Lysins for treatment of bacterial infection

Abstract

The disclosure relates to compositions and methods of endolysins for the prophylaxis and treatment of bacterial infections. More specifically, the disclosure relates to agents, compositions, and methods for preventing and / or inhibiting growth of bacteria.

Description

[0001]Attorney Docket No.061817-503001WO LYSINS FOR TREATMENT OF BACTERIAL INFECTIONCROSS REFERENCE TO RELATED APPLICATIONSThis application claims the benefit of the filing dates of U.S. Provisional Application No.63 / 571,370, filed March 28, 2024, the entire contents of which is incorporated by reference herein. SEQUENCE LISTINGThe instant application contains a Sequence Listing which has been filed electronically in XML format and is hereby incorporated by reference in its entirety. Said XML copy, created on March 26, 2025, is named 061817-503001WO.xml and is 423,304 bytes in size. BACKGROUND Bacterial infections are a leading cause of death, with about 12.7 million attributed global deaths / year. There is a significant and growing global threat of antimicrobial resistance (AMR) to traditional small-molecule antibiotics used to treat bacterial infections. The discovery of small-molecule antibiotics has greatly slowed, and bacteria can quickly evolve resistance to antibiotic compounds. Antibiotic resistance is also spread quickly and pervasively via horizontal gene transfer between bacteria, including via plasmids. Phage therapy has been suggested as an alternative to antibiotics, given the almost limitless diversity of phages, and their position as natural enemies of bacteria. Phage can be also more specific in which microbes they target. However, phage therapy has a number of disadvantages: Many phages have a narrow host-range, i.e., they infect only specific subspecies / strains of bacteria. To target a specific bacterial species with a phage specific for the bacterial species, the specific bacterial strain needs to be identified, or a cocktail of phages to cover any subspecies / strain that could be present is needed. Such a phage “bank” would require potentially thousands of individual, active phages for a given species. Additionally, many bacteria or bacterial strains have natural (intrinsic) resistance to specific phages. Bacteria have “immune systems” that allow them to resist phage infection, e.g., by CRISPR / Cas9 systems or restriction modification. Bacteria can quickly evolve de novo resistance through mutations in any pathway that is co-opted by the phage life cycle, including attachment, penetration, protein synthesis, nucleic acid synthesis, virion assembly, and lysis. Phages are difficult to discover in their natural environments, typically requiring culturing to identify a phage-host pair. This difficulty is exacerbated in bacterial targets that are difficult / impossible to culture. Biologically active Attorney Docket No.061817-503001WO phages are difficult to replicate / assemble since their reproductive cycle relies on killing their bacterial hosts. Phages are difficult to purify since phages are assemblies of many different proteins and nucleic acids in specific structures, of a size often in the order of megadaltons. Phage derived endolysins have recently emerged as promising antimicrobials. Some endolysins have shown lytic activity against bacterial cells. SUMMARY The present disclosure provides for compositions and methods of bacterial lysins. In one aspect, a method for inhibiting the growth of a microbial species is provided, the method comprising contacting the microbial species with an endolysin specific for the microbial species selected from the endolysins and microbial species in Table 1A or Table 1B. In one aspect, a method killing a microbial species is provided, the method comprising contacting the microbial species with an endolysin specific for the microbial species selected from the endolysins and microbial species in Table 1A or Table 1B. In one aspect, a method for reducing the growth of a population of microbial species population is provided, the method comprising contacting the microbial species with an endolysin specific for the microbial species selected from the endolysins and microbial species in Table 1A or Table 1B. In some embodiments, the microbial species is a Gram-negative bacteria or a Gram-positive bacteria. In one aspect, a method of inhibiting the growth, or reducing the population, or killing of at least one species of Gram-negative bacteria is provided, the method comprising contacting the bacteria with a composition containing an effective amount of a endolysin comprising an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity to a endolysin sequence selected from the group consisting of an amino acid sequence of Table 1A or Table 1B, or active fragments thereof. In one aspect, a method of inhibiting the growth, or reducing the population, or killing of at least one species of Gram-positive bacteria is provided, the method comprising contacting the bacteria with a composition containing an effective amount of an endolysin comprising an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity to an endolysin sequence selected from Table 1A or Table 1B, or active fragments thereof. Attorney Docket No.061817-503001WO In a further aspect, a method of inhibiting the growth, or reducing the population, or killing of at least one species of Gram-positive bacteria, the method comprising contacting the bacteria with a composition containing an effective amount of a chimeric endolysin comprising an N-terminal enzymatic activity domain of a first endolysin sequence selected from Table 1A or Table 1B, and a C-terminal cell wall binding domain of a second endolysin sequence selected from Table 1A or Table 1B, wherein the first and the second endolysins are different endolysin seqeuences is provided. In a yet further aspect, a method of treating a bacterial infection caused by a Gram- negative bacteria, comprising administering to a subject diagnosed with, at risk for, or exhibiting symptoms of a bacterial infection, a composition containing an effective amount of an endolysin comprising a chimeric endolysin further comprising an N-terminal enzymatic activity domain of a first endolysin sequence selected from Table 1A or Table 1B, and a C-terminal cell wall binding domain of a second endolysin sequence selected from Table 1A or Table 1B, wherein the first and the second endolysins are different endolysin seqeuences is provided. In one aspect, a method of treating a bacterial infection caused by a Gram-negative bacteria is provided, comprising administering to a subject diagnosed with, at risk for, or exhibiting symptoms of a bacterial infection, a composition containing an effective amount of a endolysin or a chimeric lysin comprising an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity to a endolysin sequence selected from Table 1A or Table 1B, or an active fragment thereof. In one aspect, a method of treating a bacterial infection caused by a Gram-positive bacteria is provided, comprising administering to a subject diagnosed with, at risk for, or exhibiting symptoms of a bacterial infection, a composition containing an effective amount of an endolysin or a chimeric lysin comprising an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity to a endolysin sequence selected from Table 1A or Table 1B, or an active fragment thereof. In some embodiments, the Gram-negative bacteria or the Gram-positive bacteria is present in a biofilm. In some embodiments, the biofilm is present on a subject or a device. In one aspect, an isolated and / or recombinant endolysin selected from Table 1A or Table 1B, or a functional variant thereof, optionally having an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity thereto is provided. Attorney Docket No.061817-503001WO In a further aspect, an isolated and / or recombinant chimeric endolysin comprising an N-terminal enzymatic activity domain of a first endolysin sequence selected from Table 1A or Table 1B, and a C-terminal cell wall binding domain of a second endolysin sequence selected from Table 1A or Table 1B, wherein the first and the