSTDDNCGSGNTGSNACSGGSK (SEQ ID NO :510)ATNTDDGCGSGNTGSNACTGGRD (SEQ ID NO :511)ATNTDDNCGSGNTGSNACSGGR (SEQ ID NO :512)ATSTDDECGSGDTNSDACSGGSGR (SEQ ID NO :513)ATSTDDECGSGDTNSDACSSGSGR (SEQ ID NO :514)ATSTDDGCGSGNTGSNACTGGGN (SEQ ID NO :515)ATSTDDNCGSGDTASDACSGGSGR (SEQ ID NO :516)ATSTDDNCGSGDTESDACSSGSGN (SEQ ID NO :517)ATSTDDNCGSGDTGSDACSGDGSS (SEQ ID NO :518)ATSTDDNCGSGNTGSDACSG (SEQ ID NO :519)ATSTSDECGSGNTGSDACSGGSGN (SEQ ID NO :520)ATTTSDECGSGNTDSDACSGGSGN (SEQ ID NO :521)FATDTDDNCGSGNTGSDACSGG (SEQ ID NO :522)FATSTDDGCGSGNTGSDACTGDGS (SEQ ID NO :523)SGYATSTDDGCGSGNTGSTACSGK (SEQ ID NO :524)SGYATSTDDNCGSGNTGSDACSGG (SEQ ID NO :525)TGGYATNTDDNCGSGNTGSNACSGGGK (SEQ ID NO :526)TGGYATNTDDNCGSGNTGSNACSGK (SEQ ID NO :527)TGYATGTDDGCGSGNTGSSACSGK (SEQ ID NO :528)TGYATGTDDGCGSGNTGSSACTGG (SEQ ID NO :529)VSSTDDGCGSGNTGSNACSGK (SEQ ID NO :530)YATATDDGCGSGNTGSNACSGGGK (SEQ ID NO :531)YATATDDGCGSGNTGSNACSGGSK (SEQ ID NO :532)YATATDDGCGSGNTGSSACSGGGK (SEQ ID NO :533)YATATDDGCGSGNTGSSACSGGGR (SEQ ID NO :534)YATDTSDNCGSGNTGSDACAGG (SEQ ID NO :535)YATITDDNCGSGDTDSDACSGA (SEQ ID NO :536)YATSTDDNCGSGNTGSDACSG (SEQ ID NO :537)YATSTDDNCGSGNTGSDACSGGGR (SEQ ID NO :538)YATSTDDNCGSGNTGSNACSGGGK (SEQ ID NO :539)VSSTDDGCGSGNTGSNACTGK (SEQ ID NO :540)In some embodiments, the lanthipeptide of the present invention comprises a core peptide oftype (5) and is selected from the group consisting of: ATEVHPGDTDNGCDTVAGGDC (SEQ ID NO :541)DTDDGCDTVKGSDC (SEQ ID NO :542)DTDDGCDTVRGGDC (SEQ ID NO :543)EFDLDIRIVERGPVAAALLGDTDDGCDTVRGSNC (SEQ ID NO :544)FELDVEIVREGPVAAALLADTDDGCDTVKGSDC (SEQ ID NO :545)FELDVEIVTEGPVTAALLADTDDGCDTVKGSDC (SEQ ID NO :546)FELDVQVVTEGPVVAALLADTDDGCDTVKGSDC (SEQ ID NO :547)GGPADVLPTITDNGCDTVKGSDC (SEQ ID NO :548)LADTDDGCDTVKGSDC (SEQ ID NO :549)LADTDDGCDTVRGSDC (SEQ ID NO :550)LANTDDGCDTVQGSDC (SEQ ID NO :551)LANTDDGCDTVRGSDC (SEQ ID NO :552)LCTTDNGCNTVGGSDC (SEQ ID NO :553)LGDTDDGCDTVRGGDC (SEQ ID NO :554)LGDTDDGCDTVRGSDC (SEQ ID NO :555)LSSTDDGCDTVRGSDC (SEQ ID NO :556)LTDTDDGCDTVKGSDC (SEQ ID NO :557)LCTTDNGCSTNKQKDC (SEQ ID NO :558)LCTTDNGCSTNKSTDC (SEQ ID NO :559)AAAALNCSTDNGCDTVAGGDC (SEQ ID NO :560)ALLSSTDDGCDTKTDGDC (SEQ ID NO :561)ALLSSTDDGCDTVKGSDC (SEQ ID NO :562)ARRCSTDNGCDTQANGDC (SEQ ID NO :563)ATASRKCSTDNGCDTLAGSDC (SEQ ID NO :564)ATEARRCSTDNGCDTVAGGDC (SEQ ID NO :565)ATLSRRCSTDNGCDTLANGDC (SEQ ID NO :566)LCSTDNGCDTRKNGDC (SEQ ID NO :567)LSSTDDGCDTDKNGDC (SEQ ID NO :568)LSSTDDGCDTKQGSDC (SEQ ID NO :569)LSSTDDGCDTVRGGDC (SEQ ID NO :570)MSSTDDGCDTVKTGDC (SEQ ID NO :571)EDFDLDITTVASAPRSPDLLNSTDDGCGETPDPAGVNG (SEQ ID NO :572)EFDLDMKIVESGPVAAALLGNTDDGCDTRRDGDC (SEQ ID NO :573)LGDTDDGCDTLKNGDC (SEQ ID NO :574)LGNTDDGCDTLKNGDC (SEQ ID NO :575)NTDDGCDTDRNGDC (SEQ ID NO :576)PGRLALLADTDDNCDTKKPGDC (SEQ ID NO :577)PGRLALLADTDDNCDTQKPGDC (SEQ ID NO :578)PVAAALLADTDDGCDTQKNGDC (SEQ ID NO :579)TDGDDGFDLDVRLVEFGPTSALLLANTDDGCDTQKQGDC (SEQ ID NO :580)VLLASTDDGCDTQKQGDC (SEQ ID NO :581)In some embodiments, the lanthipeptide of the present invention comprises a core peptide oftype (6) and is selected from the group consisting of:ALINLTDDGCKPSCQGSCATNVA(SEQ ID NO :582)ASDDGCGSSCPDACVSTAN(SEQ ID NO :583)ATLINLTDDGCGSTCSSPCATN (SEQ ID NO :584)AVLINLTDDGCGSTCSSPCATNVA (SEQ ID NO :585)FAKLINLTDDGCGSTCSSPCASSVA (SEQ ID NO :586)GLISLTDDGCGETCGACTTNVA (SEQ ID NO :587)GLVSLTDDGCGETCGACTTNVA (SEQ ID NO :588)IAGLVSLTDDGCGETCGACTTNVA (SEQ ID NO :589)IGVTDDNCGSTCASPCATNVA (SEQ ID NO :590)ILLTDDGCKPSCPESCASAVA (SEQ ID NO :591)ILTDDGCGSTCSSPCATAVA (SEQ ID NO :592)INLTDDGCGSSCPNACATNIG (SEQ ID NO :593)INLTDDGCGSSCPSACATNVG (SEQ ID NO :594)INLTDDGCGSTCSSPCATAVA (SEQ ID NO :595)INLTDDGCGSTCSSPCATH (SEQ ID NO :596)INLTDDGCGSTCSSPCATNVA (SEQ ID NO :597)INLTDDGCGTTCPSTCVTSVSD (SEQ ID NO :598)INLTDDGCKPSCQGSCATNVA (SEQ ID NO :599)INLTDDNCGSSCPKACATNVG (SEQ ID NO :600)INLTDDNCGSTCSSPCATNVA (SEQ ID NO :601)ISLTDDGCGETCGACTTNVA (SEQ ID NO :602)ITLTDDGCKPSCPASCATNVA (SEQ ID NO :603)IVLTDDGCGSSCPSACATNVA (SEQ ID NO :604)LINLTDDGCGSSCPNACATNVG (SEQ ID NO :605)LINLTDDGCGSSCPNACTTSAAD (SEQ ID NO :606)LINLTDDGCGSSCPNSCTTSAAD (SEQ ID NO :607)LINLTDDGCGSTCSSPCASSVA (SEQ ID NO :608)LINLTDDGCGSTCSSPCATNVA (SEQ ID NO :609)LINLTDDGCKPSCNGSCATNVA (SEQ ID NO :610)LINLTDDGCKPSCQGSCATNVA (SEQ ID NO :611)LINLTDDGCKPTCAGSCATNVA (SEQ ID NO :612)LINLTDDNCGSSCPKACATNVG (SEQ ID NO :613)LINLTDNGCGSTCASPCATNVG (SEQ ID NO :614)LTDDGCGSTCGACTTNVA (SEQ ID NO :615)LTDDGCKPSCKGSCATNVA (SEQ ID NO :616)LTDDGCKPSCNGSCATNVA (SEQ ID NO :617)LTDDGCKPSCQGSCATNVA (SEQ ID NO :618)NLTDDGCGASCPTTCVTSTSA (SEQ ID NO :619)NLTDDGCGSTCPKACATNIG (SEQ ID NO :620)NLTDDGCGSTCSSPCATNVA (SEQ ID NO :621)NLTDDGCGSTCTACTTNVA (SEQ ID NO :622)NLTDDGCKPSCKGSCATNVA (SEQ ID NO :623)NLTDDGCKPSCNGSCATNVA (SEQ ID NO :624)NLTDDGCKPSCQGSCATNVA (SEQ ID NO :625)NLTDDGCKPTCKGSCATNVA (SEQ ID NO :626)QEDEFDLDISILESGDGSAVLVNLTDDGCSPTCEGSCATNVA (SEQ IDNO :627)RLIVLTDDGCGSSCPSACATKVA (SEQ ID NO :628)SDSPFALDIRLIEGGDTTPLINMTDDGCGASCPNTCATSTSD (SEQ IDNO :629)SLINLTDDNCGSSCPNACATNMG (SEQ ID NO :630)SLTNLTDDGCGSTCGACTTNVA (SEQ ID NO :631)TITDDNCGSTCASPCATNVA (SEQ ID NO :632)VLINLTDDGCKPTCKGSCATNVA (SEQ ID NO :633)VNLTDDGCGSTCSSPCATAVA (SEQ ID NO :634)VNLTDDGCNPTCPESCTSAAN (SEQ ID NO :635)APVAATDEFDLDVTIVERTDAASLEVLTDDGCGATCGACTTG (SEQ IDNO :636)ATTDDGCGSTCGACTTNAA (SEQ ID NO :637)DEYELNIDLVDAGPVSGHASNTBDSCGTTG (SEQ ID NO :638)DGFDLDVRLVEVGDSAGLVNLTDDGCGETCGACTTNVA (SEQ ID NO :639)DGFDLDVSLIEIADPAGLVNLTDDNCGSTCGACTTNVA (SEQ ID NO :640)DGFDLDVSLVEIADPAGLVNLTDDNCGSTCGACTTNVA (SEQ ID NO :641)DGFDLDVSLVEIADPAGLVSLTDDNCGSTCGACTTNVA (SEQ ID NO :642)DGFDLDVSLVEIVDPAGLVNLTDDNCGSTCGACTTNVA (SEQ ID NO :643)DGFELDVALLEVADTAGLINLTDDGCGETCGACTTNVA (SEQ ID NO :644)DGFELDVTLLEVSDAASLTNLTDDGCGETCGACTTNVA (SEQ ID NO :645)GFDLDVSLLEISDTAGLVNITDDNCGSTCGACTTGVA (SEQ ID NO :646)GFELDASLLEVADSASLVNITNDNCGSTCGACTTGVA (SEQ ID NO :647)GFELDVTLVEVADPAGLVNLTDDGCGETCGACTTNVA (SEQ ID NO :648)GLINLTDDGCGSTCGACTTNVA (SEQ ID NO :649)GLINLTDDNCGSTCGACTTNVA (SEQ ID NO :650)GLINVTDDNCTSTCGACVTDGGS (SEQ ID NO :651)GLISLTDDGCGSTCGACTTNVA (SEQ ID NO :652)GLISLTNDGCGETCGACTTNVA (SEQ ID NO :653)GLISLTNDGCGTTCGACTTNVA (SEQ ID NO :654)GLITMTDDNCGSSCEKTTCITSS (SEQ ID NO :655)GLVNITNDGCGSTCGACTTGVH (SEQ ID NO :656)GLVNLTDDGCGSTCGACTTNVA (SEQ ID NO :657)GLVNLTDDGCGSTCGACVSSVA (SEQ ID NO :658)GLVNLTDDGCGSTCGACVTNVA (SEQ ID NO :659)GLVNLTDDNCGSTCGACTTNVA (SEQ ID NO :660)GLVNLTDDNCGSTCGACTTNVARRLN (SEQ ID NO :661)GLVNLTDDNCGSTCGACVTNVA (SEQ ID NO :662)GLVNLTDDNCGTTCGACTTNVA (SEQ ID NO :663)GLVNMTDDGCGSTCEKDACISAA (SEQ ID NO :664)GLVNMTDDNCGSTCEKSTCVTGA (SEQ ID NO :665)GLVNVTDDGCGSTCGACNSTVA (SEQ ID NO :666)GLVNVTDDGCGSTCGACVTGAA (SEQ ID NO :667)GLVNVTDDGCTSTCGACISNAY (SEQ ID NO :668)GLVNVTDDGCTSTCGACVSGAV (SEQ ID NO :669)GLVNVTDDGCTSTCGACVSNAD (SEQ ID NO :670)GLVNVTDDNCTSTCGACITNSA (SEQ ID NO :671)GLVNVTDDNCTSTCGACVTGAV (SEQ ID NO :672)GLVSITNDGCGSTCGACTTNVA (SEQ ID NO :673)HLVSMTDDNCGSTCEKSTCISAV (SEQ ID NO :674)HPQPKPSDGFELDVALLEVSDTAGLINLTDDGCGETCGACTTNVA (SEQ IDNO :675)ILTDDGCGSTCGACTTGVH (SEQ ID NO :676)ITDDNCGSSCGACTTGVA (SEQ ID NO :677)ITGDNCGSTCGACTTGVH (SEQ ID NO :678)KATAAVGDEFDLDVRTVETADAASLQVLTDDGCGATCGACTTGVH (SEQ IDNO :679)KATVAVGDEFDLDVRTVETADAASLQVLTDDGCGATCGACTTGVH (SEQ IDNO :680)KTLTDDGCGSTCGACTTGVH (SEQ ID NO :681)KTLTDDNCGSTCGACTTGVH (SEQ ID NO :682)LINMTDDGCTSTCGACVTNAP (SEQ ID NO :683)LLRNTDDNCGSTCVGTACPTNVANPS (SEQ ID NO :684)LSLLEVADVAGLVNLTDDGCGSTCTACTTNVA (SEQ ID NO :685)LTDDGCGSTCGACTTGAA (SEQ ID NO :686)LTDDNCGSTCGACTTNVA (SEQ ID NO :687)MDASLLEVADSASLVNITNDGCGSTCGACTTGVA (SEQ ID NO :688)NATDDGCGSTCGACTTNVA (SEQ ID NO :689)NLTDDGCGSTCGACTTGVH (SEQ ID NO :690)NLTDDGCGSTCGACVSSVA (SEQ ID NO :691)NLTNDGCGSTCGACTTNVA (SEQ ID NO :692)PDGFELDVRLVEVADTAGLVSITNDGCGSTCGACTTNVA (SEQ ID NO :693)PQTPGASDGFDLDVSLVEIDDTAGLVNLTDDNCGTTCGACTTNVA (SEQ IDNO :694)PVTASDGFDLDVRLVEVGDSAGLVNLTDDGCGETCGACTTNVA (SEQ IDNO :695)QEPAAGGQPDGFDLNVSLLEVSDAAGLTVLNDDNCGSSCGACVTF (SEQ IDNO :696)QEPAAGGQPDGFDLNVSLLEVSDAAGLTVLTDDNCGSSCGACVTF (SEQ IDNO :697)QEPAAGGQSDGFDLNVSLLEVSDAAGLTVLTDDGCGSSCGACVTF (SEQ IDNO :698)QEPAASGQSDGFDLNVSLLEVSDAAGLTVLTDDNCGSSCGACVTF (SEQ IDNO :699)QEPLAQEDGFTLNVGLLEVSDAIGLTNLTDDNCGTTCGACTTNVA (SEQ IDNO :700)QEPTADGQSDGFDLNVSLLEVSDAAGLTVLTDDGCGSSCGACVTF (SEQ IDNO :701)QEPTAGGQSDGFDLNVSLLEVSDAAGLTVLTDDGCGSSCGACVTF (SEQ IDNO :702)QEPTAGGQSDGFDLNVSLLEVSDAAGLTVLTDDNCGSSCGACVTF (SEQ IDNO :703)QEPTASGQSDGFDLNVSLLEVSDVAGLTVLTDDNCGSSCGACVTF (SEQ IDNO :704)QEPTATSQSDGFDLNVSLLEVSDAAGLTSLTDDNCGSTCGACTTNVA (SEQ IDNO :705)QEPTSQSDGFDLNVSLLEVSDAAGLTSLTDDNCGSTCGACTTNVA (SEQ IDNO :706)QEPVAQEDGFTLNVGLLEVSDAAGLTNLTDDNCGTTCGACTTNVA (SEQ IDNO :707)QEPVAQEDGFTLNVSLLEVSDAAGLTNLTDDNCGTTCGACTTNVA (SEQ IDNO :708)QEPVAQEDGFTLNVSLLEVSDAAGLTNLTDDNCGTTCGACVTNVA (SEQ IDNO :709)QESGTASDGFVLDIALLEVGDVASLTNLTDDGCGETCGACTTNVA (SEQ IDNO :710)QESTAGGQSDGFDLNVSLLEVSDAAGLTVLTDDGCGSSCGACVTF (SEQ IDNO :711)QESTAGGQSDGFDLNVSLLEVSDTAGLTVLTDDGCGSSCGACVTF (SEQ IDNO :712)QESVAQEDGFTLNIGLLEVSDAAGLTNLTDDNCGTTCGACTTNVA (SEQ IDNO :713)QESVAQEDGFTLNVGLLEVSDAAGLTNLTDDNCGTTCGACTTNVA (SEQ IDNO :714)QGSVAQEDGFTLNIGLLEVSDAAGLTNLTDDNCGTTCGACTTNVA (SEQ IDNO :715)QPSAATPDGFDLDVTLVEVADVAGLINLTDDGCGETCGACTTNVA (SEQ IDNO :716)QQTPGTSDGFDLDVSLVELADPAGLVNLTDDNCGTTCGACTTNVA (SEQ IDNO :717)QQTPGTSDGFDLNVSLVEVADPAGLVNLTDDNCGTTCGACTTNVA (SEQ IDNO :718)QSDGFDLNVSLLEVSDAAGLTVLTDDGCGSSCGACVTF (SEQ ID NO :719)QSDGFELNVSLLEVSDAAALTVLTDDNCGSSCGACVTF (SEQ ID NO :720)SLTDDGCGETCGACTTNVA (SEQ ID NO :721)SMVNLTDDNCGSTCGACTTNVA (SEQ ID NO :722)SPATASSDGFDLDVSLVEVADSASLTNLTNDNCGTTCGACTTNVA (SEQ IDNO :723)SPSSPSGDGFDLDVALLEVGDVAGLTNLTDDNCGTTCGACTTNVA (SEQ IDNO :724)SSTTPDGFELDVALLEVSDTASLTNLTDDGCGETCGACTTNVA (SEQ IDNO :725)STGPEQAFDLDIRALDIADAGPFMARNTDDNCGSTCPNACATNM (SEQ IDNO :726)SVTDDNCGSTCGACTTNVA (SEQ ID NO :727)TLTDDGCGSTCGACTTGLH (SEQ ID NO :728)TSLTDDNCGSTCGACTTNVA (SEQ ID NO :729)TSVAQDPFDLDISVVESGAPSRWVINSDGGCGLSRGNACASSGS (SEQ IDNO :730)VLTDDGCGSTCGACTTGFH (SEQ ID NO :731)VLTDDGCGSTCGACTTGLH (SEQ ID NO :732)VLTDDGCGSTCGACTTGVH (SEQ ID NO :733)VQLTDDGCGSTCTACTTG (SEQ ID NO :734)VRLTDDGCGSTCTACTTG (SEQ ID NO :735)In some embodiments, the lanthipeptide of the present invention comprises a core peptide oftype (7) and is selected from the group consisting of: ASDGGCGSTCGTSCVSNAA (SEQ ID NO :736)DGGCGSTCGSSCVSST (SEQ ID NO :737)DGGCGSTCGTSCVSNAA (SEQ ID NO :738)IASDGGCGSTCGNACISSGS (SEQ ID NO :739)IDGSSDGGCMATCGNSCVSAA (SEQ ID NO :740)SDGGCGSTCGNACISSGS (SEQ ID NO :741)SDGGCGSTCGTSCVSNGA (SEQ ID NO :742)SDGGCGSTCTGSCVSSSS (SEQ ID NO :743)VGVASDGGCGSTCGTSCVSSGT (SEQ ID NO :744)YDGGCMATCGNACVSNAA (SEQ ID NO :745)DTSEGGCGATCGGHSCTSGVV (SEQ ID NO :746)IASDGGCGSTCGGNACISSGS (SEQ ID NO :747)IASDGGSGSTCGGNACISSGS (SEQ ID NO :748)ISSDGGCGSTCGGNACISSGS (SEQ ID NO :749)LASDGGCGSTCGGNACISSGS (SEQ ID NO :750)TVGASIASDGGFGSTCGDNACISSGS (SEQ ID NO :751)AASDGGCQATCGSGACTSSGA (SEQ ID NO :752)AASDGGCQATCGSGVCISSGA (SEQ ID NO :753)ESGGAVSLSAASDGGCAASCGGNACISSGA (SEQ ID NO :754)GITAASDGGCQATCGSGACTSSGA (SEQ ID NO :755)IASDGGCGATCGGNACISSGS (SEQ ID NO :756)SDGGCAATCGGNACVSSGS (SEQ ID NO :757)SDGGCAATCGSSACISSGS (SEQ ID NO :758)In some embodiments, the lanthipeptide of the present invention comprises a core peptide oftype (8) and is selected from the group consisting of: AELVPVPVPVEEWELETTVTRTPTPIVEACGTGDGCAKTCASSCASS (SEQ ID NO :759)AESVPVPVPAEEWELDTTVTRAPTPIVEACGTGDGCAKTCASSCASS (SEQ ID NO :760)APITGDDWQLTIAITDAPVPVAEDCDTSDGCESTCASSCTS (SEQ ID NO :761)APITGDDWQLTITITDSPVPVAEDCDTSDGCESTCASSCTS (SEQ ID NO :762)APITGDEWQLTIAITDAPVPVAEDCDTSDGCESTCASSCTS (SEQ ID NO :763)APMTGDNWQLTIAITDSPVPVAEACDTSDGCESTCASSCTS (SEQ ID NO :764)ATVIAALPLTEDEWALDITVTDAPRVVANEECDTNDGCKSTCDSACAS (SEQ ID NO :765)AVAEPVPADEWELKTTITRAPTPIVAACGTSDGCGSTCASACASS (SEQ ID NO :766)AVAEPVPVEEWELDTTVTRAPTPIVEACGTGDGCAKTCASSCASS (SEQ ID NO :767)DDWELDITITDAPRPAVANCDTNDTCESTCDSSCASD (SEQ ID NO :768)DDWKLDVIITDSPTVVPADCGTGDGCAGTCASACAS (SEQ ID NO :769)DEWQLDIAITDSPTVVPTDCGTGDGCGSTCASACAS (SEQ ID NO :770)DWELTTTVTTSPVPIVEACGSGDGCKSTCASSCISS (SEQ ID NO :771)EEWELDTSVTRAPAPIVEACGTGDGCAKSCASSCVSS (SEQ ID NO :772)EEWELDTTVTRTPTPIVEACGTGDGCAKTCASSCASS (SEQ ID NO :773)ESVPVPVPAEEWELDTTVTRAPTPIVEACGTGDGCAKTCASSCASS (SEQ ID NO :774)IATYQPPQPPAVLTEPVPADEWELKTTITRTPVPIVEACGTGDGCAKTCASSCASS (SEQ IDNO :775)IGEDGFALTVRVVTDDQSPSAETACDTSNGCASTCDSSCASA (SEQ ID NO :776)LTEPVPAEEWELKTTVTRTPTPIVEACGTGDGCASTCASSCASS (SEQ ID NO :777)MAQATATLASKTVEVPLSEDEWDLSTIITTSPMPITEMCDTNDGCAKTCASSCTSS (SEQ IDNO :778)MARVTAPLASKALDAPLSDDEWELETTITHSPTPIVEACDTSDGCKKTCASSCASS (SEQ IDNO :779)MASVAAPLATETVEVPLSDEWELTTTITRAPTPIVEACGTNDGCAASCASSCASS (SEQ IDNO :780)MATATAPLTTTTVEAPLSDEWELDTTITRSPAPIVEACDTNDGCASSCASSCTSS (SEQ IDNO :781)MDTATAPLTTSTVEVPLSDEWELDTTITRTPTPIVEACGTDDGCASSCASSCASS (SEQ IDNO :782)MNTLSQPQQTTELDEGFPVDWELTTTVTTSPVPIVEACTSGDGCKSTCASSCISS (SEQ IDNO :783)MPVPVPAEEWELDTTVTRAPVPIVEACGTGDGCAKTCASSCASS (SEQ ID NO :784)MSVPIAEAAAPAIKPTTVTLPFSDEDWELEVSITDAPLPAAPDACDTSDGCESSCASSCTSD (SEQID NO :785)MSVPTAEAAAPAIKPTTVTLPFSDEDWELEVSITDAPHPVAPDACDTSDGCESSCASSCTSD (SEQID NO :786)MSVQIAEKEKAAPPIAPTIATSPSSDEEWELEVSISDAPHPVATDDCDTSDGCESSCASSCTSD (SEQID NO :787)PQPTEAVAEAVPVEEWELDTTVTRTPTPIVEACGTGDGCAKTCASSCASS (SEQ ID NO :788)PQPTTAVAEPLPAEEWELDTTVTRAPVPIVEACGTGDGCAKTCASSCASS (SEQ ID NO :789)PRPAAAVAEPLPAEEWELDTTVTRAPVPIVEACGTGDGCAKTCASSCASS (SEQ ID NO :790)PTAAVAESVPVPIEEWELDTSVTRAPAPIVEACGTGDGCAKSCASSCVSS (SEQ ID NO :791)PTTAVVAEPLPVSGDEWELDTTVTRAPTPIVEACGTGDGCAKTCASSCASS (SEQ ID NO :792)SDDEGFLVDWELTTTVTTSPVPIVEACGSGDGCKSTCASSCISS (SEQ ID NO :793)TAFSGEDAPPIGPPAATLPFSGEDWELEVSVTDAPRPVASDDCDTSDGCESSCDSSCTSD (SEQ IDNO :794)VAELVPVPVPVEEWELETTVTRTPTPIVEACGTGDGCAKTCASSCASS (SEQ ID NO :795)VEAPQGLAAEEIPDEFELDMRVIEASVPLPVLACNTDDNCNPSCNSSCATAV (SEQ ID NO :796)VSVPVPAEEWELDTTVTRAPVPIVEACGTGDGCAKTCASSCASS (SEQ ID NO :797)DADLLPKACDTGDGCKPSCASSCASAV (SEQ ID NO :798)DADLLPKACGTGDGCKPSCASSCASAV (SEQ ID NO :799)DADLLPKACGTGDGCKPSCASSCTSAV (SEQ ID NO :800)DADLLPKACGTGDGCNPSCASSCTSAV (SEQ ID NO :801)DLLPKACGTGDGCAASCASSCASAV (SEQ ID NO :802)DLLPKACGTGDGCAPFCASSCASAV (SEQ ID NO :803)DLLPKACGTGDGCAPSCASSCASAV (SEQ ID NO :804)DLLPQACGTGDGCAASCASSCASAV (SEQ ID NO :805)DSDLLPKACGTGDGCKPSCASSCASAV (SEQ ID NO :806)IPASLKDVDLLDLDVTVTAEAGAEARPVACGSSDGCGASCASACISA (SEQ ID NO :807)ACGTGDGCASTCASSCASAV (SEQ ID NO :808)ACGTGDGCGATCSSSCTSAV (SEQ ID NO :809)ACGTGDGCKSTCASSCASAV (SEQ ID NO :810)DSDLLPRACDTGDGCKPSCASSCASAV (SEQ ID NO :811)GTGDGCGATCASACANSGV (SEQ ID NO :812)GTNDGCAATCPSSCVSRV (SEQ ID NO :813)PDACGTGDGCESTCASACASAV (SEQ ID NO :814)ACDSGDGCGTTCESACTSD (SEQ ID NO :815)ACDTSDTCGSTCASACASD (SEQ ID NO :816)ACDTSDTCGSTCGSACISD (SEQ ID NO :817)ACDTSDTCGSTCGSACISS (SEQ ID NO :818)CDTSDGCGSTCASACNSAV (SEQ ID NO :819)CVASDGCDTSDGCSSTCPSACASS (SEQ ID NO :820)DCGSGDGCGSTCASACAS (SEQ ID NO :821)DCGTGDGCGSTCASACAS (SEQ ID NO :822)DDAFVLDIHVISDVRPDLMPTACDTNDGCKKTCASACTST (SEQ ID NO :823)DRMAAGCGSSDGCGSTCASACTSAV (SEQ ID NO :824)GCDTSDGCSSTCPSACASS (SEQ ID NO :825)GQQTCDTSNGCPSTCESSCNSAM (SEQ ID NO :826)PIVSSCDTGDGCASTCASSCAS (SEQ ID NO :827)PVASDDCDTSDGCESSCASSCTSD (SEQ ID NO :828)QDLMPTACDTNDGCKGTCASACTST (SEQ ID NO :829)RCDSSDTCGSTCGSACASS (SEQ ID NO :830)RCDTSDGCAATCASSCASS (SEQ ID NO :831)RGCDTNDGCGSTCASACASR (SEQ ID NO :832)SCDTSDGCSSTCPSACASS (SEQ ID NO :833)SDGCDTSDGCSSTCPSACASS (SEQ ID NO :834)VMARDDCDTNDGCQSTCDSACLS (SEQ ID NO :835)YNSCDTSNGCSSTCPSACTSGS (SEQ ID NO :836)AACRTDDGCAATCASSCVSNV (SEQ ID NO :837)ACATDDGCASTCASSCVSNV (SEQ ID NO :838)ACGDGTNDGCDPSCASACLTGGV (SEQ ID NO :839)AQKACDTSNGCPPSCASSCNSAA (SEQ ID NO :840)CDTNDGCDPTCASSCVSS (SEQ ID NO :841)CGTNDGCAGTCASSCVTHSPN (SEQ ID NO :842)CKGNTDDGCDPTCASACVSHGA (SEQ ID NO :843)CKGNTDDGCDPTCASACVTGGV (SEQ ID NO :844)CTEGTNDGCDPTCASACVTGGV (SEQ ID NO :845)CTNGTDDGCDPTCASACVTGGV (SEQ ID NO :846)CTTNDGCAPTCASSCASAV (SEQ ID NO :847)DPLFACGEGTNDGCQPTCASACVTGGV (SEQ ID NO :848)DTPCTTDDGCDPTCDSSCNSSV (SEQ ID NO :849)EDAAAPCGTDDGCAPTCASSCNSGV (SEQ ID NO :850)ELLPTACDTNDGCKPSCASSCTST (SEQ ID NO :851)GHPLAACKGGTDDGCDPTCASACISDGV (SEQ ID NO :852)GRCATDDGCDPTCASSCISNA (SEQ ID NO :853)GTDDGCDPTCASACISDAV (SEQ ID NO :854)GTDDGCDPTCASACVSDGV (SEQ ID NO :855)GTSDGCAPTCASSCASAV (SEQ ID NO :856)GVGRCATDDGCDPTCASSCISNA (SEQ ID NO :857)HPLSACGNGTDDGCDPTCASACISDGV (SEQ ID NO :858)IPVACGTSDGCDPSCASSCTSAV (SEQ ID NO :859)ISDGCATDDGCDPTCASSCVSNA (SEQ ID NO :860)ISEGCGTDDGCDPTCASSCISNA (SEQ ID NO :861)LDMTDTEDIFTLDVRIVTDANVGDTGRGCDTSDGCAATCASSCVSNS (SEQ ID NO :862)MNPCTNGTDDGCDPTCASACVTGGV (SEQ ID NO :863)QGACTNGTDDGCDPTCASACVTGGV (SEQ ID NO :864)QVPCDTSNGCPATCDSSCNSAV (SEQ ID NO :865)TTNDNCPPSCASSCLSSV (SEQ ID NO :866)VAAPCGTDDGCDPTCASSCASNA (SEQ ID NO :867)VACGTSDGCAATCASSCVSRGAS (SEQ ID NO :868)VASACDTSDGCDPTCASSCISAV (SEQ ID NO :869)VASACDTSDGCDPTCASSCISTV (SEQ ID NO :870)VSRGCATDDGCDPTCASSCVSNA (SEQ ID NO :871)SACGTGDGCSSTCASSCASAV (SEQ ID NO :872)In some embodiments, the lanthipeptide of the present invention comprises a core peptide oftype (9) and is selected from the group consisting of: ADTEDCTSDTCGSTPGSAGIANC (SEQ ID NO :873)ASMVPSADCTSDNCGETPGSAGIA (SEQ ID NO :874)ASVIPSADCTSDGCGQTPGSAGITN (SEQ ID NO :875)ASVVSSEDCTGDGCGPTPCGPGADL (SEQ ID NO :876)VSGVATEECTSDNCGDTPGSAGIA (SEQ ID NO :877)DCTSDNCSATAESAGVTCEQQ (SEQ ID NO :878)GFDSADCTSDNCSATEDSAGVTCDQVQLGCAG (SEQ ID NO :879)GFDSEECTSDNCTGTDDSAGVTC (SEQ ID NO :880)GFDSEPCSGDNCTGTGDSAGVTC (SEQ ID NO :881)GSSSEECTSDGCTGSTEKSGC (SEQ ID NO :882)In some embodiments, the lanthipeptide of the present invention comprises a core peptide oftype (10) and is selected from the group consisting of: AVIAMTDDNCGTTCPSTCTTSAGA (SEQ ID NO :883)In some embodiments, the lanthipeptide of the present invention comprises a core peptide oftype (11) and is selected from the group consisting of: MCATDDGCGTTCSTSACSTSSNDPS (SEQ ID NO :884)MCATDDGCGTTCSTSACTTSSNDPS (SEQ ID NO :885)In some embodiments, the lanthipeptide of the present invention comprises a core peptide oftype (12) and is selected from the group consisting of: ACATDDGCASTCASSCASS (SEQ ID NO :886)MPAACGTGDGCAASCASSCASAV (SEQ ID NO :887)TCGTGDGCAASCASSCASAV (SEQ ID NO :888)ACTTNDGCAPSCASSCTSSSC (SEQ ID NO :889)ANAACATEDGCAASCASSCASDV (SEQ ID NO :890)AGCNTDDGCAASCASSCASNV (SEQ ID NO :891)In some embodiments, the lanthipeptide of the present invention is selected from the group consisting of: MCSTSDGCGSTCSTSACSTSACSTSSNDPL (SEQ ID NO :892)QWSGTACVLCRTWLGHHPAERSRVLATVNSHPLRACTPNCEARS (SEQ IDNO :893)ARRRRNSSGSCFPTVRPEAVRRRRISATSSSVSC (SEQ ID NO :894)DTDDNCGGPQDSAGTTCPSAG (SEQ ID NO :895)ITSDGGCGSTCGGTACISSGS (SEQ ID NO :896)TCTVMGNCTTSCGSWTQTPLAC (SEQ ID NO :897)PSADCTSDGCTTTKTVYPC (SEQ ID NO :898)In some embodiments, the lanthipeptide of the present invention has an amino acid sequencethat comprises one or more conservative substitution(s) provided that the core peptideconserves its consensus formula as taught by the present invention. As used herein, the term“conservative substitution” is one in which an amino acid is substituted for another amino acid that has similar properties, such that one skilled in the art of peptide chemistry would expect the secondary structure and hydropathic nature of the polypeptide to be substantially unchanged. Amino acid substitutions are generally therefore based on the relative similarity of the amino acid side-chain substituents, for example, their hydrophobicity, hydrophilicity, charge, size, and the like. Exemplary substitutions that take various of the foregoing characteristics into consideration are well known to those of skill in the art and include: arginine and lysine; glutamate and aspartate; serine and threonine; glutamine and asparagine; and valine, leucine and isoleucine. Amino acid substitutions may further be made on the basis of similarityin polarity, charge, solubility, hydrophobicity, hydrophilicity and / or the amphipathic nature ofthe residues. For example, negatively charged amino acids include aspartic acid and glutamic acid; positively charged amino acids include lysine and arginine; and amino acids with uncharged polar head groups having similar hydrophilicity values include leucine, isoleucine and valine; glycine and alanine; asparagine and glutamine; and serine, threonine, phenylalanine and tyrosine. Other groups of amino acids that may represent conservative changes include: (1) ala, pro, gly, glu, asp, gln, asn, ser, thr; (2) cys, ser, tyr, thr; (3) val, ile, leu, met, ala, phe; (4) lys, arg, his; and (5) phe, tyr, trp, his. Other families of amino acid residues having similar side chains have been defined in the art. These families include amino acids with basic side chains (e.g., lysine, arginine, histidine), acidic side chains (e.g., aspartic acid, glutamic acid), uncharged polar side chains (e.g., glycine, asparagine, glutamine, serine, threonine, tyrosine, cysteine, tryptophan), nonpolar side chains (e.g., alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine), beta-branched side chains (e.g., threonine, valine, isoleucine) and aromatic side chains (e.g., tyrosine, phenylalanine, tryptophan, histidine).In some embodiments, the lanthipeptide of the present invention has an animo acid having atleast 90% of identity with one amino acid sequence as described above, provided that the corestructure of said lanthipeptide respects the core structure of formula (I), (II), (III), (IV), (V) or(VI). As used herein, the “percent identity” between the two sequences is a function of the number of identical positions shared by the sequences (i.e., % identity = number of identical positions / total number of positions x 100), taking into account the number of gaps, and the length of each gap, which need to be introduced for optimal alignment of the two sequences. The comparison of sequences and determination of percent identity between two sequences can be accomplished using a mathematical algorithm, as described below. The percent identity between two amino acid sequences can be determined using the Needleman and Wunsch algorithm (Needleman, Saul B. & Wunsch, Christian D. (1970). "A general method applicable to the search for similarities in the amino acid sequence of two proteins". Journal of Molecular Biology.48 (3): 443–53.). The percent identity between two nucleotide or amino acid sequences may also be determined using for example algorithms such as EMBOSS Needle (pair wise alignment; available at www.ebi.ac.uk). For example, EMBOSS Needle may be used with a BLOSUM62 matrix, a “gap open penalty” of 10, a “gap extend penalty” of 0.5, a false “end gap penalty”, an “end gap open penalty” of 10 and an “end gap extend penalty” of 0.5. In general, the “percent identity” is a function of the number of matching positions divided by the number of positions compared and multiplied by 100. For instance, if 6 out of 10 sequence positions are identical between the two compared sequences after alignment, then the identity is 60%. The % identity is typically determined over the whole length of the query sequence on which the analysis is performed. Two molecules having the same primary amino acid sequence or nucleic acid sequence are identical irrespective of any chemical and / or biological modification. According to the invention a first amino acid sequence having at least 70% of identity with a second amino acid sequence means that the first sequence has 70; 71; 72; 73; 74; 75; 76; 77; 78; 79; 80; 81; 82; 83; 84; 85; 86; 87; 88; 89; 90; 91; 92; 93; 94; 95; 96; 97; 98; 99 or 100% of identity with the second amino acid sequence.In some embodiments, the lanthipeptide of the present invention can further comprise a cellpermeating peptide (CPP). The cell permeating peptide can assist in facilitating the entry of the antibiotic peptide into the target cell (i.e., bacterium). Various cell permeating peptides are known in the art. For example, additional CPPs known in the art can be found on online databases (i.e., http: / / crdd.osdd.net / raghava / cppsite ), in Oikawa et al., (Screening of a Cell- Penetrating Peptide Library in Escherichia coli: Relationship between Cell Penetration Efficiency and Cytotoxicity. ACS Omega 2018, 3, 16489-164), the disclosure of each is incorporated by reference in its entirety. The peptides described herein can be prepared in a variety of ways known to one skilled in the art of peptide synthesis or variations thereon as appreciated by those skilled in the art. For example, synthetic peptides are prepared using known techniques of solid phase, liquid phase, or peptide condensation, or any combination thereof. Alternatively, the peptide of the presentinvention can be synthesized by recombinant DNA techniques well-known in the art and asdescribed herein after. Polynucleotides and host cells of the present invention: A further object of the present invention relates to a polynucleotide that encodes one or morelanthipeptide(s) of the present invention.In some embodiments, the polynucleotide of the present invention is a messenger RNA (mRNA). A further object of the present invention relates to a vector, preferably an expression vector,containing the polynucleotide of the present invention.As used herein, the term “vector” refers to a nucleic acid molecule capable of transporting another nucleic acid to which it has been linked. In some embodiments, the vector of the present invention is a plasmid. As used herein, the term “plasmid” has its general meaning in the art and refers to a circular double stranded DNA loop into which additional DNA segments can be ligated.In some embodiments, the vector of the present invention is a viral vector (e.g., bacteriophages,replication defective retroviruses, adenoviruses and adeno-associated viruses). In some embodiments, certain vectors are capable of autonomous replication in a host cell into which they are introduced (e.g., bacterial vectors having a bacterial origin of replication and episomal mammalian vectors). A further object of the present invention relates to a host cell that has been transfected, infected or transformed by a polynucleotide and / or a vector according to the present invention. As used herein, the terms “host cell” and “recombinant host cell” are used interchangeably herein. It is understood that such terms refer not only to the particular subject cell but also to the progeny or potential progeny of such a cell. Because certain modifications may occur in succeeding generations due to either mutation or environmental influences, such progeny may not, in fact, be identical to the parent cell, but are still included within the scope of the term as used herein. Moreover, certain vectors are capable of directing the expression of genes to which they are operatively-linked. Such vectors are referred to herein as “expression vectors”. In general, expression vectors of utility in recombinant DNA techniques are often in the form of plasmids., which serve equivalent functions.The recombinant expression vectors of the present invention comprise the polynucleotide ofthe present invention in a form suitable for expressing it in a host cell, which means that therecombinant expression vectors include one or more regulatory sequences, selected on the basis of the host cells to be used for expression, that is operatively-linked to the nucleic acid sequence to be expressed. Within a recombinant expression vector, the term “operably-linked” is intended to mean that the nucleotide sequence of interest is linked to the regulatory sequences in a manner that allows for expression of the nucleotide sequence (e.g., in an in vitro transcription / translation system or in a host cell when the vector is introduced into the host cell). As used herein, the term “regulatory sequence” is intended to include promoter sequences, polyadenylation signals, transcription termination sequences, upstream regulatory domains, origins of replication, internal ribosome entry sites ("IRES"), enhancers, and the like, which collectively provide for the replication, transcription and translation of a coding sequence in a host cell. Regulatory sequences include those that direct constitutive expression of a nucleotide sequence in many types of host cell and those that direct expression of the nucleotide sequence only in certain host cells (e.g., tissue-specific regulatory sequences). Typically, the regulatory sequence is a "promoter" sequence, which is used herein in its ordinary sense to refer to a nucleotide region comprising a DNA regulatory sequence, wherein the regulatory sequence is derived from a gene which is capable of binding RNA polymerase and initiating transcription of a downstream (3'-direction) coding sequence. Transcription promoters can include "inducible promoters" (where expression of a polynucleotide sequence operably linked to the promoter is induced by an analyte, cofactor, regulatory protein, etc.), "repressible promoters" (where expression of a polynucleotide sequence operably linked to the promoter is induced by an analyte, cofactor, regulatory protein, etc.), and "constitutive promoters”. It will be appreciated by those skilled in the art that the design of the expression vector can depend on such factors as the choice of the host cell to be transformed, the level of expressionof protein desired, etc. The expression vectors of the present invention can be introduced intohost cells to thereby produce the lanthipeptides of the present invention, encoded by thepolynucleotides as described herein.The recombinant expression vectors of the present invention can be designed for production ofthe peptides of interest in prokaryotic or eukaryotic cells. For example, the lanthipeptides of thepresent invention can be expressed in bacterial cells such as Escherichia coli or actinobacteriacells, insect cells (using baculovirus expression vectors), yeast cells or mammalian cells. Inparticular, the host cell of the present invention is a bacterial cell. Suitable host cells are preferably host cells that naturally express or that are engineered toexpress one or more biosynthetic gene cluster(s). As used herein, the term "biosynthetic genecluster" refers to a physically clustered group of two or more genes in a particular genome that together encode a biosynthetic pathway for the production of one or more specialised metabolites, including the lanthipeptides of the present invention. Typically, the biosynthetic gene cluster of the present invention comprises one or more nucleic acid sequence(s) that encode for a lanthionine synthetase (such as LanC). In some embodiments, the host cell is selected from the phylum of actinobacteria. As used herein, the term “actinobacteria” has its general meaning in the art and refers to a phylum of bacteria that are characterized by their high G+C content in their DNA, their filamentous or branching morphology, and their ability to form spores. Actinobacteria are found in various habitats, such as soil, water, plants, animals, and humans. They are known for their diverse secondary metabolism, which enables them to produce a variety of bioactive compounds, suchas antibiotics, antifungals, anticancer agents, immunomodulators, and enzymes. Non-limitingexamples of Actinobacteria include bacteria of the genera Actinomyces, Arthrobacter, Corynebacterium, Prankia, Micrococcus, Micromonospora, Mycobacterium, Propionibacterium, and Streptomyces.Expression of peptides in prokaryotes is most often carried with vectors containing constitutiveor inducible promoters directing the expression of the peptides of interest. In some embodiment, the vector encodes for the peptides of interest that are fused to one or more heterologous sequences such as purification tags, for example: ^-galactosidase, glutathione-S-transferase, green fluorescent proteins (GFP), and epitope tags such as FLAG, myc tag, poly histidine (e.g., 6HIS). In some embodiments, the fusion protein of the present invention comprises an AviTag® sequence. The AviTag® sequence (U.S. Pat. Nos.5,932,433, 5,874,239 & 5,723,584) is a unique peptide, just 15 residues long, that is recognized by biotin ligase (Schatz P. J., 1993).Typically, the tags typically serve three purposes: (i) to increase expression of recombinantpeptide; (ii) to increase the solubility of the recombinant peptide; and (iii) to aid in thepurification of the recombinant peptide by acting as a ligand in affinity purification. Often, infusion expression vectors, a proteolytic cleavage site is introduced at the junction of the fusionmoiety and the recombinant peptide to enable separation of the recombinant peptide from thefusion moiety subsequent to purification of the fusion protein. Typical fusion expression vectors include pGEX (Pharmacia Biotech Inc; Smith and Johnson, 1988. Gene 67: 31-40), pMAL (New England Biolabs, Beverly, Mass.) and pRIT5 (Pharmacia, Piscataway, N.J.) that fuse glutathione S-transferase (GST), maltose E binding protein, or protein A, respectively, to thetarget recombinant protein. Examples of suitable inducible non-fusion E. coli expressionvectors include pTrc (Amrann et al., (1988) Gene 69:301-315) and pET 11d (Studier et al., Gene Expression Technology: Methods in Enzymology 185, Academic Press, San Diego, Calif. (1990) 60-89)—not accurate, pET11a-d have N terminal T7 tag. The vector of the present invention can be introduced into prokaryotic or eukaryotic cells via conventional transformation or transfection techniques. As used herein, the terms “transformation” and “transfection” are intended to refer to a variety of art-recognized techniques for introducing foreign nucleic acid (e.g., DNA) into a host cell, including calcium phosphate or calcium chloride co-precipitation, DEAE-dextran-mediated transfection, lipofection, or electroporation.The host cell of the present invention, such as a prokaryotic or eukaryotic host cell in culture,can be used to produce (i.e., express) the lanthipeptides of the present invention. Accordingly,the invention further provides methods for producing the lanthipeptides of the present inventionusing the host cells of the present invention. In some embodiments, the method comprises culturing the host cell of the present invention (into which a recombinant expression vectorencoding protein of the present invention has been introduced) in a suitable medium such thatthe lanthipeptide of the present invention is produced. In some embodiments, the method furthercomprises isolating the lanthipeptide of the present invention from the medium or the host cell.Uses of the lanthipeptides: The lanthipeptides of the present invention could have diverse applications. In some embodiments, the lanthipeptides could be used to control phage propagation and protect beneficial microbial communities used in the food industry and agriculture. In some embodiments, the lanthipeptides of the present invention are particularly suitable for enhancing the production of microorganisms and / or their growth by-products by treating and / or preventing bacteriophage contamination of bacterial cultures. Advantageously, thelanthipeptides of the present invention can help reduce the likelihood of total and / or partialculture loss through the direct control of bacteriophages that may be present in the culture.Advantageously, compared to current sterilization methods that work by controlling all microorganisms that are present, the lanthipeptides of the present invention can effectively control bacteriophages without harming the bacteria that are being cultivated. Thus, the methods of the subject invention can allow for treatment and / or prevention of bacteriophage lysis without disrupting the fermentation process. Thus, the present invention provides methods for treating and / or preventing bacteriophage contamination and / or bacteriophage lysis during cultivation of a microorganism. In some embodiments, the lanthipeptides of the present invention are particularly suitable for producing microorganisms and / or growth by-products thereof, as well as the production of biomass (e.g., viable cellular material), extracellular metabolites (e.g. small molecules, growth by-products and proteins), residual nutrients and / or intracellular components (e.g. enzymes and other proteins).Typically, the lanthipeptides of the present invention can be applied to the nutrient mediumprior to, or concurrently with, inoculation, and / or at any time thereafter throughout cultivation. The microorganism is cultivated for an amount of time to produce a culture having a desiredcell density and / or a desired concentration of growth by-products. Alternatively, the microorganism is directly engineered to express one or more lanthipeptide(s) of the present invention (i.e. that is a host cell as described above). In some embodiments, the microorganism of interest is co cultured with a second microorganism directly engineered to express one or more lanthipeptide(s) of the present invention (i.e. that is a host cell as described above). In some embodiments, the microorganisms are bacteria, including Gram-positive and Gram- negative bacteria. The bacteria may be, spore-forming, or not. The bacteria may be motile or sessile. The bacteria may be anaerobic, aerobic, microaerophilic, facultative anaerobes and / or obligate aerobes. Bacteria species suitable for use according to the present invention include,for example, Acinetobacter spp. (e.g., A. calcoaceticus, A. venetianus); Agrobacterium spp.