second endolysins are different endolysin seqeuences is provided. In some embodiments, the endolysin is a chimeric endolysin. In some embodiments, the endolysin is virion associated. In some embodiments, the endolysin is cysteine modified. In some embodiments, the endolysin is protease resistant. In some embodiments, the endolysin is modified to reduce immunogenicity. In one aspect, a fusion protein comprising an endolysin of the disclosure is provided. In some embodiments, the endolysin is fused with a bacteriocin. In one aspect, a nucleic acid encoding an endolysin or a chimeric lysin selected from Table 1A or Table 1B, or a functional variant thereof is provided, optionally having an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity thereto; or encoding the endolysin or the chimeric lysin of the disclosure or the fusion protein of the disclosure. In some embodiments, the nucleic acid is DNA or RNA. In some embodiments, the RNA is a mRNA. In one aspect, a vector comprising a nucleic acid encoding an endolysin or a chimeric lysin selected from Table 1A or Table 1B or a functional variant thereof is provided, optionally having an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity thereto; or a nucleic encoding the endolysin of the disclosure or the fusion protein of the disclosure. In one aspect, a cell comprising a nucleic acid encoding an endolysin selected from Table 1A or Table 1B, or a chimeric endolysin comprising an N-terminal enzymatic activity domain of a first endolysin sequence selected from Table 1A or Table 1B, and a C-terminal cell wall binding domain of a second endolysin sequence selected from Table 1A or Table 1B, wherein the first and the second endolysin sequences are different endolysin sequences or a functional variant thereof; or encoding the endolysin of the disclosure or the fusion protein of the disclosure. In one aspect, a pharmaceutical composition comprising an effective amount of the endolysin or the chimeric lysin of the disclosure, or the fusion protein of the disclosure is provided. Attorney Docket No.061817-503001WO In one aspect, a method for inhibiting the growth of a microbial species is provided, the method comprising contacting the microbial species with a nucleic acid of the disclosure, a vector of the disclosure, or a cell of the disclosure. In one aspect, a method of treating a subject diagnosed with, at risk for, or exhibiting symptoms of a bacterial infection is provided, the method comprising, administering at least one endolysin or at least one chimeric lysin of the disclosure, nucleic acid of the disclosure, vector of the disclosure, or the pharmaceutical composition of the disclosure to the subject. In some embodiments, the method additionally comprises administering an accessory protein, wherein the accessory protein enhances the activity of the endolysin or the chimeric lysin. In some embodiments, the accessory protein is a spanin, holin, or a lipopolysaccharide disruption protein. In some embodiments, the subject is a human. In some embodiments, the infection is an infection of the skin. In some embodiments, the composition is administered topically, nasally, inhaled, rectally, endoscopically, enterally, parenterally, or orally. A method for delivering an endolysin or a chimeric lysin selected from Table 1A or Table 1B to a patient in need thereof is provided, the method comprising administering an effective amount of the endolysin or a chimeric lysin to the patient in need thereof. In some embodiments, the deliving comprises topical, oral, intratracheobronchial, pulmonary, and / or nasal administration delivery. In one aspect, a method of treating a bacterial infection caused by a microbial species is provided comprising co-administering to a subject diagnosed with, at risk for, or exhibiting symptoms of a bacterial infection, a composition containing an effective amount of a endolysin or a chimeric lysin specific for the microbial species selected from the endolysins and microbial species in Table 1A or Table 1B comprising an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity to a endolysin sequence selected from Table 1A or Table 1B, or an active fragment thereof and an antibiotic or bacteriostatic therapy. In some embodiments, the endolysin or a chimeric lysin is expressed in a probiotic bacteria. In one aspect, a method for reducing or inhibiting the colonization or growth of a microbial species on a surface is provided comprising contacting said surface with an endolysin or a chimeric lysin specific for the microbial species selected from the endolysins and microbial species in Table 1A or Table 1B. Attorney Docket No.061817-503001WO In some embodiments, the surface is the skin or a mucus membrane of a mammal. In some embodiments, the surface is the surface of a hospital apparatus or a piece ofhospital equipment. In some embodiments, the apparatus or equipment is a surgicalapparatus or piece of surgical equipment. In one aspect, a method of identifying a phage endolysin specific for a microbialspecies is provided, the method comprising: contacting a sample comprising a microbialspecies and a phage with a DNA crosslinking reagent under conditions that allow crosslinking of DNA of the microbial species with DNA of the phage; digesting the crosslinked DNA with one or more restrictions enzymes, wherein the digesting produces crosslinked DNA molecules and results in free DNA ends on the crosslinked DNAmolecules; ligating the free DNA ends with a ligase, thereby connecting the free DNAends of the crosslinked DNA molecule; sequencing the ligated DNA; and analyzing theDNA sequences for the microbial species and the phage; thereby determining themicrobial species and the phage present in the sample. In some embodiments, the method further comprising analyzing the DNA sequences to identify phage endolysins. In one aspect, an endolysin discovered by a method of the disclosure is provided. In some embodiments, the endolysin is selected from Table 1A or Table 1B. In some embodiments, the endolysin is a chimeric endolysin comprising an N- terminal enzymatic activity domain of a first endolysin sequence selected from Table 1A or Table 1B, and a C-terminal cell wall binding domain of a second endolysin sequence selected from Table 1A or Table 1B, wherein the first and the second endolysin sequences are different endolysin sequences. BRIEF DESCRIPTION OF THE DRAWINGSThe features of the present disclosure are set forth with particularity in the appended claims. A better understanding of the features and advantages of the present disclosure will be obtained by reference to the following detailed description that sets forth illustrative embodiments, in which the principles of the disclosure are utilized, and the accompanying drawings of which: FIG.1A shows spot tests of lysin activity against L. cremoris.10 µL of eluate from a lysin protein purification was spotted directly on a lawn of Lactococcus cremorisand cultured overnight on MRS medium. Underlined lysins from PG Database.FIG. 1B shows a growth inhibition and / or lysis of L. cremoris by lysin C2-NP.Overnight Lactococcus cremoris sub-cultured 1:4 in 250 µL fresh MRS medium until Attorney Docket No.061817-503001WO OD600 = approx.0.35. Purified lysin C2-NP or negative control elution buffer was added and incubated at 37ºC for 5 hours. FIGs 2A to 2C show the expression and purification of scaled production of PGL_0260. FIG.2A is a representative Coomassie Blue-stained membrane following SDS-PAGE showing expression of PGL_0260-HIS found in soluble (S) and insoluble pellet (P) fractions in E. coli. Arrow represents the purified PGL_0260-HIS endolysin. FIG.2B is a representative Coomassie Blue-stained membrane showing stable monomeric, dimeric, or trimeric forms of an exemplary nickel chromatography purified endolysin, PGL_0260. PGL_0260 monomer is shown by the arrow, and the stable dimer is shown by *, and the stable trimer is shown by **. FIG. 2C shows the activity of PGL_0260 on clinicalEMJG=NAM& 945<(*-( "*,( IC'XG#$ P=I?JHS?EI "P=I# "+(( IC'XG#$ IJI%NL=IMBJLHA@ 15*)lysate, or water were spotted on a lawn of E. faecium ")( XG PJG&#& 0GG MNL=EIM LAC=L@GAMM JBcharacterized vancomycin or multidrug (including vancomycin) resistance demonstrated clearing. Variability in vancomycin sensitivity was observed, as is common at high concentrations. MDR = Multi Drug Resistant, vanR = a Vancomycin-resistant strain. FIG.3 are graphs showing the activity of the exemplary PGL_0260 lysin in human serum as determined in a turbidity reduction test. Lysin was incubated in human serum for 0h, 1h, 19h followed by another incubation for 15 minutes in human serum containing E. faecium, and then was tested for its activity. FIGs.4A and 4B are graphs showing the activity of the exemplary PGL_0260 lysin at different pH as determined in a turbidity reduction test. Lysin when incubated in sodium phosphate buffers at pH 4.4, 6.5, 7.0, 8.0, and 9.5 for 15 mins, and then was tested for its activity. FIG.5 is a graph showing the activity of the exemplary PGL_0260 lysin at different doses as determined in a turbidity reduction test. PGL_0260 lysin at varying concentrations were added to E. faecium in PBS and OD600 monitored every 15 min over 1h. FIG.6A are representative ESMFold predicted structures of exemplary lysin with domain switching with annotations using the conserved domain database (CDD). FIG.6B is a representative Coomassie Blue-stained membrane following SDS-PAGE showing expression of chimeric lysins shown in FIG.6A. FIG. 6C show the repsentative images from a spot test of lysin activity against E. faecium, E. faecalis, a Vancomycin-Resistant Enterococci strain (VRE), and S. aureaus.10 µL of eluate from a lysin protein purification was spotted directly on a lawn of and cultured overnight on MRS medium. Attorney Docket No.061817-503001WO DETAILED DESCRIPTIONThe present disclosure relates, in part, to compositions and methods of phage derived endolysins specific for a microbial species. The endolysin compositions can be used as antimicrobials against specific bacterial cells in vitro and in vivo. The endolysins of the disclosure can be used to prevent or treat microbial infections in subjects in need thereof. The endolysins of the disclosure can be used to prevent or eradicate microbial species present in biofilms in subjects need thereof. The endolysins of the disclosure can be used to prevent or eradicate microbial species present in biofilms present on devices. The endolysins described herein can offer host specificity and can minimize damage to the microbiome in a subject compared to broad-spectrum antibiotics. They may trigger the release of pathogen-associated molecular patterns (PAMPs) in a subject but may not induce significant resistance in bacteria. Definitions The abbreviations used herein have their conventional meaning within the chemical and biological arts. The terms “a” or “an,” as used in herein means one or more. In the present description, various aspects of the invention can be presented in a range format. It should be understood that the description in range format is merely for convenience and brevity and should not be construed as an inflexible limitation on the scope of the invention. Accordingly, the description of a range should be considered to have specifically disclosed all the possible subranges as well as individual numerical values within that range. For example, description of a range such as from 1 to 6 should be considered to have specifically disclosed subranges such as from 1 to 3, from 1 to 4, from 1 to 5, from 2 to 4, from 2 to 6, from 3 to 6 etc., as well as individual numbers within that range, for example, 1, 2, 2.7, 3, 4, 5, 5.3, and 6. As another example, a range such as 95- 99% identity, includes something with 95%, 96%, 97%, 98% or 99% identity, and includes subranges such as 96-99%, 96-98%, 96-97%, 97-99%, 97-98% and 98-99% identity. This applies regardless of the breadth of the range. In the present description, any concentration range, percentage range, ratio range, or integer range is to be understood to include the value of any integer within the recited range and, when appropriate, fractions thereof (such as one tenth and one hundredth of an integer), unless otherwise indicated. The term “about,” when immediately preceding a number or numeral, means that the number or numeral ranges plus or minus 10%. Attorney Docket No.061817-503001WO “Gram-negative bacteria” generally refers to bacteria which produce a crystal violet stain that is decolorized in Gram staining, i. e., they do not retain crystal violet dye in the Gram staining protocol. Gram-negative bacteria can be characterized by an outer membrane composed of lipopolysaccharide (LPS) molecules with a highly variable O- polysaccharide (O-antigen). “Gram-positive bacteria” generally refers to bacteria which produce a crystal violet stain that is colorized in Gram staining, i. e., they do retain crystal violet dye in the Gram staining protocol. Gram-positive bacteria can have essential components such as (lipo)teichoic acids embedded in peptidoglycan (PG). Gram-positive bacteria include but are not limited to the genera Actinomyces, Bacillus, Listeria, Lactococcus, Staphylococcus, Streptococcus, Enterococcus, Mycobacterium, Corynebacterium, and Clostridium. Medically relevant species include Streptococcus pyogenes, Streptococcus pneumoniae, Staphylococcus aureus, and Enterococcus faecalis. Bacillus species, which are spore- forming, cause anthrax and gastroenteritis. Spore-forming Clostridium species are responsible for botulism, tetanus, gas gangrene and pseudomembranous colitis. Corynebacterium species cause diphtheria, Listeria species cause meningitis.Enterococcus species can cause urinary tract infections (UTI), bacteremia, and infectiveendocarditis and rarely cause intra-abdominal infections and meningitis. Staphylococcus species can cause skin infections, bacteremia, bone infections, emdocarditis, food poisoning, pneumonia, and toxoc shock syndrome. Streptococcus species can cause pharyngitis, pneumonia, wound and skin infections, sepsis, and endocarditis. The term “bactericidal” in the context of an agent or composition conventionally means having the property of causing the death of bacteria or capable of killing bacteria to an extent of at least a 3-log (99.9%) or better reduction among an initial population of bacteria. The term “bacteriostatic” in the context of an agent or composition conventionally means having the property of inhibiting bacterial growth, including inhibiting growing bacterial cells, thus causing a 2-log (99%) or better and up to just under a 3-log reduction among an initial population of bacteria. The term “antibacterial” in the context of an agent or composition is used generically to include both bacteriostatic and bactericidal agents. The term “drug resistant” in a context of a pathogen and more specifically a bacterium, generally refers to a bacterium that is resistant to the antimicrobial activity of a drug. When used in a more particular way, drug resistance specifically refers to antibiotic Attorney Docket No.061817-503001WO resistance. In some cases, a bacterium that is generally susceptible to a particular antibiotic can develop resistance to the antibiotic, thereby becoming a drug resistant microbe or strain. A “multi-drug resistant” pathogen is one that has developed resistance to at least two classes of antimicrobial drugs, each used as monotherapy. For example, certain strains of Pseudomonas aeruginosa have been found to be resistant to nearly all or all antibiotics including aminoglycosides, cephalosporins, fluoroquinolones, and carbapenems (Antibiotic Resistant Threats in the United States, 2013, U.S. Department of Health and Services, Centers for Disease Control and Prevention). One skilled in the art can readily determine if a bacterium is drug resistant using routine laboratory techniques that determine the susceptibility or resistance of a bacterium to a drug or antibiotic. The term “pharmaceutically acceptable carrier” includes any and all solvents, additives, excipients, dispersion media, solubilizing agents, coatings, preservatives, isotonic and absorption delaying agents, surfactants, propellants and the like that are physiologically compatible. The carrier(s) must