(e.g., A. radiobacter), Azotobacter spp. (A. vinelandii, A. chroococcum), Azospirillum spp. (e.g.,A. brasiliensis), Bacillus spp. (e.g., B. amyloliquefaciens, B. firmus, B. laterosporus, B.licheniformis, B. megaterium, B. mucilaginosus, B. subtilis, B. coagulans), Chlorobiaceae spp.,Dyadobacter fermenters, Frankia spp., Frateuria (e.g., F. aurantia), Klebsiella spp.,Microbacterium spp. (e.g., M. laevaniformans), Pantoea spp. (e.g., P. agglomerans),Pseudomonas spp. (e.g., P. aeruginosa, P. chlororaphis, P. chlororaphis subsp. aureofaciens(Kluyver), P. putida), Rhizobium spp., Rhodospirillum spp. (e.g., R. rubrum), Sphingomonasspp. (e.g., S. paucimobilis), and / or Xanthomonas spp.In some embodiments, the bacteria species suitable for use according to the present inventioninclude actinobacteria. In particular, actinobacteria have diverse metabolic capabilities andecological roles. They are widely used in industry for various purposes, such as: -producing antibiotics and other bioactive compounds that have medical and agriculturalapplications. For example, actinobacteria are the source of streptomycin, erythromycin, tetracycline, rifampicin, and many other drugs. -degrading organic pollutants and xenobiotics that are harmful to the environment andhuman health. For example, actinobacteria can biodegrade aromatic compounds, chlorinated compounds, pesticides, herbicides, and explosives. -improving soil fertility and plant growth by fixing nitrogen, solubilizing phosphate,producing plant hormones, and suppressing plant pathogens. For example, actinobacteria are involved in the formation of root nodules in legumes and some non- legumes, and can enhance the availability of phosphorus and other nutrients in the soil. -synthesizing novel biomaterials and biocatalysts that have industrial andbiotechnological applications. For example, actinobacteria can produce exopolysaccharides, polyhydroxyalkanoates, melanins, carotenoids, and enzymes that have potential uses in food, textile, cosmetic, and pharmaceutical industries. In some embodiments, the method is effective for treating and / or preventing infections from bacteriophages that are lytic and / or lysogenic. In some embodiments, the bacteriophage is a member of a viral family selected from Myoviridae, Siphoviridae, Podoviridae, Lipothrixviridae, Rudiviridae, Ampullaviridae, Bicaudaviridae, Clavaviridae, Corticoviridae, Cystoviridae, Fuselloviridae, Globuloviridae, Guttavirus, Inoviridae, Leviviridae, Microviridae, Plasmaviridae, and Tectiviridae. In some embodiments, the culturing methods of the present invention are used for producing a growth by-product of a microorganism. The growth by-product can be, for example, a biosurfactant, enzyme, biopolymer, acid, solvent, amino acid, nucleic acid, peptide, protein, lipid and / or carbohydrate. In some embodiments, the growth by-product is a biosurfactant, suchas a glycolipid or a lipopeptide. In some embodiments, the microbial growth by-productsinclude metabolites. As used herein, the term “metabolite” refers to any substance producedby metabolism (e.g., a growth by-product), or a substance necessary for taking part in a particular metabolic process, for example, enzymes, enzyme inhibitors, biopolymers, acids, solvents, gases, proteins, peptides, amino acids, alcohols, pigments, pheromones, hormones, lipids, ectotoxins, endotoxins, exotoxins, carbohydrates, antibiotics, anti-fungals, anti-virals and / or other bioactive compounds. In some embodiments, the growth by-product is a biopolymer, such as, for example, levan, xanthan gum, alginate, hyaluronic acid, PGAs, PHAs,cellulose, and lignin. In some embodiments, the growth by-product is a bioemulsifier, such as,for example, emulsan, alasan, or liposan. In some embodiments, the growth by-product is aprotein, a lipid, a carbon source, an amino acid, a mineral or a vitamin. In some embodiments,the growth by-products are enzymes such as, for example, oxidoreductases, transferases, hydrolases, lyases, isomerases and / or ligases. Specific types and / or subclasses of enzymes according to the subject invention can also include, but are not limited to, nitrogenases, proteases, flavodoxins, amylases, glycosidases, cellulases, glucosidases, glucanases, galactosidases, moannosidases, sucrases, dextranases, hydrolases, methyltransferases, phosphorylases, dehydrogenases (e.g., glucose dehydrogenase, alcohol dehydrogenase), oxygenases (e.g., alkane oxygenases, methane monooxygenases, dioxygenases), hydroxylases (e.g., alkane hydroxylase), esterases, lipases, ligninases, mannanases, oxidases, laccases, tyrosinases, cytochrome P450 enzymes, peroxidases (e.g., chloroperoxidase and otherhaloperoxidases), and lactases. In some embodiments, the growth by-products includeantibiotic compounds, such as, for example, aminoglycosides, amylocyclicin, bacitracin, bacillaene, bacilysin, bacilysocin, corallopyronin A, difficidin, etnangien gramicidin, β-lactams, licheniformin, macrolactinsublancin, oxydifficidin, plantazolicin, ripostatin,spectinomycin, subtilin, tyrocidine, and / or zwittermicin A. In some embodiments, an antibioticcan also be a type of biosurfactant. In some embodiments, the growth by-products include otherbioactive compounds, such as, for example, butanol, ethanol, acetate, ethyl acetate, lactate, acetoin, benzoic acid, 2,3-butanediol, beta-glucan, indole-3-acetic acid (IAA), lovastatin, aurachin, kanosamine, reseoflavin, terpentecin, pentalenolactone, thuringiensin (β-exotoxin), polyketides (PKs), terpenes, terpenoids, phenyl-propanoids, alkaloids, siderophores, as well as ribosomally and non-ribosomally synthesized peptides, to name a few.In some embodiments, the lanthipeptides of the present invention can be used in agriculture.For example, methods are provided wherein the one or more lanthipeptides of the presentinvention is / are applied to a plant and / or its environment to treat and / or prevent the spread ofpests and / or diseases. In some embodiments, the lanthipeptides can be used to prevent spoilage of food, prolong the consumable life of food, and / or to prevent food-borne illnesses. For example, methods are provided wherein the lanthipeptides can be applied to a food product, such as fresh produce, baked goods, meats, and post-harvest grains, to prevent undesirable microbial growth. In some embodiments, the lanthipeptides of the present invention are particularly suitable for therapeutic purposes.Thus, a further object of the present invention relates to a method of therapy in a subject in needthereof comprising administering to the subject a therapeutically effective amount of one or more lanthipeptide(s) of the present invention. A further object of the present invention also relates to a method of therapy in a subject in need thereof comprising administering to the subject a therapeutically effective amount of one ormore polynucleotide(s) of the present invention.In some embodiments, the subject can be human or any other animal (e.g., birds and mammals) (e.g., domestic animals such as cats and dogs; livestock and farm animals such as horses, cows, pigs, chickens, etc.). Typically said subject is a mammal including a non-primate (e.g., a camel, donkey, zebra, cow, pig, horse, goat, sheep, cat, dog, rat, and mouse) and a primate (e.g., a monkey, chimpanzee, and a human). In some embodiments, the subject is a non-human animal. In some embodiments, the subject is a farm animal or pet. In some embodiments, the subject is a human. In some embodiments, the subject is a human infant. In some embodiments, the subject is a human child. In some embodiments, the subject is a human adult. In some embodiments, the subject is an elderly human. In some embodiments, the subject is a premature human infant.In some embodiments, the lanthipeptides can be used to enhance animal health. For example,methods are provided wherein the lanthipeptides can be applied to animal feed or water, ormixed with the feed or water, and used to prevent the spread of viral disease in livestock andaquaculture operations.In some embodiments, the lanthipeptides can be used to enhance human health.In particular, the lanthipeptides of the present invention are particularly suitable for treating a viral infection. Thus, a further object of the present invention relates to a method of treating a viral infection in a subject in need thereof comprising administering to the subject a therapeutically effective amount of one or more lanthipeptide(s) of the present invention. A further object of the present invention also relates to a method of treating a viral infection ina subject in need thereof comprising administering to the subject a therapeutically effectiveamount of one or more polynucleotide(s) of the present invention.As used herein, the term “treatment" is understood as meaning the therapeutic effect produced on an animal or human by the active substances when they are administered to said animal or human at the time of contamination of said animal or human by the virus or after contamination. The method herein disclosed can be carried-out during the primary infection phase, during the asymptomatic phase or after the appearance of clinical signs or symptoms of the disease. In some embodiments, the method herein disclosed is carried-out during the primary infection phase. In some embodiments, the method herein disclosed is carried-out after the primary infection phase, i.e. in the chronic phase (which may be asymptomatic or after the appearance of clinical signs or symptoms of the disease). In some embodiments, the therapeutic intervention takes place within 24 or 48 hours of said animal or human being exposed to said virus, as quickly as possible. Said treatment includes any curative effect obtained by virtue of the implementation of the method herein disclosed, along with the improvement in the clinical signs or symptoms observed in the animal or patient as well as the improvement in the condition of the animal or patient. The term includes, in particular, the effects obtained as a consequence of inhibiting viral replication and / or inhibiting cell death and inflammation induced by the virus. Accordingly, the term "treatment" covers the slowing down, reduction, interruption, and stopping of the viral infection and / or of the harmful consequences of the viral infection; treatment does not necessarily require the complete removal of all the clinical signs of the viral infection and the symptoms of the disease, nor the complete elimination of the virus. Themethod herein disclosed can be carried-out to an animal or human at risk of developing a viralinfection (prophylaxis) or after contamination by the virus has taken place, in particular after manifestation of the first clinical signs or symptoms of the disease, for example after proteins or antibodies specific to the said virus have been detected in the blood of the animal or patient (treatment). In some embodiments, the viral infection comprises infection by a RNA virus or a DNA virus. In some embodiments, the subject is infected by one or more viruses selected from the group consisting of Arenaviridae, Astroviridae, Birnaviridae, Bromoviridae, Bunyaviridae, Caliciviridae, Closteroviridae, Comoviridae, Cystoviridae, Flaviviridae, Flexiviridae, Hepevirus, Leviviridae, Luteoviridae, Mononegavirales, Mosaic Viruses, Nidovirales, Nodaviridae, Orthomyxoviridae, Picobirnavirus, Picornaviridae, Potyviridae, Reoviridae, Retroviridae, Sequiviridae, Tenuivirus, Togaviridae, Tombusviridae, Totiviridae, Tymoviridae,Hepadnaviridae, Herpesviridae, Paramyxoviridae or Papillomaviridae viruses. Relevanttaxonomic families of RNA viruses include, without limitation, Astroviridae, Birnaviridae, Bromoviridae, Caliciviridae, Closteroviridae, Comoviridae, Cystoviridae, Flaviviridae, Flexiviridae, Hepevirus, Leviviridae, Luteoviridae, Mononegavirales, Mosaic Viruses, Nidovirales, Nodaviridae, Orthomyxoviridae, Picobirnavirus, Picornaviridae, Potyviridae, Reoviridae, Retroviridae, Sequiviridae, Tenuivirus, Togaviridae, Tombusviridae, Totiviridae,and Tymoviridae viruses. In some embodiments, the viral infection comprises infection by oneor more viruses selected from the group consisting of adenovirus, rhinovirus, hepatitis, immunodeficiency virus, polio, measles, Ebola, Coxsackie, Rhino, West Nile, small pox, encephalitis, yellow fever, coronavirus, Dengue, influenza (including human, avian, and swine), lassa, lymphocytic choriomeningitis, junin, machuppo, guanarito, hantavirus, Rift Valley Fever, La Crosse, California encephalitis, Crimean-Congo, Marburg, Japanese Encephalitis, Kyasanur Forest, Venezuelan equine encephalitis, Eastern equine encephalitis, Western equine encephalitis, severe acute respiratory syndrome (SARS), parainfluenza, respiratory syncytial, Punta Toro, Tacaribe, pachindae viruses, adenovirus, Dengue fever, influenza A and influenza B (including human, avian, and swine), junin, measles, parainfluenza, Pichinde, punta toro, respiratory syncytial, rhinovirus, Rift Valley Fever, severe acute respiratory syndrome (SARS), Tacaribe, Venezuelan equine encephalitis, West Nile and yellow fever viruses, tick-borne encephalitis virus, Japanese encephalitis virus, St. Louis encephalitis virus, Murray Valley virus, Powassan virus, Rocio virus, louping-ill virus, Banzi virus, Ilheus virus, Kokobera virus, Kunjin virus, Alfuy virus, bovine diarrhea virus, and Kyasanur forest disease. In some embodiments, the method herein disclosed is carried-out in an animal or human before said animal or human is exposed to said virus, during exposure to said virus or after exposure to said virus. Intervention after exposure to the virus can be carried out at any time but will preferably be carried out as quickly as possible after exposure, in particular within 48 hours of the animal or human being exposed to said virus. Furthermore, it is also possible to envisage a plurality of successive interventions, so as to increase the beneficial effects of the treatment. In order to increase the chances of cure, or at least prolong the life expectancy of the animal or human, or the prophylactic effect, it is possible in particular to carry out one or more successive interventions before the animal or human is exposed to the virus and / or during exposure to the virus and / or after exposure to the virus, in particular within 48 hours of said animal or human being exposed to said virus. The method herein disclosed can be used in the prophylaxis and / or treatment of a viral infection, in the primary infection phase and / or in the chronic phase (which may be asymptomatic or after the appearance of clinical signs or symptoms of the disease). The animal or human infected by the virus may be in the primary infection phase or in the chronic phase. The method herein disclosed can also be used to prevent, reduce and / or inhibit viral replication in an animal or human infected by a virus, in the primary infection phase and / or in the chronic phase (which may be asymptomatic or after the appearance of clinical signs or symptoms of the disease). As used herein, the term "prophylaxis" or "prevent a viral infection" denotes any degree of retardation in the time of appearance of clinical signs or symptoms of the viral infection, as well as any degree of inhibition of the severity of the clinical signs or symptoms of the viral infection,including, but not being limited to, the total prevention of the viral infection. This requires thatthe method herein discloses is carried-out in the subject likely to be contaminated by a virus before any clinical sign or symptom of the disease appears. The prophylactic intervention can take place before said animal or human is exposed to the virus responsible for the viral infection,or at the time of exposure. Such a prophylactic administration serves to prevent and / or reducethe severity of any subsequent infection. Compositions: A further object of the present invention relates to a composition comprises an amount of one or more lanthipeptide(s) of the present invention. A further object of the present invention relates to a composition comprises an amount of one or more polynucleotides(s) of the present invention. In some embodiments, the composition of the present invention is a pharmaceutical composition.Thus, a further object of the present invention relates to a pharmaceutical compositioncomprising one or more lanthipeptide(s) of the present invention and a pharmaceutically acceptable carrier.Thus, a further object of the present invention relates to a pharmaceutical compositioncomprising one or more polynucleotides(s) of the present invention and a pharmaceutically acceptable carrier. As used herein, the term “pharmaceutical composition” refers to a composition described herein, or pharmaceutically acceptable salts thereof, with other agents such as carriers and / or excipients. The pharmaceutical compositions as provided herewith typically include a pharmaceutically acceptable carrier. As used herein, the term “pharmaceutically acceptable carrier” includes any and all solvents, diluents, or other liquid vehicle, dispersion or suspension aids, surface active agents, isotonic agents, thickening or emulsifying agents, preservatives, solid binders, lubricants and the like, as suited to the particular dosage form desired. Remington's Pharmaceutical-Sciences, Sixteenth Edition, E. W. Martin (Mack Publishing Co., Easton, Pa., 1980) discloses various carriers used in formulating pharmaceutical compositions and known techniques for the preparation thereof. Pharmaceutically acceptable carriers that may be used in these compositions include, but are not limited to, ion exchangers, alumina, aluminum stearate, lecithin, serum proteins, such as human serum albumin, buffer substances such as phosphates, glycine, sorbic acid, potassium sorbate, partial glyceride mixtures of saturated vegetable fatty acids, water, salts or electrolytes, such as protamine sulfate, disodium hydrogen phosphate, potassium hydrogen phosphate, sodium chloride, zinc salts, colloidal silica, magnesium trisilicate, polyvinyl pyrrolidone, cellulose-based substances, polyethylene glycol, sodium carboxymethylcellulose,polyacrylates, waxes, polyethylene-polyoxypropylene- block polymers, polyethylene glycoland wool fat. For use in administration to a patient, the composition will be formulated for administration to the patient. The compositions of the present invention may be administered orally, parenterally, by inhalation spray, topically, rectally, nasally, buccally, vaginally or via an implanted reservoir. The used herein includes subcutaneous, intravenous, intramuscular, intra-articular, intra-synovial, intrasternal, intrathecal, intrahepatic, intralesional and intracranial injection or infusion techniques. Sterile injectable forms of the compositions of this invention may be aqueous or an oleaginous suspension. These suspensions may be formulated according to techniques known in the art using suitable dispersing or wetting agents and suspending agents. The sterile injectable preparation may also be a sterile injectable solution or suspension in a non-toxic parenterally acceptable diluent or solvent, for example as a solution in 1,3-butanediol. Among the acceptable vehicles and solvents that may be employed are water, Ringer's solution and isotonic sodium chloride solution. In addition, sterile, fixed oils are conventionally employed as a solvent or suspending medium. For this purpose, any bland fixed oil may be employed including synthetic mono-or diglycerides. Fatty acids, such as oleic acid and its glyceride derivatives are useful in the preparation of injectables, as are natural pharmaceutically-acceptable oils, such as olive oil or castor oil, especially in theirpolyoxyethylated versions. These oil solutions or suspensions may also contain a long-chainalcohol diluent or dispersant, such as carboxymethyl cellulose or similar dispersing agents that are commonly used in the formulation of pharmaceutically acceptable dosage forms including emulsions and suspensions. Other commonly used surfactants, such as Tweens, Spans and other emulsifying agents or bioavailability enhancers which are commonly used in the manufacture of pharmaceutically acceptable solid, liquid, or other dosage forms may also be used for the purposes of formulation. The compositions of this invention may be orally administered in any orally acceptable dosage form including, but not limited to, capsules, tablets, aqueous suspensions or solutions. In the case of tablets for oral use, carriers commonly used include lactose and corn starch. Lubricating agents, such as magnesium stearate, are also typically added. For oral administration in a capsule form, useful diluents include, e.g., lactose. When aqueous suspensions are required for oral use, the active ingredient is combined with emulsifying and suspending agents. If desired, certain sweetening, flavoring or coloring agents may also be added. Alternatively, the compositions of this invention may be administered in the form of suppositories for rectal administration. These can be prepared by mixing the agent with a suitable non-irritating excipient that is solid at room temperature but liquid at rectal temperature and therefore will melt in the rectum to release the drug. Such materials include cocoa butter, beeswax and polyethylene glycols. The compositions of this invention may also be administered topically, especially when the target of treatment includes areas or organs readily accessible by topical application, including diseases of the eye, the skin, or the lower intestinal tract. Suitable topical formulations are readily prepared for each of these areas or organs. For topical applications, the compositions may be formulated in a suitable ointment containing the active component suspended or dissolved in one or more carriers. Carriers for topical administration of the compounds of this invention include, but are not limited to, mineral oil, liquid petrolatum, white petrolatum, propylene glycol, polyoxyethylene, polyoxypropylene compound, emulsifying wax and water. Alternatively, the compositions can be formulated in a suitable lotion or cream containing the active components suspended or dissolved in one or more pharmaceutically acceptable carriers. Suitable carriers include, but are not limited to, mineral oil, sorbitan monostearate, polysorbate 60, cetyl esters wax, cetearyl alcohol, 2- octyldodecanol, benzyl alcohol and water. Topical application for the lower intestinal tract can be effected in a rectal suppository formulation (see above) or in a suitable enema formulation. Patches may also be used. The compositions of this invention may also be administered by nasal aerosol or inhalation. Such compositions are prepared according to techniques well- known in the art of pharmaceutical formulation and may be prepared as solutions in saline, employing benzyl alcohol or other suitable preservatives, absorption promoters to enhance bioavailability, fluorocarbons, and / or other conventional solubilizing or dispersing agents.In some embodiments, the lanthipeptide or polynucleotide of the present invention can beconjugated to at least one other molecule. Typically, said molecule is selected from the group consisting of polynucleotides, polypeptides, lipids, lectins, carbohydrates, vitamins, cofactors, and drugs.In some embodiments, the lanthipeptide or polynucleotide of the present invention isformulated with lipidoids. The synthesis of lipidoids has been extensively described (see Mahon et al., Bioconjug Chem. 201021:1448-1454; Schroeder et al., J Intern Med. 2010267:9-21; Akinc et al., Nat Biotechnol. 200826:561-569; Love et al., Proc Natl Acad Sci USA. 2010 107:1864-1869; Siegwart et al., Proc Natl Acad Sci US A.2011108:12996-3001). While these lipidoids have been used to effectively deliver double stranded small interfering RNA molecules in rodents and non-human primates (see Akinc et al., Nat Biotechnol.200826:561- 569; Frank-Kamenetsky et al., Proc Natl Acad Sci USA.2008105:11915-11920; Akinc et al., Mol Ther. 2009 17:872-879; Love et al., Proc Natl Acad Sci USA. 2010 107:1864-1869; Leuschner et al., Nat Biotechnol. 201129:1005-1010), the present disclosure describes their formulation and use in delivering polynucleotides.In some embodiments, the lanthipeptide or polynucleotide of the present invention isformulated using one or more lipid-based structures that include but are not limited to liposomes, lipoplexes, or lipid nanoparticles (Paunovska, Kalina, David Loughrey, and James E. Dahlman. "Drug delivery systems for RNA therapeutics." Nature Reviews Genetics (2022): 1-16). Liposomes are artificially prepared vesicles which can primarily be composed of a lipid bilayer and can be used as a delivery vehicle for the administration of pharmaceutical formulations. Liposomes can be of different sizes such as, but not limited to, a multilamellar vesicle (MLV) which can be hundreds of nanometers in diameter and can contain a series of concentric bilayers separated by narrow aqueous compartments, a small unicellular vesicle (SUV) which can be smaller than 50 nm in diameter, and a large unilamellar vesicle (LUV) which can be between 50 and 500 nm in diameter. Liposome design can include, but is not limited to, opsonins or ligands in order to improve the attachment of liposomes to unhealthy tissue or to activate events such as, but not limited to, endocytosis. Liposomes can contain a low or a high pH in order to improve the delivery of the pharmaceutical formulations. As a non-limiting example, liposomes such as synthetic membrane vesicles are prepared by the methods, apparatus and devices described in US Patent Publication No. US20130177638, US20130177637, US20130177636, US20130177635, US20130177634, US20130177633, US20130183375, US20130183373 and US20130183372. In some embodiments, the liposomes are formed from 1,2-dioleyloxy-N,N- dimethylaminopropane (DODMA) liposomes, DiLa2 liposomes from Marina Biotech (Bothell, Wash.), 1,2-dilinoleyloxy-3-dimethylaminopropane (DLin-DMA), 2,2-dilinoleyl-4-(2- dimethylaminoethyl)-[1,3]-dioxolane (DLin-KC2-DMA), and MC3 (as described in US20100324120) and liposomes which can deliver small molecule drugs such as, but not limited to, DOXIL® from Janssen Biotech, Inc. (Horsham, Pa.). The polypeptide of polynucleotide of the present invention can be encapsulated by the liposome and / or it can be contained in an aqueous core which can then be encapsulated by the liposome (see International Pub. Nos. WO2012031046, WO2012031043, WO2012030901 and WO2012006378 and US Patent Publication No. US20130189351, US20130195969 and US20130202684). In some embodiments, the polynucleotide of the present invention is formulated with stabilized plasmid-lipid particles (SPLP) or stabilized nucleic acid lipid particle (SNALP) that have been previously described and shown to be suitable for oligonucleotide delivery in vitro and in vivo (see Wheeler et al. Gene Therapy. 19996:271-281; Zhang et al. Gene Therapy. 19996:1438- 1447; Jeffs et al. Pharm Res.200522:362-372; Morrissey et al., Nat Biotechnol.20052:1002- 1007; Zimmermann et al., Nature.2006441:111-114; Heyes et al. J Contr Rel.2005107:276- 287; Semple et al. Nature Biotech.201028:172-176; Judge et al. J Clin Invest.2009119:661- 673; deFougerolles Hum Gene Ther. 2008 19:125-132; U.S. Patent Publication No US20130122104). The original manufacture method by Wheeler et al. was a detergent dialysis method, which was later improved by Jeffs et al. and is referred to as the spontaneous vesicle formation method. The liposome formulations are composed of 3 to 4 lipid components in addition to the polynucleotide. As an example a liposome can contain, but is not limited to, 55% cholesterol, 20% disteroylphosphatidyl choline (DSPC), 10% PEG-S-DSG, and 15% 1,2- dioleyloxy-N,N-dimethylaminopropane (DODMA), as described by Jeffs et al. As another example, certain liposome formulations contain, but are not limited to, 48% cholesterol, 20% DSPC, 2% PEG-c-DMA, and 30% cationic lipid, where the cationic lipid can be 1,2- distearloxy-N,N-dimethylaminopropane (DSDMA), DODMA, DLin-DMA, or 1,2- dilinolenyloxy-3-dimethylaminopropane (DLenDMA), as described by Heyes et al. In some embodiments, the polynucleotide of the present invention is formulated in a lipid nanoparticle such as those described in International Publication No. WO2012170930. Lipid nanoparticle formulations typically comprise a lipid such as, in particular, an ionizable cationic lipid, and further comprise a neutral lipid, a sterol and a molecule capable of reducing particle aggregation, for example a PEG or PEG-modified lipid. The lipid can be selected from, but is not limited to, DLin-DMA, DLin-K-DMA, 98N12-5, C12-200, DLin-MC3-DMA, DLin-KC2- DMA, DODMA, PLGA, PEG, PEG-DMG, PEGylated lipids and amino alcohol lipids. In some embodiments, the lipid is a cationic lipid such as, but not limited to, DLin-DMA, DLin-D- DMA, DLin-MC3-DMA, DLin-KC2-DMA, DODMA and amino alcohol lipids. The amino alcohol cationic lipid can be the lipids described in and / or made by the methods described in US Patent Publication No. US20130150625. As a non-limiting example, the cationic lipid can be 2-amino-3-[(9Z,12Z)-octadeca-9,12-dien-1-yloxy]-2-{[(9Z,2Z)-octadeca-9,12-dien-1- yloxy]methyl}propan-1-ol (Compound 1 in US20130150625); 2-amino-3-[(9Z)-octadec-9-en- 1-yloxy]-2-{[(9Z)-octadec-9-en-1-yloxy]methyl}propan-1-ol (Compound 2 in US20130150625); 2-amino-3-[(9Z,12Z)-octadeca-9,12-dien-1-yloxy]-2- [(octyloxy)methyl]propan-1-ol (Compound 3 in US20130150625); and 2-(dimethylamino)-3- [(9Z,12Z)-octadeca-9,12-dien-1-yloxy]-2-{[(9Z,12Z)-octadeca-9,12-dien-1- yloxy]methyl}propan-1-ol (Compound 4 in US20130150625); or any pharmaceutically acceptable salt or stereoisomer thereof. Nanoparticle formulations of the present disclosure can be coated with a surfactant or polymer in order to improve the delivery of the particle. In some embodiments, the nanoparticle is coated with a hydrophilic coating such as, but not limited to, PEG coatings and / or coatings that have a neutral surface charge. The hydrophilic coatings can help to deliver nanoparticles with larger payloads such as, but not limited to, polynucleotides within the central nervous system. As a non-limiting example nanoparticles comprising a hydrophilic coating and methods of making such nanoparticles are described in US Patent Publication No. US20130183244. The invention will be further illustrated by the following figures and examples. However, these examples and figures should not be interpreted in any way as limiting the scope of the present invention. FIGURES:Figure 1. a. Description of the discovery pipeline of metabolic pathways that producelanthipeptide compounds dedicated to phage infection. b. Typical genomic architecture of alanthipeptide-producing biosynthetic gene cluster encoded in defense islands. c. Schematic representation of the biosynthesis steps involved in the production of a mature lanthipeptide compoundFigure 2. a. Percentage of lanthipeptide BGCs encoded near defense systems. Comparison thepercentage of class I lanthipeptide BGCs encoded near defense systems depending on theirphylogenetic clade. b. Percentage of class I lanthipeptide BGCs encoded within prophages orplasmids.. Figure 3. Experimental validation of the anti-phage activity of defensive lanthipeptides. a. Schematic representation of the genetic constructions introduced in the genomes of the strainsused in this study. b. Plaque assay results showing the specific anti-phage activity of the type 6lanthipeptide produced by the BGC from S. malaysiensis. c. Liquid assays comparing phageparticle production in the strain producing the type 6 defensive lanthipeptide from S.malaysiensis and its control strain. d. Microscopy images taken 24h after infection with afluorescent version of the phage Pablito. The strains used here express the BGC from S. malaysiensis. Figure 4. Conservons are involved in the regulation of the production of defensivelanthipeptides. a. Plaque assays showing infectivity of phage CM216 in the different wild-type S. coelicolor A3(2) strains. b. Percentage of class I lanthipeptide BGCs encoded near aconservon system.Figure 5. Investigation of the mechanism of action of defensive lanthipeptides. a. Driedbiomass of liquid cultures (in DNB medium) of strains encoding the production of the defensive lanthipeptide from Streptomyces spp. Rtd22, and the control strain. Biomass was recoveredafter 24h of incubation. b. Microscopy pictures of colonies overexpressing the defensivelanthipeptide from Streptomyces spp. CNT318, S. malaysiensis and their respective controlstrain, 24h after incubation in liquid DNB medium. c. Comparison of infectivity of the wildtype phage LD10 compared to an isolated escapee mutant. d. Absorption assays of the phagePablito on the strain producing the defensive lanthipeptide form S. malaysiensis, compared tothe control strain. e. Liquid assay comparing the production of particles of wild-type phageLD10 and its escapee in the strain producing the defensive lanthipeptide from S. malaysiensis,and its control strain, at MOI = 0,1. The escapee of LD10 can replicate in the strain that producesthe lanthipeptide. f. Liquid assay comparing the production of particles of phage LD10 in thestrain producing the defensive lanthipeptide from S.malaysiensis and its control strain, at MOI= 10. g. Rezarurin assay comparing the metabolic activity of the strain producing the defensivelanthipeptide from S.malaysiensis and its control strain, during infection by LD10 at MOI=10.Figure 6. Characterisation of two other lanthipeptide BGCs. a. Bar graph showing the EOPof the phages of the collection against the S.olivaceus lanthipeptide BGC expressing strain andits control. b. Bar graph showing the EOP of the phages of the collection against the Kitasatospora spp. lanthipeptide BGC expressing strain and its control. EXAMPLE: Methods: Genomic detection of lanthipeptide BGCs near known defense sysems. We downloaded 29,414 genomes of Actinobacteria from the RefSeq database (all assembly qualities: complete, chromosome, scaffold and contigs). Genomic detection of lanthipeptide BGCs was done using antiSMASH v6.1.1. The core biosynthetic genes of each BGC were retrieved using the antiSMASH annotation: the Precursor lanthipeptide, the serine / threonine dehydratase, and the lanthionine synthetase genes. Defense systems were detected using DefenseFinder v1.2.1 with models v1.2.3. To determine the proximity of lanthipeptide BGCs of all classes to known defense systems, we assessed the presence of a defense system within 23 proteins upstream or downstream of the BGC’s lanthionine synthetase. To avoid the presence of many closely related genomes we clustered all synthetase at 80% identity and 80% coverage using Mmseqs2. All the defensive % were calculated by using the average of all clusters. Phylogenetic studies For all retrieved lanthionine synthetase proteins were clustered using Mmseqs2 with 80% identity and 80% coverage, and sequences too short or too long were manually discarded. Only the LanC domains (annotated by PFAM PF05147) were aligned using muscle super5 v5.1 and trimmed using clipkit v1.3.0. The phylogenetic tree was built using IQ-TREE v 2.2.3 with models finder and 2000 ultrafast bootstrap. Detection of mobile genetic elements and conservon systems Plasmids and prophages were detected using genomad [REF] v1.7.4. Conservon detection was done using MacSyFinder [REF] v2.1.1 with a coverage threshold of 0.4 and custom Conservonmodels. The HMM protein models of the conservon proteins were built using the BLASTp[REF] results (50% identiy 80% coverage) of Streptomyces coelicolor A3(2) conservon proteins (CnvA, CnvB, CnvC, CnvD, CnvF8) on the RefSeq nr database. Proteins were aligned using mafft v7.505 (auto mode) and HMM profiles were created using hmmbuild [REF] (HMMER v3.3.2) and a GA threshold of 20 was applied to all profiles. The detection definition was to detect at least 2 genes to be detected as a conservation system. Defining lanthipeptide types based on the core peptide sequence. The tool antiSMASH v6.1.1 was used to define the sequences of the core and leader peptides from the sequence of the precursor lanthipeptide of a given BGC. For precursors that were not properly annotated with antiSMASH, to delimit the boundaries between the leader and the core peptide we blasted their amino acid sequence against a public database of predicted core peptide created by Walker et al 2020 (Walker, M.C., Eslami, S.M., Hetrick, K.J. et al. Precursor peptide-targeted mining of more than one hundred thousand genomes expands the lanthipeptide natural product family. BMC Genomics 21, 387 (2020).). We then BLAST all our precursors against each other and calculated a proximity score for each pair (% identity, % of coverage average between the two members of the pair). We used this proximity score to compute a distance matrix that was clustered with Louvains methods using python-louvain v0.16. All the obtained types were then clustered again using the same method to create subtypess. In total weobtained 12 types, and 6 rare with only one identified sequence (see Table 1).Table 1: number of precursors by type Type Number precursorsOther 7Type 1 181Type 2 217Type 3 58Type 4 66Type 5 41Type 6 154Type 7 23Type 8 114Type 9 10Type 10 2Type 11 3Type 12 7Construction of Streptomyces strains for expression of lanthipeptide BGCs The sequence of the defensive lanthipeptide BGCs identified in the genomes NZ_CP015726.1(Streptomyces sp. RTd22), NZ_JAIY01000006.1 (S. sclerotialus), NZ_LJIW01000001.1 (S.malaysiensis), NZ_FOLM01000022.1 (Streptomyces sp. CNT318), NZ_JOFH01000009(S.olivaceus) were retrieved. The sequence of a non-defensive lanthipeptide BGC identified inthe genome NC_016109.1 (Kitasatospora setae). The genes of the BGC were refactored into 2different synthetic operons: -Operon 1: all modifying enzymes (except for the predicted fxlM methyltransferase)were kept in their natural chromosomal organization, a synthetic RBS sequence was placed before the START codon of the first enzyme, and the operon was put under the control of the constitutive ErmE* promoter; -Operon 2: the precursor lanthipeptide gene was placed under the control of theconstitutive KasOp* promoter and a synthetic RBS before its START codon, when applicable the predicted N-acetyltransferase present in the BGC was placed after the lanthipeptide precursor gene on this same operon, with a synthetic RBS sequence. Sequence of synthetic RBS and promoters used in this work: Name SequenceStrong RBS AAGCTTGAACAGGAGGCCCCAT (SEQ ID NO :899)ErmE* TCGATCTTGACGGCTGGCGAGAGGTGCGGGGAGGATCTGACCGACGC promoter GGTCCACACGTGGCACCGCGATGCTGTTGTGGGCACAATCGTGCCGGT TGGTAGGATCCAGCG (SEQ ID NO :900)KasOp* TGTTCACATTCGAACGGTCTCTGCTTTGACAACATGCTGTGCGGTGTTG promoterTAAAGTCGTGGCCA (SEQ ID NO :901)The sequences of the designed operons were synthetized by Genscript and cloned into the pOJ436 cosmid vector. For the construction of strains to test each BGC, 2 vectors were clone: one vector containing the full lanthipeptide BGC (operons 1 and 2), one negative control vector with an incomplete BGC (operon 1 only). These constructs were then introduced in thechromosome of the strain S. albus J1074 by conjugation from Escherichia coli S17. Positive S.albus clones were screen on a growth medium supplemented with Apramycin and the integration of the BGCs was confirmed by colony PCR. Bacteriophage isolation and sequencing The isolation of bacteriophages from soil samples of different locations was carried out following the “enrichment” phage isolation protocol previously described by Dowding (1973). Soil samples of each location, 0.5 gram each, were added to separate 50 ml Falcon tubes containing 10 ml of Difco Nutrient Broth (DNB) (BD Biosciences), supplemented with filter sterilized glucose (0.5%) and Ca(NO3)2.4H2O (4 mM), or 10mL of standard Maltose-YeastExtract-Malt Extract (MYM) medium To each tube, 5 µl of each spore stock of S. coelicolor,S. griseus, S. venezuelae or S. lividans was and culture were incubated overnight with shakingat 30°C. Cultures were then centrifuged at 4000 x g for 10 minutes, and the supernatants were filter sterilized and stored in the dark at 4°C until further use. Isolation of single phages was carried out by plating serial dilutions of filtered supernatants on DNB soft agar plates (0.5% agarose (w / v), glucose 0.5%, Ca(NO3)2.4H2O 4 mM), inoculated with 5 µl spore stock of the bacterial host that was used for propagation. Plates were incubated for 24-48 hours at 30°C until plaques appeared. High titer phage stocks from single plaques were obtained by picking each plaque and introducing them to 10 mL DNB broth (glucose 0,5%, Ca(NO3)2.4H2O 4 mM) inoculated with 10 µl of S. albus spores, and incubated overnight at 30°C with shaking. Lysates were then filtered through a 0.45 µm Millipore filter into sterile 15 ml tubes and individual viruses were stored in the dark at 4°C until further use. DNA isolation of phages from cell lysates was performed using the Phage DNA Isolation Kit (Norgen Biotek Corp.) and quantified with a Qubit dsDNA Assay kit. Whole genome sequencing was performed by the Institute Pasteur Biomics Platform and we performed de novo assembly of the genomes of the phages named CM2016, CE2, CB1, LD10, CF9, G0P4, VD188, VD317, VD96 and VD140. Plaque assays Square plates containing 35 mL of either DNB soft agar medium (0.5% agarose (w / v), glucose 0.5%, Ca(NO3)2.4H2O 4 mM) or MYM soft agar (0.5% agarose (w / v)) were inoculated with approximately 108spores of the strain of interest. Plates were dried and 4 µl droplets of serial dilutions of each phage were placed on the agar surface, with dilutions from 10-1to 10-7. Plates were incubated at 30°C overnight and placed at room temperature for another 24h. Liquid assays Liquid cultures were done in Erlenmeyer flasks with DNB media (glucose 0.5%, Ca(NO3)2.4H2O 4 mM) inoculated with spores at OD450 = 0.15. Cultures were incubated for 5h with shaking at 30°C, then phages were added at a multiplicity of infection (MOI) of 0.1. After infection, we sample 500µl of culture every 10 minutes, immediately filter sterilize all samples, and store them at 4°C until use. Then we assess the number of phage particles in eachsample by titrating them on DNB soft agar medium inoculated with wild-type S. albus spores.Plaque forming units are counted after 24h of incubation at 30°C. Absorption assays Liquid cultures of 20 mL DNB medium (glucose 0.5%, Ca(NO3)2.4H2O 4 mM) were inoculated with 107spores of strain of interest in an Erlenmeyer flask. Cultures were incubated at 30°C for 5h with shaking. Phages were then added at an MOI of 0.1. After infection, 100 µL samples of cultures were taken every 10 min until 1h of incubation, and transferred into anEppendorf tube containing 900 µL DNB medium. Samples were vortexed and centrifuged for7 min at max speed. Supernatants were filtered, sterilized and stored at 4°C. Phage titers were determined as previously described. Isolation of phage escapees Each phage lysate was diluted and spread on the surface of soft DNB agar plates inoculated with spores of the strains S. coelicolor ΔcvnF8, in order to get single lysis plaques. Each lysisplaque was picked and amplified in DNB media inoculated with wild-type S. albus spores, byincubation at 30°C overnight with shaking. Filter sterilized lysates were used to compared the sensitivity of the amplified phages to the wild-type initial phage, by performing plaque assayson plates of wild-type S. coelicolor and S. coelicolor ΔcvnF8. Phages were considered asescapees when their infection was not inhibited by the lanthipeptide, as compared to the wild- type phage. The collected escapees were then amplified and sequenced as previously described Resazurin viability assayCultures of S. malaysiensis lanthiphage expressing and control strains were inoculated in 30mL of DNB medium supplemented with 0.5% glucose and calcium nitrate at a concentration of 5 × 10⁷ spores / mL. The cultures were incubated at 30°C with shaking for 5 hours. At designated time points (120, 90, 60, 45, 30, and 15 minutes before measurement), 500 µL of each culture was transferred to a fresh tube as a non-infected control, while another 500 µL was infected with DJones2 WT at an MOI of 10. Infections were initiated at different times to ensure varying infection durations (e.g., 2 hours, 1.5 hours, 1 hour, etc.), but all infections concluded simultaneously. This synchronization allowed for fluorescence measurements to be taken at the same moment, enabling a direct comparison of metabolic activity across different infection periods. At the end of the infection phase, for each strain, 200 µL of each sample was transferred to a 96-well plate, washed with PBS, and resuspended in 100 µL of PBS containing 0.15 mg / mL resazurin. Fluorescence was recorded over 30 minutes using an excitation wavelength of 550 nm and an emission wavelength of 590 nm. Each condition was tested in triplicate to ensure reproducibility. The metabolic activity ratio between infected and non- infected samples was determined using the slope of the fluorescence curves. In parallel, for each time point, PFU counts were determined to monitor the inhibition of LP10 replication inthe lanthipeptide BGC from the S.malaysiensis strain expressing strain but not in the control.Results: Example 1 Genomic identification of defensive lanthipeptide BGCs Recent studies have shown that we can use genomics to predict to a certain level the function of a gene or a group of genes. On one hand the field of natural products has developed methods to detect genes involved in the production of lanthipeptides and other compounds. Lanthipeptides are produced by metabolic pathways encoded in chromosomally adjacent genes,referred to as biosynthetic gene clusters (BGCs). These gene clusters contain genes responsiblefor encoding precursor peptides, enzymes for post-translational modifications, transporters, andregulatory proteins (Figure 1b,c). Publicly available computational tools such as antiSMASH(