be “acceptable” in the sense of not being deleterious to the subject to be treated in amounts typically used in medicaments. Pharmaceutically acceptable carriers are compatible with the other ingredients of the composition without rendering the composition unsuitable for its intended purpose. Furthermore, pharmaceutically acceptable carriers are suitable for use with subjects as provided herein without undue adverse side effects (such as toxicity, irritation, and allergic response). Side effects are “undue” when their risk outweighs the benefit provided by the composition. Non-limiting examples of pharmaceutically acceptable carriers or excipients include any of the standard pharmaceutical carriers such as phosphate buffered saline solutions, water, and emulsions such as oil / water emulsions and microemulsions. For solid compositions comprising a lyophilized endolysin polypeptide, excipients such as urea or mesna (2-mercaptoethane sulfonate) can be included to improve stability. Other excipients include bulking agents, buffering agents, tonicity modifiers, surfactants, preservatives and co-solvents. For solid oral compositions comprising endolysin polypeptide, suitable pharmaceutically acceptable excipients include, but are not limited to, starches, sugars, diluents, granulating agents, lubricants, binders, disintegrating agents and the like. For liquid oral compositions, suitable pharmaceutically acceptable excipients include, but are not limited to, water, glycols, oils, alcohols, flavoring agents, preservatives, and the like. For topical solid compositions such as creams, gels, foams, ointments, or sprays, suitable excipients include, but are not limited to a cream, a cellulosic or oily base, emulsifying agents, stiffening agents, rheology modifiers or thickeners, surfactants, emollients, Attorney Docket No.061817-503001WO preservatives, humectants, alkalizing or buffering agents, and solvents. Suitable excipients for the formulation of the foam base include, but are not limited to, propylene glycol, emulsifying wax, cetyl alcohol, and glyceryl stearate. Potential preservatives include methylparaben and propylparaben. The term “inhalable composition” refers to pharmaceutical compositions of the present disclosure that are formulated for direct delivery to the respiratory tract during or in conjunction with routine or assisted respiration (e.g., by intratracheobronchial, pulmonary, and / or nasal administration), including, but not limited to, atomized, nebulized, dry powder and / or aerosolized formulations. The term “effective amount” refers to an amount which, when applied or administered in an appropriate frequency or dosing regimen, is sufficient to prevent or inhibit bacterial growth or prevent, reduce or ameliorate the onset, severity, duration or progression of the disorder being treated (here bacterial pathogen growth or infection), prevent the advancement of the disorder being treated, cause the regression of the disorder being treated, or enhance or improve the prophylactic or therapeutic effect(s) of another therapy, such as antibiotic or bacteriostatic therapy. The term “co-administer” is intended to embrace separate administration of an endolysin polypeptide and an antibiotic or any other antibacterial agent in a sequential manner as well as administration of these agents in a substantially simultaneous manner, such as in a single mixture / composition or in doses given separately, but nonetheless administered substantially simultaneously to the subject, for example at different times in the same day or 24-hour period. Such co-administration of endolysin polypeptides with one or more additional antibacterial agents can be provided as a continuous treatment lasting up to days, weeks, or months. Additionally, depending on the use, the co- administration need not be continuous or co-extensive. For example, if the use were as a topical antibacterial agent to treat, e.g., a bacterial ulcer or an infected diabetic ulcer, the endolysin could be administered only initially within 24 hours of the first antibiotic use and then the antibiotic use may continue without further administration of endolysin. The term “subject” refers to a subject to be treated and includes inter alia a mammal, a plant, a lower animal, a single cell organism or a cell culture. For example, the term “subject” is intended to include organisms, e.g., prokaryotes and eukaryotes, which are susceptible to – afflicted with Gram-negative or Gram-positive bacterial infections. Examples of subjects include mammals, e.g., humans, dogs, cows, horses, pigs, sheep, goats, cats, mice, rabbits, rats, and transgenic non-human animals. In certain Attorney Docket No.061817-503001WO embodiments, the subject is a human, e.g., a human suffering from, at risk of suffering from, or susceptible to a Gram-negative or Gram-positive bacterial infection, whether such infection be systemic or confined to a particular organ or tissue. The term “fusion polypeptide” refers to an expression product resulting from the fusion of two or more nucleic acid segments, resulting in a fused expression product typically having two domains or segments with different properties or functionality. In a more particular sense, the term “fusion polypeptide” also refers to a polypeptide or peptide comprising two or more heterologous polypeptides or peptides covalently linked, either directly or via an amino acid or peptide linker. The polypeptides forming the fusion polypeptide are typically linked C-terminus to N-terminus, although they can also be linked C-terminus to C-terminus, N-terminus to N-terminus, or N-terminus to C-terminus. The term “fusion polypeptide” can be used interchangeably with the term “fusion protein.” Thus the open-ended expression “a polypeptide comprising” a certain structure includes larger molecules than the recited structure such as fusion polypeptides. The term “active fragment” refers to a portion of a full-length polypeptide disclosed herein which retains one or more functions or biological activities of the isolated original polypeptide. The term “functional variant” refers a portion of a full-length polypeptide disclosed herein or a polypeptide with amino acid substitutions, insertions, or deletions that retains one or more functions or biological activities of the isolated original polypeptide. For example, a functional variant may not include the starting methionine (M) at the N- terminus of a protein. The term “hydrophobic group” refers to a chemical group such as an amino acid side chain which has low or no affinity for water molecules but higher affinity for oil molecules. Hydrophobic substances tend to have low or no solubility in water or aqueous phases and are typically apolar but tend to have higher solubility in oil phases. Examples of hydrophobic amino acids include glycine (Gly), alanine (Ala), valine (Val), leucine (Leu), isoleucine (Ile), proline (Pro), phenylalanine (Phe), methionine (Met), and tryptophan (Trp). The term “derivative” in the context of a peptide or polypeptide (which as stated herein includes an active fragment) is intended to encompass for example, a polypeptide modified to contain one or more-chemical moieties other than an amino acid that do not substantially adversely impact or destroy the endolysin activity. The chemical moiety can be linked covalently to the peptide, e.g., via an amino terminal amino acid residue, a Attorney Docket No.061817-503001WO carboxy terminal amino acid residue, or at an internal amino acid residue. Such modifications include the addition of a protective or capping group on a reactive moiety, addition of a detectable label, such as antibody and / or fluorescent label, addition or modification of glycosylation, or addition of a bulking group such as PEG (pegylation) and other changes that do not substantially adversely impact or destroy the activity of the endolysin polypeptide. Polyethylene glycol (PEG) conjugation to proteins has been used as a method for extending th circulateng half-life of many pharmaceutical proteins. Thus, in the context of endolysin polypeptide derivatives, the term “derivative” encompasses endolysin