[0011] ) have been developed to efficiently identify BGCs that produce a variety of uncharacterized lanthipeptides in thousands of microbial genomes. On the other hand, the field of bacterial immunity has demonstrated that we can use genomics to predict the anti-phage function of uncharacterized genes. Indeed, bacterial genes involved in anti-phage defense are generally clustered in genomic regions called “defense islands”. Therefore, the co-localization of genetic elements with known defense systems is a strong predictor of antiviral function. This feature has successfully been used to discover dozens of novel anti-phage systems ([3,12,13]). In this work, we used genomics to predict whether BGCs that encode the biosynthesis of lanthipeptides, could have an anti-phage function. To assess the anti-phage function of a given lanthipeptide-producing BGC we determined whether it is often encoded within defense islands. To do this: 1) we detected all lanthipeptide BGCs in a database of 29k genomes ofActinobacteria using antiSMASH; 2) we detected all known anti-phage systems in a 20 kbregion around each BGC with the tool DefenseFinder

[0014] , previously developed by our team.We detected a total of 13.9k lanthipeptide BGCs, with 8.7% being encoded next to at least one known defense system. Lanthipeptide BGCs are classified in different established classes based on the enzymes involved in the post-translational modifications. To further characterize the lanthipeptide BGCs that co-localize with known defense systems, we determined whether certain classes were enriched in defense islands. We show that class I lanthipeptide BGCs are found up to 4 times more in defense islands (17.6 vs 4.5%), compared to other classes of lanthipeptide BGCs (Figure 2a). To delve into this specific class, we computed a phylogenetic tree of the lanthionine synthetase gene, present in all lanthipeptide BGCs. By mapping on this tree the presence of known defense systems next to the corresponding BGC, we can track the emergence of a clade of class I lanthipeptide BGCs potentially dedicated to anti-phage defense. We refer to this clade as “defensive clade” since up to 26.7% of the BGCs are encoded near defense systems, compared to only 4.5% of BGCs outside of this clade (Figure 2a). The genomic context of the BGCs from this defensive clade were further analyzed manually to confirm their presence within defense islands (Data not shown). We also show that BGCs from this defensive clade are often encoded within mobile genetic elements, such as plasmids or prophages, further reinforcing the prediction of their involvement in anti-phage defense (Figure 2b). We refer to the compounds produced by the BGCs of the defensive clade as “defensive lanthipeptides”. Since the amino acid sequence of the core peptide dictates the molecular structure of the lanthipeptides produced by these BGCs, we conducted an analysis of the sequence diversity among core peptides from this defensive clade. Through comparison of sequence similarities, we categorized the various core peptides into 12 distinct types containing more than 2 BGC homologues (Data not shown). Experimental validation of the anti-phage function of defensive lanthipeptides in heterologous hosts. To test the anti-phage activity of the defensive lanthipeptides produced by the BGCs of interest, we use synthetic biology techniques to construct lanthipeptide producing strains that overexpress a complete lanthipeptide BGC. For each lanthipeptide BGC to test, we constructed a corresponding control strain expressing an incomplete version of the BGC (all enzymes, except for the precursor lanthipeptide gene) that does not produce the lanthipeptide of interest (Figure 3a). The genes of each candidate BGC were designed to be expressed under the control of synthetic promotors and ribosome binding sites to ensure strong constitutive expression; the designed DNA sequences were fully synthetized by Genscript and cloned into the cosmid vectorpOJ436, then introduced into the chromosome of the strain S. albus J1074 by conjugation. Weconstructed a total of 4 strains overexpressing different lanthipeptide BGCs, and their respective negative control strains (Figure 3): 2 BGCs producing different Type 2 lanthipeptides, and 2 BGCs producing different Type 6 lanthipeptides. In addition, we set a collection of an array ofdiverse phages that infect Streptomyces species isolated from environmental soil samples, incollaboration with the citizen science project “Science à la Pelle” and collaborators from Leiden University (The Netherlands). We used these phages and our constructed strains to develop protocols to screen the anti-phage function of the cloned lanthipeptide BGCs. We performed protocols of viral plaque assays in solid media to compare the infectivity levels of phages on lanthipeptide-producing strains (expressing the full lanthipeptide BGC) compared to control strains (expressing an incomplete BGC) (Figure 3b). We also compared the phage propagation in both strains in liquid medium to further assess the anti-phage activity of the produced lanthipeptides (Figure 3c) and confirmed by microscopy that the replication of a fluorescent phage was inhibited (Figure 3d).We confirmed that 4 of the 5 tested lanthipeptide-producing BGCs confer a clearly identifiabledefense against one or several phages (Data not shown): 2 Type 6 lanthipeptides, one Type 4lanthipeptide and one Type 2 lanthipeptide. Therefore, we consider that the lanthipeptidecompounds produced by the BGCs from the described defensive clade have an anti-phage function, hence revealing an entire new family of RiPPs that participate in phage defense. Conservon systems regulate the expression of defensive lanthipeptide in native strainsWe identified that the highly characterized strain Streptomyces coelicolor encodes a BGC thatproduces a type 6 defensive lanthipeptide. A previous study demonstrated that a conservon system called cnv8 regulates the expression of this lanthipeptide BGC, and is encoded in the same genomic region (Data not shown). Indeed, they built single knockouts strains for each gene of cnv8 and demonstrated that these deletions activate the expression of the lanthipeptideBGC at different levels

[0015] (Data not shown). We tested these strains against our collection ofphages and compared their susceptibility to phage infection. Our results show that the resistanceof S. coelicolor to phage infection increases with the expression levels of the lanthipeptideBGC, hence demonstrating the anti-phage role of the produced lanthipeptide in a native strain(Figure 4a). We observe anti-phage activity against 10 of the 11 phages tested (only phageG0P4 is resistant). To further investigate the role of these conservon systems in the regulation of the production of defensive lanthipeptides, we detected the presence of such systems in the vicinity of the BGCs of interest. We observe numerous examples of defensive lanthipeptide BCGs encoded next toconservon systems, suggesting their involvement in the regulation (Figure 4b). Moreover, wedemonstrate that this genomic co-localization is more prominent in class I lanthipeptide BGCs from the defensive clade, compared to the rest, suggesting that conservon systems could be involved in the regulation of genes involved in anti-phage defense. Exploring the anti-phage mechanism of action of defensive lanthipeptides To start characterizing the mechanism of action of the lanthipeptides of interest, we first assessed whether their production could be toxic for the host or alter its viability and development. Therefore, we compared the growth of the lanthipeptide-expressing strains and their respective control, both in liquid and solid media, as well as compared the development of hyphae (characteristic of Actinobacteria) with microscopy. Our results show no difference in the growth or development of these strains, hence excluding an effect on phage replication due to differences in the viability of the host (Figure 5a,b). Many known lanthipeptides have been shown to interact with the membrane or cell wall components. Therefore, we hypothesized that our defensive lanthipeptides could prevent phage infection by blocking phage absorption. To test this hypothesis, we conducted phage absorption assays to compare the absorption efficiency in our lanthipeptide producing strains and the negative control strains. Our results show no significant difference between the strains, hence demonstrating that the lanthipeptide produced does not block absorption. However, we see a significant difference in the number of phage particles produced after the first infection cycle, meaning that the anti-phage effect of the defensive lanthipeptide is visible from the early stages of infection (Figure 5d). A method that has been used to understand the mechanism of actions of defense systems, is the isolation of phages that are resistant to a given anti-phage system