polypeptides chemically modified by covalent attachment of one or more PEG molecules. It is anticipated that pegylated endolysin polypeptides may exhibit prolonged circulation half-life compared to the unpegylated endolysin polypeptides, while retaining biological and therapeutic activity. The term “biofilm” refers to bacteria that attach to surfaces and aggregate in a hydrated polymeric matrix of their own synthesis. A biofilm is an aggregate of microorganisms in which cells adhere to each other on a surface. These adherent cells are frequently embedded within a self-produced matrix of extracellular polymeric substance (EPS). Biofilm EPS, which is also referred to as slime (although not everything described as slime is a biofilm) or plaque, is a polymeric conglomeration generally composed of extracellular DNA, proteins, and polysaccharides. The terms “bind” and “bound” as used herein is used in accordance with its plain and ordinary meaning and refers to the association between atoms or molecules. The association can be direct or indirect. For example, bound atoms or molecules may be bound, e.g., by covalent bond, linker (e.g., a first linker or second linker), or non-covalent bond (e.g. electrostatic interactions (e.g., ionic bond, hydrogen bond, halogen bond), van der Waals interactions (e.g. dipole-dipole, dipole-induced dipole, London dispersion), ring stacking (pi effects), hydrophobic interactions and the like). As used herein, the term “conjugated” when referring to two moieties means the two moieties are bonded, wherein the bond or bonds connecting the two moieties may be covalent or non-covalent. In embodiments, the two moieties are covalently bonded to each other (e.g., directly or through a covalently bonded intermediary). In embodiments, the two moieties are non-covalently bonded (e.g., through ionic bond(s), van der Waal’s bond(s) / interactions, hydrogen bond(s), polar bond(s), or combinations or mixtures thereof). Attorney Docket No.061817-503001WO The term “amino acid” refers to naturally occurring and synthetic amino acids, as well as amino acid analogs and amino acid mimetics that function in a manner similar to the naturally occurring amino acids. Naturally occurring amino acids are those encoded by the genetic code, as well as those amino acids that are later modified, e.g.,DS@LJRSKLJGEIA$ V%?=L>JRSCGON=H=NA$ =I@ 8%KDJMKDJMALEIA& 0HEIJ =?E@ =I=GJCM LABALM NJcompounds that have the same basic chemical structure as a naturally occurring amino=?E@$ E&A&$ =I U ?=L>JI ND=N EM >JOI@ NJ = DS@LJCAI$ = ?=L>JRSG CLJOK$ =I =HEIJ CLJOK$ =I@an R group, e.g., homoserine, norleucine, methionine sulfoxide, methionine methyl sulfonium. Such analogs have modified R groups (e.g., norleucine) or modified peptide backbones, but retain the same basic chemical structure as a naturally occurring amino acid. Amino acid mimetics refers to chemical compounds that have a structure that is different from the general chemical structure of an amino acid, but that functions in a manner similar to a naturally occurring amino acid. The terms “non-naturally occurring amino acid” and “unnatural amino acid” refer to amino acid analogs, synthetic amino acids, and amino acid mimetics which are not found in nature. Amino acids may be referred to herein by either their commonly known three letter symbols or by the one-letter symbols recommended by the IUPAC-IUB Biochemical Nomenclature Commission. Nucleotides, likewise, may be referred to by their commonly accepted single-letter codes. The terms “polypeptide,” “peptide,” and “protein” are used interchangeably herein to refer to a polymer of amino acid residues. The terms apply to amino acid polymers in which one or more amino acid residue is an artificial chemical mimetic of a corresponding naturally occurring amino acid, as well as to naturally occurring amino acid polymers and non-naturally occurring amino acid polymers. A “fusion protein” refers to a chimeric protein encoding two or more separate protein sequences that are recombinantly expressed as a single moiety. As to amino acid sequences, one of skill will recognize that individual substitutions, deletions or additions to a nucleic acid, peptide, polypeptide, or protein sequence which alters, adds or deletes a single amino acid or a small percentage of amino acids in the encoded sequence is a "conservatively modified variant" where the alteration results in the substitution of an amino acid with a chemically similar amino acid. Conservative substitution tables providing functionally similar amino acids are well known in the art. Such conservatively modified variants are in addition to and do not exclude polymorphic variants, interspecies homologs, and alleles of the disclosure. Attorney Docket No.061817-503001WO The following eight groups each contain amino acids that are conservative substitutions for one another: 1) Alanine (A), Glycine (G); 2) Aspartic acid (D), Glutamic acid (E); 3) Asparagine (N), Glutamine (Q); 4) Arginine (R), Lysine (K); 5) Isoleucine (I), Leucine (L), Methionine (M), Valine (V); 6) Phenylalanine (F), Tyrosine (Y), Tryptophan (W); 7) Serine (S), Threonine (T); and 8) Cysteine (C), Methionine (M) (see, e.g., Creighton, Proteins (1984)). Percentage of “sequence identity” is determined by comparing two optimally aligned sequences over a comparison window, wherein the portion of the polynucleotide or polypeptide sequence in the comparison window may comprise additions or deletions (i.e., gaps) as compared to the reference sequence (which does not comprise additions or deletions) for optimal alignment of the two sequences. The percentage is calculated by determining the number of positions at which the identical nucleic acid base or amino acid residue occurs in both sequences to yield the number of matched positions, dividing the number of matched positions by the total number of positions in the window of comparison and multiplying the result by 100 to yield the percentage of sequence identity. The terms “identical” or percent “identity,” in the context of two or more nucleic acids or polypeptide sequences, refer to two or more sequences or subsequences that are the same or have a specified percentage of amino acid residues or nucleotides that are the same (i.e., about 60% identity, preferably 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or higher identity over a specified region, when compared and aligned for maximum correspondence over a comparison window or designated region) as measured using a BLAST or BLAST 2.0 sequence comparison algorithms with default parameters described below, or by manual alignment and visual inspection (see, e.g., NCBI web site http: / / www.ncbi.nlm.nih.gov / BLAST / or the like). Such sequences are then said to be "substantially identical." This definition also refers to, or may be applied to, the compliment of a test sequence. The definition also includes sequences that have deletions and / or additions, as well as those that have substitutions. As described below, the preferred algorithms can account for gaps and the like. Preferably, Attorney Docket No.061817-503001WO identity exists over a region that is at least about 25 amino acids or nucleotides in length, or more preferably over a region that is 50-100 amino acids or nucleotides in length. An amino acid or nucleotide base “position” is denoted by a number that sequentially identifies each amino acid (or nucleotide base) in the reference sequence based on its position relative to the N-terminus (or 5'-end). Due to deletions, insertions, truncations, fusions, and the like that must be taken into account when determining an optimal alignment, in general the amino acid residue number in a test sequence determined by simply counting from the N-terminus will not necessarily be the same as the number of its corresponding position in the reference sequence. For example, in a case where a variant has a deletion relative to an aligned reference sequence, there will be no amino acid in the variant that corresponds to a position in the reference sequence at the site of deletion. Where there is an insertion in an aligned reference sequence, that insertion will not