[0016] , called phage “escapees”. To obtain phages that escape the anti-phage effect of our defensive lanthipeptides, we haveisolated single plaques of phages that replicate on an agar plate inoculated with the strains S.coelicolor ΔcvnF8, which overexpress a type 6 defensive lanthipeptide. We have isolated a total of 15 escapees of 4 different phages (an example shown in Figure 5c): VD188 (6 escapees),CF9 (2 escapees), LD10 (3 escapees) and CE2 (4e scapees). By sequencing their genome, weobserved that all escapees had mutations in the same gene, encoding for a putative N- acetyltransferase enzyme: 4 escapees gained a STOP mutation, 9 escapees a point mutation of a conserved residue, 2 escapees had additional disruptive sequences inserted in the gene . We show that these escapees are also resistant to other type 6 lanthipeptides produced by heterologous expression (Figure 5e), hence confirming that this N-acetyl transferase is involved in the anti-phage effect of defensive lanthipeptides. We are currently exploring what could be the potential target of this phage enzyme, and whether it interacts directly with the produced lanthipeptide, or with another protein / metabolite involved in the lanthipeptide mechanism of action. To confirm that the defensive lanthipeptide has a specific activity against phage and does not impact bacteria, an assay measuring the metabolic activity during the infection by the phage LD10 of the heterologous expression strain producing the malay lanthiphage or a control was carried out. During this assay, metabolic activity and efficiency of plating (EOP) were measured at different timepoints during an infection at high MOI (10). A higher reduction of metabolic activity was observed in the control strain than in the defensive lanthipeptide producing strain. As reduction of metabolic activity is used here as proxy for cell death, this assay indicates thatcells producing the defensive lanthipeptide from the S. malaysiensis strain are dying less thatthe control strain during phage infection. Efficiency of plating during this assay confirmed thatthere was almost no replication of the phage in the defensive lanthipeptides producing strains,while the phage replicates normally in the control. Taken together, these results indicate that the effect of the defensive lanthipeptide is specific to the phage and does not lead to death of the bacteria producing them (Figure 5f,g). Example 2 ABGC producing another defensive lanthipeptide from Streptomyces olivaceus (olvA)previously characterised was predicted as belonging to the defensive clade, cloned in an heterologous expression strain, and tested against the collection of phages. OlvA was confirmed to have an antiphage activity against all the phages of the collection (Figure 6a). As a control of the bioinformatics prediction, a BGC encoding for a lanthipeptide class I predicted to be non-defensive was chosen and cloned in an heterologous expression host(S.albus). This BGC was identified in Kitasatospora setae (NC_016109.1), and was tested inplaque assays against the collection of phages. No reduction of efficiency of plating was observed, the lanthipeptide is confirmed to not have an antiphage activity (Figure 6b). REFERENCES: Throughout this application, various references describe the state of the art to which this invention pertains. The disclosures of these references are hereby incorporated by reference into the present disclosure. 1. Atanasov AG, Zotchev SB, Dirsch VM, Orhan IE, Banach M, Rollinger JM, et al. Natural products in drug discovery: advances and opportunities. Nat Rev Drug Discov. 2021;20(3):200–16. 2. Newman DJ, Cragg GM. Natural Products as Sources of New Drugs over the Nearly Four Decades from 01 / 1981 to 09 / 2019. J Nat Prod.2020;83(3):770–803. 3. Georjon H, Bernheim A. The highly diverse antiphage defence systems of bacteria. Nat Rev Microbiol.2023;21(10):686–700. 4. Bernheim A, Millman A, Ofir G, Meitav G, Avraham C, Shomar H, et al. Prokaryotic viperins produce diverse antiviral molecules. Nature [Internet]. 2021;589(7840):120–4. Available from: http: / / dx.doi.org / 10.1038 / s41586-020-2762-2 5. van Bergeijk DA, Terlouw BR, Medema MH, van Wezel GP. Ecology and genomics of Actinobacteria: new concepts for natural product discovery. Vol. 18, Nature Reviews Microbiology. Nature Research; 2020. p.546–58. 6. Zdouc MM, van der Hooft JJJ, Medema MH. Metabolome-guided genome mining of RiPP natural products. Trends Pharmacol Sci.2023 Aug;44(8):532–41. 7. Medema MH, de Rond T, Moore BS. Mining genomes to illuminate the specialized chemistry of life. Vol.22, Nature Reviews Genetics. Nature Research; 2021. p.553–71. 8. Pfeiffer IP-M, Schröder M-P, Mordhorst S. Opportunities and challenges of RiPP-based therapeutics. Nat Prod Rep [Internet]. 2024; Available from: http: / / xlink.rsc.org / ?DOI=D3NP00057E 9. van Staden ADP, van Zyl WF, Trindade M, Dicks LMT, Smith C. Therapeutic Application of Lantibiotics and Other Lanthipeptides: Old and New Findings. Appl Environ Microbiol.2021;87(14). 10. Ramírez-Rendón D, Guzmán-Chávez F, García-Ausencio C, Rodríguez-Sanoja R, Sánchez S. The untapped potential of actinobacterial lanthipeptides as therapeutic agents. Mol Biol Rep.2023;50(12):10605–16. 11. Blin K, Shaw S, Augustijn HE, Reitz ZL, Biermann F, Alanjary M, et al. antiSMASH7.0: new and improved predictions for detection, regulation, chemical structures andvisualisation. Nucleic Acids Res [Internet]. 2023 Jul 5;51(W1):W46–50. Available from: https: / / doi.org / 10.1093 / nar / gkad344 12. Gao L, Altae-Tran H, Böhning F, Makarova KS, Segel M, Schmid-Burgk JL, et al. Diverse enzymatic activities mediate antiviral immunity in prokaryotes. Science [Internet]. 2020;369(6507):1077–84. Available from: http: / / www.ncbi.nlm.nih.gov / pubmed / 32855333 13. Doron S, Melamed S, Ofir G, Leavitt A, Lopatina A, Keren M, et al. Systematicdiscovery of antiphage defense systems in the microbial pangenome. Science (80- ).2018;359(6379):0–12. 14. Tesson F, Hervé A, Mordret E, Touchon M, d’Humières C, Cury J, et al. Systematic and quantitative view of the antiviral arsenal of prokaryotes. Nat Commun [Internet]. 2022;13(1):2561. Available from: https: / / doi.org / 10.1038 / s41467-022-30269-9 15. Bonet B, Ra Y, Cantu Morin LM, Soto Bustos J, Livny J, Traxler MF, et al. The cvn8 Conservon System Is a Global Regulator of Specialized Metabolism in Streptomyces coelicolor during Interspecies Interactions [Internet].2021. Available from: https: / / doi.org / 10 16. Stokar-Avihail A, Fedorenko T, Hör J, Garb J, Leavitt A, Millman A, et al. Discovery of phage determinants that confer sensitivity to bacterial immune systems. Cell. 2023 Apr;186(9):1863-1876.e16.

Claims

CLAIMS:

1. A lanthipeptide that comprises the core peptide of consensus formulaTXDXCXXXCXXXC (I) wherein X represents any amino acid residue.

2. The lanthipeptide of claim 1 that comprises the core peptide of formula of type 2TXDXCXXTCXXXC.

3. The lanthipeptide of claim 2 that is selected from the group consisting of:AALLRSTDDGCGATCAGTACVSFGGNV AALLRSTDDGCGSTCSGTACASFGGNV ALLQNTEDNCGQTCESACPATGC DLYQLTNDNCGTTCETACTSCPK DTGEWDLDVSFIEAGDSVKHLIYMTNDNCGQTCASACVSCP EATSDNCTSTRASACVTCT EDNCGRTCESACPATGC ELLRLTDDGCGATCESACNSCP ELMNQTSDNCGSSNESACVGCFTE ELMRPTDDGCGHTCESACNSCPE EMMRLTDDGCGSTCESACNSCA GGTVEHIIKMTEDNCGSTCESACTSC GTVIGELLNSTSDGCGSTGASACAGCVTD HIIKMTGDNCGTTCQSACTTC HLIRLTNDGCNSTCATACTSCP IGIEDLDITFIEAGGTVDHIIKMTNDGCGSTCQSACTSC IIKMTDDGCGSTCQSACNSC IIRLTGDNCGSTCQSACVSCP IKMTEDGCGSTCASACTSC IKMTEDNCGGTCASACTSC IKMTEDNCGSTCASACTSC IKMTEDNCGSTCESACTSC IKMTEDSCGSTCESACTSC IKMTQDNCGTTCESACTSC IPELLRSTSDNCGKTCASACTSCKQD IPELLRSTSDNCGKTCSSACTSCKQN IQMTEDGCGSTCASACTSC IRMTEDNCGNTCESACTSC KILYDSSGGCGATCQSSCASCSKILYDTSDGCGSTCASACTSCS KILYDTSDGCGSTCQSACTSCR KMTGDNCGTTCESACTSC LDALLNLTGDNCGGTCASACTSCP LDALLNLTGDNCGTTCESACTSC LDDLLNLTGDGCGTTCQSACTSCP LGSVLYDTSDNCGHTCESACSSCP LLIQLTGDGCGSTCQSACVSCP LLRITSDNCGKTCQSACTSCRS LLRSTSDNCGGTCASACTSCKS LLRSTSDNCGKTCASACTSCKQD LLRSTSDNCGKTCASACTSCQS LMNKTSDNCGSTSESACAGCITD LMNSTSDNCGSTNESACAGCITD LMNTTSDNCGSTNESACAGCITD LMRATDDGCGSTCASACTSCK LMRSTSDNCGKTCASACTSCKS LRLTDDGCGATCESACNSCP LTDDGCGSTCASACTSCS LYDTGDNCGQTCQSACNSCP LYDTSDGCGTTCASACTSCR LYDTSDNCGHTCQSACVSCM MNSTSDNCGSTDESACAGCVID MRLTDDNCGSTCESACNSCP QLIQLTGDGCGSTCATACVSCP QLIRLTDDGCNSTCATACVSCP QLIRLTGDGCNSTCATACTSCP QLIRLTGDGCNSTCATACVSCP QLIRLTNDGCGSTCASACTSCP QLIRLTNDGCGSTCQSACTSCP QLIRLTNDGCGTTCQSACTSCP QLIRLTNDGCNSTCASACVSCP QLIRLTNDGCNSTCATACTSCP QLIRLTNDGCNSTCATACVSCP QLIRLTNDGCNSTCGTACVSCP QLIRLTSDGCGSTCATACTSCP QLIRLTSDGCNSTCATACTSCP QLIRLTSDGCNSTCATACVSCP QLIRLTSGGCNSTCATACVSCPQLIRMTDDGCNSTCATACISCGT QLIRMTDDGCNSTCATACNSCP QLIRMTDDGCNSTCATACTSCP QLIRMTDDGCNSTCATACTSCPA QLIRMTDDGCNSTCATACTSCPS QLIRMTDDGCNSTCGTACVSCGS QLIRMTDDGCNSTCGTACVSCGT QLIRMTNDGCNSTCATACTSCPA QLIRMTNDGCNSTCATACVSCP RILYDTSDGCGQTCESACNSCG SPTEDNCGQTCESACPQTGC VAADQLIQLTGDGCGSTCASACVSCP VAELMNSTSDGCTSTGASACVTCVIS VDDILRMTDDNCGQTCESACTSCP VDHIIKMTNDGCGSTCQSACTSC VEELMRPTDDGCGHTCESACNSCPE VPELMRSTDDNCGSTCASACTTCSKK AALLRSTDDGCGSTCEGSACASGGGNV ADHLIRLTDDGCGQTCESACNSSCP CESACSPSCTDNGN DLMRLTDDGCGTTCESACPAQSGC DWELDITFIESGESVDKLIYMTNDGCGKTCQSACSTTCPA DWELDITFVESGESVDKLIYMTNDGCGKTCQSACSTTCPA ELLSLTDDNCGTTCESACTTTCP ELMRPTDDGCGQTCESACMQTCP ELMRPTDDGCGSTCESACTPTCP GRHCHSNDGCGHTCDSACAASCTDGDD GVDKLIYMTNDGCGKTCQSACTSCPK HLINMTDDGCGHTCEKSTCISAA HLINMTDDGCGHTCEKSTCISSA HLINMTDDGCGNTCAGSTCISAA HLINMTDDGCGQTCEKSTCISAA HLINMTDDGCGQTCEKSTCISAT HLINMTDDGCGSTCEKSTCITSA HLINMTDDGCGTTCEKSTCISAA HLINMTDDGCGTTCEKSTCITAA INPTDDGCGTSCPDSCTPS ISVTDDGCGTTCPKACTTGSR IYMTNDGCGKTCQSACSTTCPIYMTNDGCGSTCQSACSTTCP KLIQMTDDGCGKTCQSACSTTCP KLIRMTDDGCGATCQSACSTTCP KLIRMTDDGCGTSCQSACPATCP KLIRMTDDGCGTTCQSACSPTCP KLIRMTDDGCGTTCQSACSTTCP LDELMRLTDDNCGTTCQSACSTTCA LINLTDDGCGSTCASPCATAMG LINLTDDGCGSTCPKACATNCG LINLTDDGCGTSCPTTCVTSTSA LINLTDDGCGTSCPTTCVTSTSD LVEELIRMTDDGCGTTCQSACPNTCPGD LWGMTDDGCGQTCQSACAPSCTARKGT MTNDGCGKTCQSACSTTCPK QVWNSGTNCHTDDGCGQTCESACSNSCTDGG RDGEQAGADDWELDIKFIEAGDAVKHLIYMTNDQCGTTCQSAC TNTCPS RERACQTDDGCGHTCEKSACTTTA RLIHMTNDGCGQTCQSACSTTCP RLIQMTDDGCGQTCESACQQTCP RLIQMTDDGCGQTCESACQSTCP RLIQMTDDGCGQTCESACSATCP RLIQMTDDGCGQTCESACSSSCP RLIQMTDDGCGQTCESACSTTCP RLIQMTDDGCGQTCQSACSTTCP RLIQMTDDGCGSTCESACNATCP RLIQMTDDGCGSTCQSACSTTCP RLIRMTDDGCGETCESACSTTCP RLIRMTDDGCGKTCESACTTTCP RLIRMTDDGCGKTCQSACPNTC RLIRMTDDGCGKTCQSACSSTCP RLIRMTDDGCGQTCESACSATCP RLIRMTDDGCGQTCQSACSTTCP RLIRMTDDGCGTTCETACSTTCP RLIRMTDDGCGTTCQSACSTTCP RLIRMTDDGCGVTCESACSTTCP RLIRMTDDGCGVTCQSACSTTCP SINLTDDGCGTTCEGACCTSGSD SLVNMTNDGCGTTCEKDTCISGA SLVTMTDDGCGSTCQGSTCISSVTDDGCDHTCEKSACTTTA TDDGCGHTCEKSACTTTD TNDGCGKTCQSACSPSCTNNG TNDGCGQTCESACTPSCTQNG TNDGCGQTCETACTQSCTDNG TNDGCGQTCQSACAPSCTDNG TNDGCGQTCQTACTNSCTRRTVG TWNSGRTCNSNDGCGHTCQSACANSCTDGE VLVNMTDDGCGTTCAKTTCISAA WSMTNDGCGKTCETACTPSCTDNG WSMTNDGCGSTCQSACTQSCTNSGGGG ALLNDTGDGCGSTCQSACANSTCIGG ALLNDTGDGCGSTCQSACSNSTCIGG ALLNDTGDGCGSTCQSACSNSTCISGG DLMRNTDDNCGQTCQSACSNSTCG DLMRSTDDNCGATCQSACSNSTC DTGDGCGATCQSACSNSTCIG ELMSSTDDGCGETCASACSNSTCIA IADLMRNTDDNCGQTCQSACSNSTC IAELMSSTDDGCGQTCASACSNSTCVA LDALLNLTGDNCGTTCESACSTTCA LDELMRLTDDGCGHTCQSACPNSGC LDSLLNLTGDNCGSTCESACSTSCS LGSLLNDTSDNCTSTCASACSNSTCIGG LGWLLNDTSDNCTSTCNSACSNSTCIGG LKDTDDGCGSTCQSACSNSTCIAG LLNDTDDNCTSTCQSACSNSTCIGG LLNDTGDGCGATCQSACSNSTCIGG LLNDTGDGCGSTCQSACANSTCVSG LLNDTGDGCGSTCQSACSNSTCISG LLNDTGDGCTATCQSACSNSTCG LLNDTGDGCTSTCQSACSNSTCIGG LLNKTSDQCGSTNQSACVTCIGD LLNSTSDNCTSTCQSACSNSTCVA LLNSTSDNCTSTCQSACSNSTCVAN LMRNTDDNCGQTCQSACSNSTC LMRSTDDNCGATCQSACSNSTC LNDASDNCGSTCQSACSNSTCIGG LNDTGDGCGQTCESACSNSTCELNDTGDGCGQTCESACSNSTCG LNDTGDGCGQTCQSACSNSTCE LNDTGDGCGQTCQSACSNSTCIG LNDTGDGCTSTCKSACSNSTCIA LNDTGDGCTSTCQSACSNSTCG LNDTGDNCTSTCQSACSNSTCIGS LNDTSDGCTSTCQSACSNSTCIGG LNDTSDGCTSTCQSACSNSTCVGG LNDTSDNCGSTCQSACSNSTCIGG LNDTSDNCGSTCQSACSNSTCIGS LNDTSDNCTATCSSACSNSTCIGG LNDTSDNCTSTCASACSNSTCIGG LNDTSDNCTSTCQSACTNSTCIGG LRSNTDDGCGQTCESACSNSTC LVNDTSDNCTSTCESACSNSTCE SDFDLRIETVASAPVLGSLLNDTSDNCGSTCQSACSNSTCIGG TTGDGCGQTCQSACVNTGV VAELMRNTDDGCTSTCESACTNSTCIV VAGLLNDTGDGCGSTCQSACSNSTCISG VAGLLNDTSDGCTATCQSACSNSTCISG VASLLNDTGDGCTSTCQSACSNSTCIGG VGMLLNDTGDGCGQTCESACSNSTCE VNDDGLVPCDTSDGCGSTCASACTNSGL ALLNDTGDGCGSSCQSACSNSTCIGG LDSLLNLTGDNCGSTCESACSTTCP LMGNTDDNCGVSCQSACSNSNCE LNDTGDGCTATCESACSNSTCE LNDTSDGCTSTCQSACSNSTCIGS LNDTSDNCTSTCESACSNSTCIGG SDFDLRIETVASLPVLGSLLNDTSDNCGSTCQSACSNSTCIGG VAGLLNDTGDGCGATCQSACSNSTCIGS VAGLLNDTGDGCTSTCQSACSNSTCIGG4. The lanthipeptide of claim 1 that comprises the core peptide of formula of type 6TDDXCXXXCX(X)XCXT.