correspond to a numbered amino acid position in the reference sequence. In the case of truncations or fusions there can be stretches of amino acids in either the reference or aligned sequence that do not correspond to any amino acid in the corresponding sequence. The terms “numbered with reference to” or “corresponding to,” when used in the context of the numbering of a given amino acid or polynucleotide sequence, refers to the numbering of the residues of a specified reference sequence when the given amino acid or polynucleotide sequence is compared to the reference sequence. An amino acid residue in a protein “corresponds” to a given residue when it occupies the same essential structural position within the protein as the given residue. The term “isolated,” when applied to a nucleic acid or protein, denotes that the nucleic acid or protein is essentially free of other cellular components with which it is associated in the natural state. It can be, for example, in a homogeneous state and may be in either a dry or aqueous solution. Purity and homogeneity are typically determined using analytical chemistry techniques such as polyacrylamide gel electrophoresis or high performance liquid chromatography. A protein that is the predominant species present in a preparation is substantially purified. As may be used herein, the terms “nucleic acid,” “nucleic acid molecule,” “nucleic acid oligomer,” “oligonucleotide,” “nucleic acid sequence,” “nucleic acid fragment” and “polynucleotide” are used interchangeably and are intended to include, but are not limited to, a polymeric form of nucleotides covalently linked together that may have various lengths, either deoxyribonucleotides or ribonucleotides, or analogs, derivatives or modifications thereof. Different polynucleotides may have different three-dimensional Attorney Docket No.061817-503001WO structures, and may perform various functions, known or unknown. Non-limiting examples of polynucleotides include a gene, a gene fragment, an exon, an intron, intergenic DNA (including, without limitation, heterochromatic DNA), messenger RNA (mRNA), transfer RNA, ribosomal RNA, a ribozyme, cDNA, a recombinant polynucleotide, a branched polynucleotide, a plasmid, a vector, isolated DNA of a sequence, isolated RNA of a sequence, a nucleic acid probe, and a primer. Polynucleotides useful in the methods of the disclosure may include natural nucleic acid sequences and variants thereof, artificial nucleic acid sequences, or a combination of such sequences. A polynucleotide is typically composed of a specific sequence of four nucleotide bases: adenine (A); cytosine (C); guanine (G); and thymine (T) (uracil (U) for thymine (T) when the polynucleotide is RNA). Thus, the term “polynucleotide sequence” is the alphabetical representation of a polynucleotide molecule; alternatively, the term may be applied to the polynucleotide molecule itself. This alphabetical representation can be input into databases in a computer having a central processing unit and used for bioinformatics applications such as functional genomics and homology searching. Polynucleotides may optionally include one or more non-standard nucleotide(s), nucleotide analog(s) and / or modified nucleotides. As used herein, a “subsequence” refers to a length of contiguous amino acids or nucleotides that form a part of a sequence described herein. A subsequence may be identical to a part of a full length sequence when aligned to the full length sequence, or less than 100% identical to the part of the full length sequence to which it aligns (e.g., 90% identical to 50% of the full sequence, or the like). The term “exogenous” is used herein to refer to any molecule, including nucleic acids, protein or peptides, small molecular compounds, and the like that originate from outside the organism. In contrast, the term “endogenous” refers to any molecule that originates from inside the organism (i.e., naturally produced by the organism). A polynucleotide is “operably linked” to another polynucleotide when it is placed into a functional relationship with the other polynucleotide. For example, a promoter or enhancer is operably linked to a coding sequence if it affects the transcription of the sequence. A peptide is "operably linked" to another peptide when the polynucleotides encoding them are operably linked, preferably they are in the same open reading frame. Attorney Docket No.061817-503001WO A “promoter” is a sequence of DNA needed to turn a gene on or off. Promoters are located immediately upstream and / or overlapping the transcription start site, and are usually between about one hundred to several hundred base pairs in length. The term “antibody” refers to a polypeptide encoded by an immunoglobulin gene or functional fragments thereof that specifically binds and recognizes an antigen. The recognized immunoglobulin genes include the kappa, lambda, alpha, gamma, delta, epsilon, and mu constant region genes, as well as the myriad immunoglobulin variable region genes. Light chains are classified as either kappa or lambda. Heavy chains are classified as gamma, mu, alpha, delta, or epsilon, which in turn define the immunoglobulin classes, IgG, IgM, IgA, IgD and IgE, respectively. A “cell” as used herein, refers to a cell carrying out metabolic or other functions sufficient to preserve or replicate its genomic DNA. A cell can be identified by well- known methods in the art including, for example, presence of an intact membrane, staining by a particular dye, ability to produce progeny or, in the case of a gamete, ability to combine with a second gamete to produce a viable offspring. Cells may include prokaryotic and eukaryotic cells. Prokaryotic cells include but are not limited to bacteria. Eukaryotic cells include but are not limited to yeast cells and cells derived from plants and animals, for example mammalian, insect (e.g., spodoptera) and human cells. Cells may be useful when they are naturally nonadherent or have been treated not to adhere to surfaces, for example by trypsinization. The term “plasmid,” “expression vector,” or “viral vector” refers to a nucleic acid molecule that encodes for genes and / or regulatory elements necessary for the expression of genes. Expression of a gene from a plasmid can occur in cis or in trans. If a gene is expressed in cis, gene and regulatory elements are encoded by the same plasmid. Expression in trans refers to the instance where the gene and the regulatory elements are encoded by separate plasmids. Suitable viral vectors contemplated herein include, for example, lentiviral vectors and onco-retroviral vectors. As used herein, the term “expression” is used in accordance with its plain ordinary meaning and refers to a step involved in the production of the polypeptide including, but not limited to, transcription, post-transcriptional modification, translation, post- translational modification, and secretion. Expression may be detected using conventional techniques for detecting protein (e.g., ELISA, Western blotting, flow cytometry, immunofluorescence, immunohistochemistry, etc.). Attorney Docket No.061817-503001WO Endolysins Provided herein are endolysin polypeptides (including active fragments thereof). In particular, the present disclosure relates to endolysin polypeptides (including fragments thereof) active against microorganisms including Gram-negative bacteria, such as Acinetobacter, Paenibacillus, or Campylobacter, and Gram-positive bacteria, such as Streptococcus species, Enterococcus species, and / or Staphylococcus species. Endolysins are bacteriophage-encoded peptidoglycan hydrolases. Bacterial cells can be lysed by endolysins specific for the bacterial species by targeting peptidoglycans in the cell wall. Gram-positive bacteria can be targeted with endolysins due to their naturally exposed peptidoglycan layer. Endolysins can have a modular architecture composed of one or more catalytic or enzymatically active domains (EAD) that may be connected by flexible linkers to one or more cell wall-binding domains (CBD). The EADs can be broadly distributed into three classes (glycosidases, amidases, and peptidases) depending on the type of bond in the peptidoglycan (murein) cell wall that they can act upon. Differences in CBD presence and composition can be largely dependent upon the bacterial target. Endolysins of Gram positive bacteria can contain one or more N-terminal EAD and one or more C-terminal CBD, but endolysins acting on Gram-negative bacteria typically only have one EAD. In both cases, a successful phage lytic cycle relies on endolysin access to the peptidoglycan cell wall, meaning the enzyme must cross the inner or cytoplasmic membrane. This access is typically achieved through holins, proteins that form channels in the inner membrane which allow the enzyme access to the periplasmic space. The mode of action for endolysins can have implications for their application as antimicrobials. For Gram-positive bacteria, externally applied endolysins can directly access and degrade the cell wall, but for Gram negative bacteria the outer membrane poses a barrier that requires further consideration when selecting and screening candidate endolysins. The activity of an endolysins can include degrading the cell wall / membrane, binding of the cell wall / membrane, or cell surface receptors, penetrating the cell wall / membrane, and / or outer membrane destabilization. In one aspect, the isolated bacterial endolysin comprises an amino acid sequence selected from Table 1A or Table 1B, or functional variants thereof. In one aspect, the isolated bacterial endolysin can be a recombinant endolysin. In one aspect, the lysin is a chimeric lysin. In one embodiment, the isolated bacterial endolysin is selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 80%, 85%, 90%, 91%, 92%, Attorney Docket No.061817-503001WO 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to a sequence selected fromSEQ ID NO: 1-313 or SEQ ID NOs. 314-364.In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 80% sequence identity to a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 85% sequence identity to a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 90% sequence identity to a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 91% sequence identity to a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 92% sequence identity to a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 93% sequence identity to a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 94% sequence identity to a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 95% sequence identity to a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 96% sequence identity to a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 97% sequence identity to a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 98% sequence identity to a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 99% sequence identity to a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one aspect, the bacterial endolysin is a bacterial endolysin having at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to a200 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313or SEQ ID NOs.314-364. Attorney Docket No.061817-503001WO In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 85% sequence identity to a 200 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 90% sequence identity to a 200 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 91% sequence identity to a 200 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 92% sequence identity to a 200 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 93% sequence identity to a 200 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 94% sequence identity to a 200 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 95% sequence identity to a 200 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 96% sequence identity to a 200 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 97% sequence identity to a 200 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 98% sequence identity to a 200 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 99% sequence identity to a 200 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one aspect, the bacterial endolysin is a bacterial endolysin having at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to a Attorney Docket No.061817-503001WO150 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 80% sequence identity to a 150 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 85% sequence identity to a 150 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 90% sequence identity to a 150 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 91% sequence identity to a 150 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 92% sequence identity to a 150 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 93% sequence identity to a 150 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 94% sequence identity to a 150 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 95% sequence identity to a 150 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 96% sequence identity to a 150 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 97% sequence identity to a 150 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. In one embodiment, the isolated bacterial endolysin is an isolated bacterial endolysin having at least 98% sequence identity to a 150 amino acid continuous sequence within a sequence selected from SEQ ID NOs: 1-313 or SEQ ID NOs.314-364. Attorney Docket No.061817-503001WO Table 1A: Illustrative Endolysin Sequences and Targeted Microbial Species Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Table 1B: Illustrative Endolysin Sequences and Targeted Microbial Species Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO Attorney Docket No.061817-503001WO In one embodiment, the endolysin targets a microbial species. In one embodiment, the microbial species is a Gram-positive bacteria. In one embodiment, the microbial species is a Gram-negative bacteria. In one embodiment, the endolysin targets a Streptococcus species. In one embodiment, the endolysin targets an Enterococcus species. In one embodiment, the endolysin targets a Staphylococcus species. In one embodiment, the endolysin targets a Lactococcus species. In one embodiment, the endolysin targets an Acinetobacter species. In one embodiment, the endolysin targets a Paenibacillus species. In one embodiment, the endolysin targets a Campylobacter species. In one embodiment, the targeting comprises a lytic activity against a microbial species. In one embodiment, the targeting comprises a hydrolase activity against a microbial species. In one embodiment, the targeting comprises a glycosidase activity against a microbial species. In one embodiment, the targeting comprises an amidase activity against a microbial species. In one embodiment, the targeting comprises a peptidase activity against a microbial species. In one embodiment, the endolysin has activity against a microbial species. In one embodiment, the activity comprises inhibiting the growth of a microbial species. In one Attorney Docket No.061817-503001WO embodiment, the activity comprises killing a microbial species. In one embodiment, the activity comprises reducing the growth of a microbial species. In some embodiments, the lysin of the disclosure retains activity against a microbial species under physiological conditions. In some embodiments, the lysin of the disclosure retains activity against a microbial species in human serum. In some embodiments, the lysin of the disclosure retains activity against a microbial species under strongly acidic, acidic, neutral, alkaline, or strongly alkaline pH levels. In one embodiment, the endolysin is engineered to reduce protease degradation and increase stability of the endolysin. Proteases that degrade endolysins include but are not limited to trypsin, chymotrypsin, pepsin, and peptidase. Protease degradation can be reduced, for example by removing or mutating protease cleavage sites. In one embodiment, the endolysin is protease resistant. In one embodiment, the endolysin engineered to reduce immunogenicity. In one embodiment, the endolysin is a fusion protein. In one embodiment, the endolysin comprises an N or C terminal fusion protein. In one embodiment, the