5. The lanthipeptide of claim 4 that is selected from the group consisting of:ALINLTDDGCKPSCQGSCATNVAASDDGCGSSCPDACVSTAN ATLINLTDDGCGSTCSSPCATN AVLINLTDDGCGSTCSSPCATNVA FAKLINLTDDGCGSTCSSPCASSVA GLISLTDDGCGETCGACTTNVA GLVSLTDDGCGETCGACTTNVA IAGLVSLTDDGCGETCGACTTNVA IGVTDDNCGSTCASPCATNVA ILLTDDGCKPSCPESCASAVA ILTDDGCGSTCSSPCATAVA INLTDDGCGSSCPNACATNIG INLTDDGCGSSCPSACATNVG INLTDDGCGSTCSSPCATAVA INLTDDGCGSTCSSPCATH INLTDDGCGSTCSSPCATNVA INLTDDGCGTTCPSTCVTSVSD INLTDDGCKPSCQGSCATNVA INLTDDNCGSSCPKACATNVG INLTDDNCGSTCSSPCATNVA ISLTDDGCGETCGACTTNVA ITLTDDGCKPSCPASCATNVA IVLTDDGCGSSCPSACATNVA LINLTDDGCGSSCPNACATNVG LINLTDDGCGSSCPNACTTSAAD LINLTDDGCGSSCPNSCTTSAAD LINLTDDGCGSTCSSPCASSVA LINLTDDGCGSTCSSPCATNVA LINLTDDGCKPSCNGSCATNVA LINLTDDGCKPSCQGSCATNVA LINLTDDGCKPTCAGSCATNVA LINLTDDNCGSSCPKACATNVG LINLTDNGCGSTCASPCATNVG LTDDGCGSTCGACTTNVA LTDDGCKPSCKGSCATNVA LTDDGCKPSCNGSCATNVA LTDDGCKPSCQGSCATNVA NLTDDGCGASCPTTCVTSTSA NLTDDGCGSTCPKACATNIG NLTDDGCGSTCSSPCATNVANLTDDGCGSTCTACTTNVA NLTDDGCKPSCKGSCATNVA NLTDDGCKPSCNGSCATNVA NLTDDGCKPSCQGSCATNVA NLTDDGCKPTCKGSCATNVA QEDEFDLDISILESGDGSAVLVNLTDDGCSPTCEGSCATNVA RLIVLTDDGCGSSCPSACATKVA SDSPFALDIRLIEGGDTTPLINMTDDGCGASCPNTCATSTSD SLINLTDDNCGSSCPNACATNMG SLTNLTDDGCGSTCGACTTNVA TITDDNCGSTCASPCATNVA VLINLTDDGCKPTCKGSCATNVA VNLTDDGCGSTCSSPCATAVA VNLTDDGCNPTCPESCTSAAN APVAATDEFDLDVTIVERTDAASLEVLTDDGCGATCGACTTG ATTDDGCGSTCGACTTNAA DEYELNIDLVDAGPVSGHASNTBDSCGTTG DGFDLDVRLVEVGDSAGLVNLTDDGCGETCGACTTNVA DGFDLDVSLIEIADPAGLVNLTDDNCGSTCGACTTNVA DGFDLDVSLVEIADPAGLVNLTDDNCGSTCGACTTNVA DGFDLDVSLVEIADPAGLVSLTDDNCGSTCGACTTNVA DGFDLDVSLVEIVDPAGLVNLTDDNCGSTCGACTTNVA DGFELDVALLEVADTAGLINLTDDGCGETCGACTTNVA DGFELDVTLLEVSDAASLTNLTDDGCGETCGACTTNVA GFDLDVSLLEISDTAGLVNITDDNCGSTCGACTTGVA GFELDASLLEVADSASLVNITNDNCGSTCGACTTGVA GFELDVTLVEVADPAGLVNLTDDGCGETCGACTTNVA GLINLTDDGCGSTCGACTTNVA GLINLTDDNCGSTCGACTTNVA GLINVTDDNCTSTCGACVTDGGS GLISLTDDGCGSTCGACTTNVA GLISLTNDGCGETCGACTTNVA GLISLTNDGCGTTCGACTTNVA GLITMTDDNCGSSCEKTTCITSS GLVNITNDGCGSTCGACTTGVH GLVNLTDDGCGSTCGACTTNVA GLVNLTDDGCGSTCGACVSSVA GLVNLTDDGCGSTCGACVTNVA GLVNLTDDNCGSTCGACTTNVAGLVNLTDDNCGSTCGACTTNVARRLN GLVNLTDDNCGSTCGACVTNVA GLVNLTDDNCGTTCGACTTNVA GLVNMTDDGCGSTCEKDACISAA GLVNMTDDNCGSTCEKSTCVTGA GLVNVTDDGCGSTCGACNSTVA GLVNVTDDGCGSTCGACVTGAA GLVNVTDDGCTSTCGACISNAY GLVNVTDDGCTSTCGACVSGAV GLVNVTDDGCTSTCGACVSNAD GLVNVTDDNCTSTCGACITNSA GLVNVTDDNCTSTCGACVTGAV GLVSITNDGCGSTCGACTTNVA HLVSMTDDNCGSTCEKSTCISAV HPQPKPSDGFELDVALLEVSDTAGLINLTDDGCGETCGACTTNVA ILTDDGCGSTCGACTTGVH ITDDNCGSSCGACTTGVA ITGDNCGSTCGACTTGVH KATAAVGDEFDLDVRTVETADAASLQVLTDDGCGATCGACTTGVH KATVAVGDEFDLDVRTVETADAASLQVLTDDGCGATCGACTTGVH KTLTDDGCGSTCGACTTGVH KTLTDDNCGSTCGACTTGVH LINMTDDGCTSTCGACVTNAP LLRNTDDNCGSTCVGTACPTNVANPS LSLLEVADVAGLVNLTDDGCGSTCTACTTNVA LTDDGCGSTCGACTTGAA LTDDNCGSTCGACTTNVA MDASLLEVADSASLVNITNDGCGSTCGACTTGVA NATDDGCGSTCGACTTNVA NLTDDGCGSTCGACTTGVH NLTDDGCGSTCGACVSSVA NLTNDGCGSTCGACTTNVA PDGFELDVRLVEVADTAGLVSITNDGCGSTCGACTTNVA PQTPGASDGFDLDVSLVEIDDTAGLVNLTDDNCGTTCGACTTNVA PVTASDGFDLDVRLVEVGDSAGLVNLTDDGCGETCGACTTNVA QEPAAGGQPDGFDLNVSLLEVSDAAGLTVLNDDNCGSSCGACVTF QEPAAGGQPDGFDLNVSLLEVSDAAGLTVLTDDNCGSSCGACVTF QEPAAGGQSDGFDLNVSLLEVSDAAGLTVLTDDGCGSSCGACVTF QEPAASGQSDGFDLNVSLLEVSDAAGLTVLTDDNCGSSCGACVTFQEPLAQEDGFTLNVGLLEVSDAIGLTNLTDDNCGTTCGACTTNVA QEPTADGQSDGFDLNVSLLEVSDAAGLTVLTDDGCGSSCGACVTF QEPTAGGQSDGFDLNVSLLEVSDAAGLTVLTDDGCGSSCGACVTF QEPTAGGQSDGFDLNVSLLEVSDAAGLTVLTDDNCGSSCGACVTF QEPTASGQSDGFDLNVSLLEVSDVAGLTVLTDDNCGSSCGACVTF QEPTATSQSDGFDLNVSLLEVSDAAGLTSLTDDNCGSTCGACTTNVA QEPTSQSDGFDLNVSLLEVSDAAGLTSLTDDNCGSTCGACTTNVA QEPVAQEDGFTLNVGLLEVSDAAGLTNLTDDNCGTTCGACTTNVA QEPVAQEDGFTLNVSLLEVSDAAGLTNLTDDNCGTTCGACTTNVA QEPVAQEDGFTLNVSLLEVSDAAGLTNLTDDNCGTTCGACVTNVA QESGTASDGFVLDIALLEVGDVASLTNLTDDGCGETCGACTTNVA QESTAGGQSDGFDLNVSLLEVSDAAGLTVLTDDGCGSSCGACVTF QESTAGGQSDGFDLNVSLLEVSDTAGLTVLTDDGCGSSCGACVTF QESVAQEDGFTLNIGLLEVSDAAGLTNLTDDNCGTTCGACTTNVA QESVAQEDGFTLNVGLLEVSDAAGLTNLTDDNCGTTCGACTTNVA QGSVAQEDGFTLNIGLLEVSDAAGLTNLTDDNCGTTCGACTTNVA QPSAATPDGFDLDVTLVEVADVAGLINLTDDGCGETCGACTTNVA QQTPGTSDGFDLDVSLVELADPAGLVNLTDDNCGTTCGACTTNVA QQTPGTSDGFDLNVSLVEVADPAGLVNLTDDNCGTTCGACTTNVA QSDGFDLNVSLLEVSDAAGLTVLTDDGCGSSCGACVTF QSDGFELNVSLLEVSDAAALTVLTDDNCGSSCGACVTF SLTDDGCGETCGACTTNVA SMVNLTDDNCGSTCGACTTNVA SPATASSDGFDLDVSLVEVADSASLTNLTNDNCGTTCGACTTNVA SPSSPSGDGFDLDVALLEVGDVAGLTNLTDDNCGTTCGACTTNVA SSTTPDGFELDVALLEVSDTASLTNLTDDGCGETCGACTTNVA STGPEQAFDLDIRALDIADAGPFMARNTDDNCGSTCPNACATNM SVTDDNCGSTCGACTTNVA TLTDDGCGSTCGACTTGLH TSLTDDNCGSTCGACTTNVA TSVAQDPFDLDISVVESGAPSRWVINSDGGCGLSRGNACASSGS VLTDDGCGSTCGACTTGFH VLTDDGCGSTCGACTTGLH VLTDDGCGSTCGACTTGVH VQLTDDGCGSTCTACTTG VRLTDDGCGSTCTACTTG6. The lanthipeptide of claim 1 that comprises the core peptide of formula of type 8TXDXCXXXCXSXC.

7. The lanthipeptide of claim 6 that is selected from the group consisting of:AELVPVPVPVEEWELETTVTRTPTPIVEACGTGDGCAKTCASSCASS AESVPVPVPAEEWELDTTVTRAPTPIVEACGTGDGCAKTCASSCASS APITGDDWQLTIAITDAPVPVAEDCDTSDGCESTCASSCTS APITGDDWQLTITITDSPVPVAEDCDTSDGCESTCASSCTS APITGDEWQLTIAITDAPVPVAEDCDTSDGCESTCASSCTS APMTGDNWQLTIAITDSPVPVAEACDTSDGCESTCASSCTS ATVIAALPLTEDEWALDITVTDAPRVVANEECDTNDGCKSTCDSACAS AVAEPVPADEWELKTTITRAPTPIVAACGTSDGCGSTCASACASS AVAEPVPVEEWELDTTVTRAPTPIVEACGTGDGCAKTCASSCASS DDWELDITITDAPRPAVANCDTNDTCESTCDSSCASD DDWKLDVIITDSPTVVPADCGTGDGCAGTCASACAS DEWQLDIAITDSPTVVPTDCGTGDGCGSTCASACAS DWELTTTVTTSPVPIVEACGSGDGCKSTCASSCISS EEWELDTSVTRAPAPIVEACGTGDGCAKSCASSCVSS EEWELDTTVTRTPTPIVEACGTGDGCAKTCASSCASS ESVPVPVPAEEWELDTTVTRAPTPIVEACGTGDGCAKTCASSCASS IATYQPPQPPAVLTEPVPADEWELKTTITRTPVPIVEACGTGDGCAKTCASSCASS IGEDGFALTVRVVTDDQSPSAETACDTSNGCASTCDSSCASA LTEPVPAEEWELKTTVTRTPTPIVEACGTGDGCASTCASSCASS MAQATATLASKTVEVPLSEDEWDLSTIITTSPMPITEMCDTNDGCAKTCASSCTSS MARVTAPLASKALDAPLSDDEWELETTITHSPTPIVEACDTSDGCKKTCASSCASS MASVAAPLATETVEVPLSDEWELTTTITRAPTPIVEACGTNDGCAASCASSCASS MATATAPLTTTTVEAPLSDEWELDTTITRSPAPIVEACDTNDGCASSCASSCTSS MDTATAPLTTSTVEVPLSDEWELDTTITRTPTPIVEACGTDDGCASSCASSCASS MNTLSQPQQTTELDEGFPVDWELTTTVTTSPVPIVEACTSGDGCKSTCASSCISS MPVPVPAEEWELDTTVTRAPVPIVEACGTGDGCAKTCASSCASS MSVPIAEAAAPAIKPTTVTLPFSDEDWELEVSITDAPLPAAPDACDTSDGCESSCASSCTSD MSVPTAEAAAPAIKPTTVTLPFSDEDWELEVSITDAPHPVAPDACDTSDGCESSCASSCTSD MSVQIAEKEKAAPPIAPTIATSPSSDEEWELEVSISDAPHPVATDDCDTSDGCESSCASSCTSD PQPTEAVAEAVPVEEWELDTTVTRTPTPIVEACGTGDGCAKTCASSCASS PQPTTAVAEPLPAEEWELDTTVTRAPVPIVEACGTGDGCAKTCASSCASS PRPAAAVAEPLPAEEWELDTTVTRAPVPIVEACGTGDGCAKTCASSCASS PTAAVAESVPVPIEEWELDTSVTRAPAPIVEACGTGDGCAKSCASSCVSS PTTAVVAEPLPVSGDEWELDTTVTRAPTPIVEACGTGDGCAKTCASSCASS SDDEGFLVDWELTTTVTTSPVPIVEACGSGDGCKSTCASSCISS TAFSGEDAPPIGPPAATLPFSGEDWELEVSVTDAPRPVASDDCDTSDGCESSCDSSCTSD VAELVPVPVPVEEWELETTVTRTPTPIVEACGTGDGCAKTCASSCASSVEAPQGLAAEEIPDEFELDMRVIEASVPLPVLACNTDDNCNPSCNSSCATAV VSVPVPAEEWELDTTVTRAPVPIVEACGTGDGCAKTCASSCASS DADLLPKACDTGDGCKPSCASSCASAV DADLLPKACGTGDGCKPSCASSCASAV DADLLPKACGTGDGCKPSCASSCTSAV DADLLPKACGTGDGCNPSCASSCTSAV DLLPKACGTGDGCAASCASSCASAV DLLPKACGTGDGCAPFCASSCASAV DLLPKACGTGDGCAPSCASSCASAV DLLPQACGTGDGCAASCASSCASAV DSDLLPKACGTGDGCKPSCASSCASAV IPASLKDVDLLDLDVTVTAEAGAEARPVACGSSDGCGASCASACISA ACGTGDGCASTCASSCASAV ACGTGDGCGATCSSSCTSAV ACGTGDGCKSTCASSCASAV DSDLLPRACDTGDGCKPSCASSCASAV GTGDGCGATCASACANSGV GTNDGCAATCPSSCVSRV PDACGTGDGCESTCASACASAV ACDSGDGCGTTCESACTSD ACDTSDTCGSTCASACASD ACDTSDTCGSTCGSACISD ACDTSDTCGSTCGSACISS CDTSDGCGSTCASACNSAV CVASDGCDTSDGCSSTCPSACASS DCGSGDGCGSTCASACAS DCGTGDGCGSTCASACAS DDAFVLDIHVISDVRPDLMPTACDTNDGCKKTCASACTST DRMAAGCGSSDGCGSTCASACTSAV GCDTSDGCSSTCPSACASS GQQTCDTSNGCPSTCESSCNSAM PIVSSCDTGDGCASTCASSCAS PVASDDCDTSDGCESSCASSCTSD QDLMPTACDTNDGCKGTCASACTST RCDSSDTCGSTCGSACASS RCDTSDGCAATCASSCASS RGCDTNDGCGSTCASACASR SCDTSDGCSSTCPSACASS SDGCDTSDGCSSTCPSACASSVMARDDCDTNDGCQSTCDSACLS YNSCDTSNGCSSTCPSACTSGS AACRTDDGCAATCASSCVSNV ACATDDGCASTCASSCVSNV ACGDGTNDGCDPSCASACLTGGV AQKACDTSNGCPPSCASSCNSAA CDTNDGCDPTCASSCVSS CGTNDGCAGTCASSCVTHSPN CKGNTDDGCDPTCASACVSHGA CKGNTDDGCDPTCASACVTGGV CTEGTNDGCDPTCASACVTGGV CTNGTDDGCDPTCASACVTGGV CTTNDGCAPTCASSCASAV DPLFACGEGTNDGCQPTCASACVTGGV DTPCTTDDGCDPTCDSSCNSSV EDAAAPCGTDDGCAPTCASSCNSGV ELLPTACDTNDGCKPSCASSCTST GHPLAACKGGTDDGCDPTCASACISDGV GRCATDDGCDPTCASSCISNA GTDDGCDPTCASACISDAV GTDDGCDPTCASACVSDGV GTSDGCAPTCASSCASAV GVGRCATDDGCDPTCASSCISNA HPLSACGNGTDDGCDPTCASACISDGV IPVACGTSDGCDPSCASSCTSAV ISDGCATDDGCDPTCASSCVSNA ISEGCGTDDGCDPTCASSCISNA LDMTDTEDIFTLDVRIVTDANVGDTGRGCDTSDGCAATCASSCVSNS MNPCTNGTDDGCDPTCASACVTGGV QGACTNGTDDGCDPTCASACVTGGV QVPCDTSNGCPATCDSSCNSAV TTNDNCPPSCASSCLSSV VAAPCGTDDGCDPTCASSCASNA VACGTSDGCAATCASSCVSRGAS VASACDTSDGCDPTCASSCISAV VASACDTSDGCDPTCASSCISTV VSRGCATDDGCDPTCASSCVSNA SACGTGDGCSSTCASSCASAV8. The lanthipeptide of claim 1 that comprises the core peptide of formula of type 10TDDNCGTTCXSTCTT.

9. The lanthipeptide of claim 8 that is selected from the group consisting of:AVIAMTDDNCGTTCPSTCTTSAGA10. The lanthipeptide of claim 1 that comprises the core peptide of formula of type 11TDDGCGTTCSTSCXTSSXXXS.

11. The lanthipeptide of claim 10 that is selected from the group consisting of:MCATDDGCGTTCSTSACSTSSNDPS MCATDDGCGTTCSTSACTTSSNDPS12. The lanthipeptide of claim 1 that comprises the core peptide of formula of type 12CXTXDGCAXXCXSSCXS.

13. The lanthipeptide of claim 12 that is selected from the group consisting of:ACATDDGCASTCASSCASS MPAACGTGDGCAASCASSCASAV TCGTGDGCAASCASSCASAV ACTTNDGCAPSCASSCTSSSC ANAACATEDGCAASCASSCASDV AGCNTDDGCAASCASSCASNV14. A lanthipeptide that comprises the core peptide of consensus formulaTXDXCGXXCXXXC (II) wherein X represents any amino acid residue.

15. The lanthipeptide that is selected from the group consisting of:AALLRSTDDGCGSTCSGTACTSFGGNV AALQQSTSDNCGSTCTGTACISYTGDPV ACATDDGCGHTCELSACHSQR ACQTDDGCGHTCELSACHSQR ACSTSDGCGSSCGTSACATSSYDPA AKLSCDTDDGCGQTCSTSACNSQANNPSAKLSCDTSDGCGQTCSTSACNSQANNPA AKLSCDTSDGCGQTCSTSACNSQANNPS AMACQTDDGCGSTCEISACHSQK AVGEDGFRLEFAVIESAVPLAKLGCNTSDGCGHTCQGSACNSQ ANNPS CDTSDNCGATCGTSACNSGSLDPS CNTDDGCGDTCNTSACNTSSYDPA DLLRDTSDNCGSSCSGTACTSFVGDPA DLLRDTSDNCGSTCSGTACASFTGDPA DLMRDTSDNCGSTCSGTACTSYVGDPA DMRVVESTTPLVEMMCSTDDGCGVSCGTSACSTGSNDPS DSLPLAKMSCNTDDNCGGSTCGS DTSDGCGNTCSTSACSTNSADPF EEEFVLDMRVVESTTPLVAMMCSTSDGCGSTCSTSACSTSSND PF ETMAPLMVDCDTSDGCGSTCETSACTSGTASPA EVFMCNTNDGCGSTCSGSACSTSSYDPR EVFMCNTNDGCGSTCSTSACSTSSYDPR FMCNTNDGCGSTCSTSACSTSSYDPR GGLLLSTSDNCGSTCDGTACTSAMAYPA GKLMCDTGDGCGSTCQGSACNSYIDDPF IAIMMCDTSDGCGNSCSTSACNTSSNDPS IAIMMCDTSDGCGNSCSTSACSTSSNDPV IAIMMCDTSDGCGQSCSTSACSTSSNDPS ITMCSTDDNCGSTCKPSACASNSADPF IVIMMCDTSDGCGQSCSTSACSTSSNDPS LLRDTNDNCGSTCSGSACASGGGNVG LLRSTSDNCGSTCDGTACVSFASDPA LLRSTSDNCGSTCDGTACVSFVSDPA LQRSTSDNCGSTCSGTACNTSMSDVS LRCDTDDGCGNTCQGSACASFTNNPV LRCDTSDGCGNTCQTSACSSFTNNPV LRCDTSDGCGSTCATSACNSATNNPF LRCTTGDGCGETCSGSACTTSAYDPRD LVIMMCDTSDGCGATCSTSACSTGSNDPF LVIMMCDTSDGCGDTCNTSACSTGSNDPF LVIMMCDTSDGCGNTCGTSACSTGSNDPF LVIMMCDTSDGCGNTCSTSACSTGSNDPF LVIMMCDTSDGCGSSCSTSACSTASNDPS LVIMMCDTSDGCGSTCSTSACSSGSNDPF LVIMMCDTSDGCGSTCSTSACSTGSNDPFLVIMMCDTSDGCGSTCSTSACTTFSNDPL LVIMSCDTSDGCGDTCNTSACASGSNDPF LVITMCDTSDGCGSTCSTSACTTFSNDPY MACSTSDNCGGSTCGSACTSHVTQPL MADCDTSDGCGSTCATTACISNANDPF MCDTSDGCGNTCSTSACTTFSNDPY MCDTSDGCGSTCSTSACTTFSNDPY MCSTSDGCGNSCSTSACTTKASEPL MCSTSDGCGNTCSTSACSSSSYDPF MCSTSDGCGSSCSTSACTTKASEPL MEDCDTSDGCGNTCSTSACTTSSNDPS MGNCSTSDGCGSTCQTSACNSGVANPV MLCSTGDGCGSSCSTSACTTNVADPS MSCDTEDNCGNTTCGSACTSQVAQAPF MSCDTSDGCGGTTCGSACTSQVAQTPY MSCDTSDNCGGTTCGSACTSHVATPL MSCDTSDNCGGTTCGSACTSQVAQNPF PLAKLGCNTSDGCGHTCQGSACNSQANNPS QTDDGCGQTCQISACHSQR SCDTSDGCGSTCSTSACSTGSNNPF SFLRSTDDGCGSTCSNGSTACASSVNDPS SLLRDTDDGCGSTCSNGATACTSLSGDAA SLLRSTDDGCGSTCSNGSTACASSVNDHS SLLRSTDDGCGSTCSNGSTACASSVNDPS TDDNCGSTCGGTACASGP TMCSTGDGCGATCRPSACNSVSSDPF TMGCQTDDGCGTTCQISACHSQK TRSTDDNCGSTCSGSACASGGGNV TSDGCGSSCSGSACTSFTDDPV VAMMCDSSDGCGSTCSTSACSTNSNDPA VIESSTPLVIMMCSTSDGCGSTCSTSACSTSSYDPA VIESSYPIAALACDTNDGCGSTCASACNSSAADPA VIMACSTSDGCGSTCNTSACATSSYDPA VIMMCDTSDGCGQSCSTTACTTSSLDPS VIMMCSTSDGCGNTCDTSACSTSAYDPR VIMMCSTSDGCGSSCSTSACATKSSDPV VIMMCSTSDGCGSSCSTSACTTKSCDPV VITMCATDDNCGSTCQPSACSSISDDPS VVEATTSLVVMMCDTGDGCGSTCSTSACSTSSNDPSVVEVTTPLVIMMCSTSDGCGNTCGTSACSTSSYDPR VVLMCDTDDGCGSTCSNSACATGSNDPS VVMACSTSDGCGETCSTSACSTSSYDPA VVMACSTSDGCGQTCSTSACSTSSYDPA VVMACSTSDGCGSTCSTSACNTSSYDPA VVMMCSTSDGCGATCNTSACNTSSYDPN VVMMCSTSDGCGSSCSTSACATKSSDPT VVMMCSTSDGCGSSCSTSACTTKSCDPV AAHPFGKLQCATGDGCGSTCSGGASACSSFVEDPA AAHPIGKLMCSTGDGCGSTCSGSSSACSSFIEDPA AEHPYGKLMCSTGDGCGPTCQGGASACNSFVEDS ATHPIGRLMCTTSDGCGNTCTNGASSCNSLLRDPE ATYSNGNNQCSTNDGCGQTCENGASACNSSIDDPDHNH CPTDDGCGATCENGASACDSFVEEPA CPTDDGCGNTCAGADSSCNSAADNPF CPTNDGCGETCKDGASACQSVANNVF DCPTDDGCGNTCAGSDSSCNSFADDPS DCPTDDGCGNTCSGNDSSCNSFADDPS DSPLTVFMCPTSDGCGDTCLRTPSE FSCATSDGCGNTCANGASACNSFTDDPA GDCPTDDGCGNTCSGNASSCNSTFDDPS GGPDNCPTDDGCGNTCQNGASACDSFIDDPV GKLACTTNDGCGNTCQNGASACNSFVGDPF GKLLCATNDGCGNTCANGASACTSFTEDPA GKLMCATNDGCGQTCANGASACSSFIEDPA GKLMCNTGDGCGNTCAGSASACNSYVGDPV GKLMCNTGDGCGNTCAGTASACNSYVGDPF GKLMCNTGDGCGNTCQGSASACNSYVSDPV GKLMCNTGDGCGNTCQGTASACNSYVSDPV GKLMCSTGDGCGNTCANGASACGSFIEDPA GKLMCSTGDGCGPTCQGGASACNSFVEDSA GKLMCSTGDGCGSTCATNASACSSFIEDPA GKLMCSTGDGCGSTCATNSSACNSFVEDPA GKLMCSTGDGCGSTCSGGSSACSSFIEDPA GKLMCSTGDGCGSTCSGGSSACSSFVEDPA GKLMCSTGDGCGSTCSNGASACNSFVEDPA GKLMCSTGDGCGTTCATGASACGSFTEDPA GKLMCSTGDGCGTTCATNSSACNSFVEDPA GKLMCSTSDGCGGTCQGGSSACSSYIEDPAGKLMCTTGDGCGTTCATGSSACNSFVEDPA GKLMCTTSDGCGTTCANGSSACSSFVEDPA GKLQCSTGDGCGSTCSGGASACSSFVEDPA GKLTCTTGDGCGNTCAGTASACNSYVGDPV GLMDCPTDDGCGNTCSGNDSSCNSFTDDPS GNCPTDDGCGDTCSGNASACNSTFDDPS GNCPTDDGCGNTCAGNDSTCNSTFDDPS GNCPTDDGCGNTCSGNASTCNSAFDDPS GNLGDCPTDDGCGNTCENGASACDSFIDDPV GNTNDCPTDDGCGDTCQDGASACDSFIDDPA GQADCPTDDGCGNTCAGSASSCNSSMNALA GRTPCPTDDGCGNTCSGSSSACNSAMNALS GSNCPTDDGCGITCANGASACTSEGNNQF HGYGHLMCSTGDGCGTTCQTGASACGSFTEDPA LACSTGDGCGSTCANGASSCNSSAEYPA LACTTSDGCGNTCQNGASACNSFVGDPF LMCDTGDGCGSTCSNGASACDSAAGDPA LMCSTGDGCGSTCATGASACASFTEDPA LMCSTGDGCGSTCATGASACGSFTEDPA LMCSTGDGCGSTCATGSSACNSFVEDPA LMCSTGDGCGTTCATGASACGSFTEDPA LMCSTGDGCGTTCATGASACNSSTEEPS LMCSTGDGCGTTCATNSSACNSFVEDPA LMCSTSDGCGNTCGGNASSCSSLVRDPE MCPTSDGCGNTCVNGASACQSSIEDAA MCSTGDGCGTTCATGASACGSFTEDPA MGDCPTDDGCGNTCAGNDSACNSFADDPS MGDCPTDDGCGNTCAGSDSSCNSFADDPS MGDCPTDDGCGNTCEGDASSCGSFADDPS MGDCPTDDGCGNTCEGEASACNSFADDPS MGDCPTDDGCGNTCVGNDSACNSFADDPS NCPTSDGCGDTCANGASSCVSSIEDAA NCPTSDGCGDTCANGASSCVSSIEDAG NCPTSDGCGDTCANGASSGWPAIAAAAAQSAPRRGDSHAWLSP RRCL SNDCPTDDGCGNTCSNGASACTSQNNNQF SNNCPTDDGCGDTCKNDASACTSESNHGF SSNCPTDDGCGNSCANGASACISHNNNQF SVKVVLAAHPLGRLMCSTNDGCGQTCSGGASSCSSLVRDPE TGDCPTDDGCGDSCKDGASACDSFIGDPSTGDGCGNTCQQGASACNSFVGDPA TGDGCGQTCATGASACGSFTEDPA TGDGCGSTCSNGASACDSAAGDPA TGDGCGTTCATGASACGSFTEDPA TGDGCGTTCATGSSACNSFVEDPA TSDGCGNTCANGASSCNSYIEDPS TSDGCGNTCQNGASACNSYVADPF TSDGCGSTCNDGASACNSSIEPPLS TVFMCPTSDGCGNTCENGASACQSSIEDAA TVFMCPTSDGCGNTCVNGASACQSSIEDAA YADCPTDDGCGNTCANGASACDSYIGDPA YNFDCPTSDGCGNTCANGASSCVSTIEDAA YNFNCPTSDGCGNTCANGASSCASTIEDAA MCSTSDGCGSTCSTSACSTSSNDPF MCSTSDGCGSTCSTSACSTSSNDPA GTPGRACDTSDNCPPTC16. A lanthipeptide that comprises the core peptide of consensus formulaTXDXCGXXCXXXXC (III) wherein X represents any amino acid residue.

17. The lanthipeptide of claim 16 that is selected from the group consisting of:AAAACATDDGCGSTCPSACSGSSV ADTILMCSTNDTCGSSCPSACTTS DLDIRLIETSDEAESLINLTEDNCGSSCPNACTGSY INLTDDGCGSSCPSACATSASD INLTDDGCGSSCPSACTTSTAD INLTDDGCGSSCPSACTTSTSD LINLTDDGCGSSCPSACTTSASD LMCSTGDGCGSSCPSACTTS LMCSTGDTCGSSCPSACTTS MLVASTDDNCGSSCPNACTTSSS SDDGCGSSCPSACTSTAN TTDTESPFADLDITFLETGPSAALLVASTDDNCGSSCPNACTTSSS ATETVLMCSTGDTCGSSCPSACTTS FIEGTPASETVLMCTTGDTCGSSCPSACTTS LMCGTGDTCGSSCPSACTTS NTSLRCGTGDTCGSSCPSACTTS SETVLMCSTGDTCGSSCPSACTTSTSLRCGTGDTCGSSCPSACTTS TVAEADPFGLDISFIEGTPATETVLMCTTGDTCGSSCPSACVT S TVLMCSTGDTCGSSCPSACSGSTV TVLMCSTGDTCGSSCPSACTTS TVLMCSTGDTCGSSCPSACVTS TVLMCTTGDTCGSSCPSACTTS TVLTCTTGDTCGSSCPSACVTS TWLRCGTGDTCGSSCPSACTTS VSDDGLVPCGTGDGCGSTCASACANSGV YIVRSCDTSDTCGSTCYSACASS AADTVLMCSTGDNCGSSCPSACTTS ANETVLMCGTGDNCGSSCPSACTTS ASESVLMCTTGDNCGSSCPSACGGSSVE ASETVLMCSTSDNCGSSCGSACTTS ATETALMCGTGDNCGSSCPSACTTS ATETVLMCGTGDNCGSSCPSACTTS DLMRNTDDNCGSSCQSACSNSTC DLMRNTDDNCGTSCQSACSNSTCG DQSDPFGLDITFIENTPASESVLMCSTGDNCGSSCPSACTTS ESETVLMCGTGDNCGSSCPSACATS ITMCATDDNCGSTCKPSACSTSSDNPS LLCGTGDNCGSSCPSACTTS LLCSTGDNCGSSCPSACTTS LMCSTGDNCGSSCPSACTTS LMCSTGDNCGTSCPSACPTS LMCSTGDNCGTSCPSACTTS LMCSTSDNCGSSCPSACTTS LMCTTGDNCGTSCPSACTTS LMGNTDDNCGSSCQSACSNSDCE LMTNTDDNCGSTCQSACSNSSC SALMCSTGDNCGTSCPSACANSGS TELLCSTGDNCGSSCPSACTTS TILMCGTGDNCGSSCPSACSGSTV TMLMCSTGDNCGSSCPSACTTS TVLLCSTGDNCGSSCPSACTTS TVLMCGTGDNCGSSCPSACTTS TVLMCSTGDNCGASCPSACATS TVLMCSTGDNCGSSCPSACTTS TVLTCSTGDNCGSSCPSACSGSTVVAALMRDTSDNCGSTCPSACASGGGKVG VITMCATDDNCGTTCKPSACSTSSDNPS18. A lanthipeptide that comprises the core peptide of consensus formulaTXDXCGXXCXXXXXXC (IV) wherein X represents any amino acid residue.

19. The lanthipeptide of claim 18 that is selected from the group consisting of:ASPSAPTGDCTDDNCGSGNTASDACVTNG ASPTAPTGDCTDDNCGSGNTGSEACVTNG ATGSDDCTSDKCGSGETGSDACTTNG ATSTDDDCGSGDTGSSACTTTSN ATSTDDDCGSGNTGSDACTTNADE ATSTDDDCGSGNTGSDACTTNADVGGVR ATSTDDDCGSGNTGSDACTTNADVGVR ATSTDDECGSGNTESQACTTTSD ATSTDDNCGSGNTDSDACTTNADAGVR ATSTDDNCGSGNTGSNACTTNADIGGVR ATSTDDNCGSGNTRSDACTTKADGS AVASEDCTSDECGSGETSSDACTTNS FSTNTDDNCGSGNTGSNACTTKNN LTTDDECGSGETGTNACTTNADAS MSSEDCTSDNCGSGNTGSNACTTRA VIGADTSDNCGSGNTGSNACTTNC ASGYSTNTSDGCGSGNTGSNACTTRCDGGN ATGTDDNCGSGNTGSNACTTRCDASD ATGYATGTDDNCGSGNTGSNACTTRCDAGN ATNTDDDCGSGDTGTSACTTSADG GYATATDDGCGSGNTGSNACTTKCDGGN GYATATDDGCGSGNTGSNACTTRCDDGN GYATATDDGCGSGNTGSNACTTRCDGGN SGGYATSTNDGCGSGNTGSNACTTKCDGGN SGHATNTDDECGSGNTGTSACTT STGYATNTDDNCGSGNTGSNACTTRCDGSF YATATDDGCGSGNTGSNACTTKCDGGN YATSTNDGCGSGNTGSNACTTKSDGDN YSTNTSDGCGSGNTGSNAGTTRCDGGN AGGYATNTDDNCGSGNTGSNACSGGGK AGGYATSTDDNCGSGNTGSNACSGGGKAGGYATSTDDNCGSGNTGSNACSGGSK ASGYATNTDDGCGSGNTGSNACTGK ASGYATSTDDGCGSGNTGSNACSGGSK ASGYATSTDDGCGSGNTGSNACTGK ASGYATSTDDNCGSGNTGSNACSGGSK ATNTDDGCGSGNTGSNACTGGRD ATNTDDNCGSGNTGSNACSGGR ATSTDDECGSGDTNSDACSGGSGR ATSTDDECGSGDTNSDACSSGSGR ATSTDDGCGSGNTGSNACTGGGN ATSTDDNCGSGDTASDACSGGSGR ATSTDDNCGSGDTESDACSSGSGN ATSTDDNCGSGDTGSDACSGDGSS ATSTDDNCGSGNTGSDACSG ATSTSDECGSGNTGSDACSGGSGN ATTTSDECGSGNTDSDACSGGSGN FATDTDDNCGSGNTGSDACSGG FATSTDDGCGSGNTGSDACTGDGS SGYATSTDDGCGSGNTGSTACSGK SGYATSTDDNCGSGNTGSDACSGG TGGYATNTDDNCGSGNTGSNACSGGGK TGGYATNTDDNCGSGNTGSNACSGK TGYATGTDDGCGSGNTGSSACSGK TGYATGTDDGCGSGNTGSSACTGG VSSTDDGCGSGNTGSNACSGK YATATDDGCGSGNTGSNACSGGGK YATATDDGCGSGNTGSNACSGGSK YATATDDGCGSGNTGSSACSGGGK YATATDDGCGSGNTGSSACSGGGR YATDTSDNCGSGNTGSDACAGG YATITDDNCGSGDTDSDACSGA YATSTDDNCGSGNTGSDACSG YATSTDDNCGSGNTGSDACSGGGR YATSTDDNCGSGNTGSNACSGGGK VSSTDDGCGSGNTGSNACTGK20. A lanthipeptide that comprises the core peptide of consensus formulaTXDXCGXGXTXXXXC (V) wherein X represents any amino acid residue.

21. The lanthipeptide of claim 20 that is selected from the group consisting of:ATEVHPGDTDNGCDTVAGGDC DTDDGCDTVKGSDC DTDDGCDTVRGGDC EFDLDIRIVERGPVAAALLGDTDDGCDTVRGSNC FELDVEIVREGPVAAALLADTDDGCDTVKGSDC FELDVEIVTEGPVTAALLADTDDGCDTVKGSDC FELDVQVVTEGPVVAALLADTDDGCDTVKGSDC GGPADVLPTITDNGCDTVKGSDC LADTDDGCDTVKGSDC LADTDDGCDTVRGSDC LANTDDGCDTVQGSDC LANTDDGCDTVRGSDC LCTTDNGCNTVGGSDC LGDTDDGCDTVRGGDC LGDTDDGCDTVRGSDC LSSTDDGCDTVRGSDC LTDTDDGCDTVKGSDC LCTTDNGCSTNKQKDC LCTTDNGCSTNKSTDC AAAALNCSTDNGCDTVAGGDC ALLSSTDDGCDTKTDGDC ALLSSTDDGCDTVKGSDC ARRCSTDNGCDTQANGDC ATASRKCSTDNGCDTLAGSDC ATEARRCSTDNGCDTVAGGDC ATLSRRCSTDNGCDTLANGDC LCSTDNGCDTRKNGDC LSSTDDGCDTDKNGDC LSSTDDGCDTKQGSDC LSSTDDGCDTVRGGDC MSSTDDGCDTVKTGDC EDFDLDITTVASAPRSPDLLNSTDDGCGETPDPAGVNG EFDLDMKIVESGPVAAALLGNTDDGCDTRRDGDC LGDTDDGCDTLKNGDC LGNTDDGCDTLKNGDC NTDDGCDTDRNGDC PGRLALLADTDDNCDTKKPGDCPGRLALLADTDDNCDTQKPGDC PVAAALLADTDDGCDTQKNGDC TDGDDGFDLDVRLVEFGPTSALLLANTDDGCDTQKQGDC VLLASTDDGCDTQKQGDC22. A lanthipeptide that comprises the core peptide of consensus formulaSXXGCGSTCXXXXC (VI) wherein X represents any amino acid residue.

23. The lanthipeptide of claim 22 that is selected from the group consisting of:ASDGGCGSTCGTSCVSNAA DGGCGSTCGSSCVSST DGGCGSTCGTSCVSNAA IASDGGCGSTCGNACISSGS IDGSSDGGCMATCGNSCVSAA SDGGCGSTCGNACISSGS SDGGCGSTCGTSCVSNGA SDGGCGSTCTGSCVSSSS VGVASDGGCGSTCGTSCVSSGT YDGGCMATCGNACVSNAA DTSEGGCGATCGGHSCTSGVV IASDGGCGSTCGGNACISSGS IASDGGSGSTCGGNACISSGS ISSDGGCGSTCGGNACISSGS LASDGGCGSTCGGNACISSGS TVGASIASDGGFGSTCGDNACISSGS AASDGGCQATCGSGACTSSGA AASDGGCQATCGSGVCISSGA ESGGAVSLSAASDGGCAASCGGNACISSGA GITAASDGGCQATCGSGACTSSGA IASDGGCGATCGGNACISSGS SDGGCAATCGGNACVSSGS SDGGCAATCGSSACISSGS24. A lanthipeptide that comprises the core peptide of consensus formulaCXXDXCXXTXXXXG (VII) wherein X represents any amino acid residue.

25. The lanthipeptide of claim 24 that is selected from the group consisting of:ADTEDCTSDTCGSTPGSAGIANCASMVPSADCTSDNCGETPGSAGIA ASVIPSADCTSDGCGQTPGSAGITN ASVVSSEDCTGDGCGPTPCGPGADL VSGVATEECTSDNCGDTPGSAGIA DCTSDNCSATAESAGVTCEQQ GFDSADCTSDNCSATEDSAGVTCDQVQLGCAG GFDSEECTSDNCTGTDDSAGVTC GFDSEPCSGDNCTGTGDSAGVTC GSSSEECTSDGCTGSTEKSGC26. A lanthipeptide that is selected from the group consisting of :MCSTSDGCGSTCSTSACSTSACSTSSNDPL QWSGTACVLCRTWLGHHPAERSRVLATVNSHPLRACTPNCEAR S ARRRRNSSGSCFPTVRPEAVRRRRISATSSSVSC DTDDNCGGPQDSAGTTCPSAG ITSDGGCGSTCGGTACISSGS TCTVMGNCTTSCGSWTQTPLAC PSADCTSDGCTTTKTVYPC27. A polynucleotide that encodes for one or more lanthipeptide(s) according to any one ofclaims 1 to 26.

28. A vector that comprises the polynucleotide of claim 27.

29. A host cell that has been transfected, infected or transformed by the polynucleotide ofclaim 27 and / or the vector of claim 28.

30. The host cell of claim 29 the host cell is selected from the phylum of actinobacteria.

31. Use of the lanthipeptide according to any one of claims 1 to 26 for controlling phagepropagation.

32. A method of treating a viral infection in a subject in need thereof comprisingadministering to the subject a therapeutically effective amount of:- one or more lanthipeptide(s) according to any of claims 1 to 26, or.- one or more polynucleotide(s) according to claim 27.

33. A composition comprises an amount of- one or more lanthipeptide(s) according to any of claims 1 to 26, or.- one or more polynucleotide(s) according to claim 27.

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