endolysin is fused with a bacteriocin. In one embodiment, the bacteriocin is derived from a Gram- positive bacteria. In one embodiment, the bacteriocin is derived from a Gram-negative bacteria. Exemplary bacteriocins comprise colicin, microcin, and bacteriocins from Archaea. Exemplary bacteriocins are shown in Table 2. In one embodiment, the bacteriocin is selected from a bacteriocin in Table 2. Table 2: Exemplary Bacteriocins Attorney Docket No.061817-503001WO In one embodiment, the endolysin is a chimeric lysin. In one embodiment, the chimeric lysin comprises domains from one or more endolysins. In one embodiment, the chimeric lysin comprises domains from one or more endolysins selected from Table 1A or Table 1B. In one embodiment, the chimeric lysin comprises catalytic N-terminal domains and cell wall-binding domains from one or more endolysins. In one embodiment, the chimeric lysin comprises rearranged N- and C-terminal domains of the same endolysin. In one embodiment, the chimeric lysin comprises rearranged N- and C-terminal domains of the different endolysins. In one embodiment, the chimeric lysin comprises the enzymatic activity domain of a first endolysin and the cell-wall binding domain of a second endolysin, wherein the first and the second endolysin are different endolysin sequences selected from Table 1A or Table 1B. In one embodiment, the chimeric lysin comprises a N-terminal enzymatic activity domain of a first endolysin and a C-terminal cell-wall binding domain of a second endolysin, wherein the first and the second endolysin are different endolysin sequences selected from Table 1A or Table 1B. In one embodiment, the chimeric lysin comprises a N-terminal cell-wall binding domain of a first endolysin and a C-terminal enzymatic activity domain of a second endolysin, wherein the first and the second endolysin are different endolysin sequences selected from Table 1A or Table 1B. In some embodiments, the chimeric lysin comprises more than two domains. In some emdodiments, the chimeric lysin comprises a first and a second enzymatic activity domain of a first and a second endolysin and a third cell-wall binding domain of a third endolysin, wherein the first, second and the third endolysins are different endolysin sequences selected from Table 1A or Table 1B. In some emdodiments, the chimeric lysin comprises a first and a second enzymatic activity domain of a first and a second endolysin and a third cell-wall binding domain of a third endolysin, wherein the first and the second endolysin are the same endolysin sequences selected from Table 1A or Table 1B, and the third endolysin is a different endolysin sequence selected from Table 1A or Table 1B. In some emdodiments, the chimeric lysin comprises a first and a second cell-wall binding domain of a first and a second endolysin and a third enzymatic activity domain of a third endolysin, wherein the first, second and the third endolysins are different endolysin sequences selected from Table 1A or Table 1B. Attorney Docket No.061817-503001WO In some emdodiments, the chimeric lysin comprises a first and a second cell wall binding domain of a first and a second endolysin and a third enzymatic activity domain of a third endolysin, wherein the first and the second endolysin are the same endolysin sequences selected from Table 1A or Table 1B, and the third endolysin is a different endolysin sequence selected from Table 1A or Table 1B. In one aspect, an isolated and / or recombinant chimeric endolysin comprising an N- terminal enzymatic activity domain of a first endolysin sequence selected from Table 1A or Table 1B, and a C-terminal cell wall binding domain of a second endolysin sequence selected from Table 1A or Table 1B, wherein the first and the second endolysins are different endolysin seqeuences is provided. In embodiments, an isolated and / or recombinant chimeric endolysin comprising an N-terminal cell-wall binding domain of a first endolysin sequence selected from Table 1A or Table 1B, and a C-terminal enzymatic activity domain of a second endolysin sequence selected from Table 1A or Table 1B, wherein the first and the second endolysins are different endolysin seqeuences is provided. In embodiments, an isolated and / or recombinant chimeric endolysin comprising a first and a second enzymatic activity domain of a first and a second endolysin selected from Table 1A or Table 1B, and a cell-wall binding domain of a third endolysin sequence selected from Table 1A or Table 1B is provided. In embodiments, an isolated and / or recombinant chimeric endolysin comprising a first and a second cell-wall binding domain of a first and a second endolysin selected from Table 1A or Table 1B, and an enzymatic activity domain of a third endolysin sequence selected from Table 1A or Table 1B is provided, In one embodiment, the endolysin is a circular permuted endolysin. A circular permutation is a relationship between proteins whereby the proteins have a changed order of amino acids in their peptide sequence. The result is a protein structure with different connectivity, but overall similar three-dimensional (3D) shape. In one embodiment, the endolysin is virion associated. In one embodiment, the endolysin further comprises a virion-associated polysaccharide depolymerases. In one embodiment, the polysaccharide depolymerase is a hydrolase. In one embodiment, the hydrolase is a sialidase, rhamnosidase, levanase, xylanase, or a dextranase. In one embodiment, the polysaccharide depolymerases is a lyase. In Attorney Docket No.061817-503001WO one embodiment, the lyase is a hyaluronidase, pectate / pectin lyase, alginate lyase, or a K5 lyase. In one embodiment, the endolysin is cysteine modified. In one embodiment, the endolysin comprises an N-terminal cysteine. In one embodiment, the endolysin comprises a C-terminal cysteine. In one aspect, the bacterial endolysin comprises an N or C terminal fusion protein. In embodiments, the fusion protein is a tag. In one embodiment, the fusion protein is a signal sequence. In one embodiment, the fusion protein is a protein tag. In some embodiments, the fusion protein has a purification tag. In one embodiment, the purification tag is a histidine (6x His) tag. In some embodiments, the purification tag is a FLAG-tag, Strep-tag, MBP, GST, and epitope tags like HA, V5, and c-Myc. In one embodiment, the fusion protein is a fluorescent protein. In one embodiment, the fluorescent protein is a GFP protein. In one embodiment, the fluorescent protein is a GFP, an eGFP, a RFP, a YFP, a BFP, or a CFP. In one embodiment, the bacterial endolysin comprises a targeting protein or peptide. In one embodiment, the targeting protein or peptide targets the bacterial endolysin to a specific cell type. In one embodiment, the targeting protein is an antibody or an antibody fragment. Provided herein are, inter alia, nucleic acids encoding an endolysin described herein. In some embodiments, the nucleic acid is a DNA or RNA. In some embodiments, the DNA is circular plasmid DNA, linear double-strand DNA, single strand DNA, or chimeric RNA and DNA. In some embodiments, the RNA is mRNA. In some embodiments, the mRNA comprises nucleic acid mimetics selected from the group of peptide nucleic acid (PNA), morpholino nucleic acid, cyclohexenyl nucleic acid (CeNAs), and locked nucleic acid (LNA). In some embodiments, the mRNA comprises modified sugar moieties, optionally wherein the modified sugar moiety is selected from the group of N1-methylpseudouridine, 9-Methyladenine, 2'-O-(2-methoxyethyl), 2'-dimethylaminooxyethoxy, 2'- dimethylaminoethoxyethoxy, 2'-O-methyl, and 2'-fluoro. In some embodiments, the mRNA comprises a modified nucleobase, optionally wherein the modified nucleobase is selected from the group of a 5-methylcytosine; a 5-hydroxymethyl cytosine; a xanthine; a hypoxanthine; a 2-aminoadenine; a 6-methyl derivative of adenine; a 6-methyl derivative of guanine; a 2-propyl derivative of adenine; a 2-propyl derivative of guanine; a 2- thiouracil; a 2-thiothymine; a 2-thiocytosine; a 5-halouracil; a 5-halocytosine; a 5- Attorney Docket No.061817-503001WO propynyl uracil; a 5-propynyl cytosine; a 6-azo uracil; a 6-azo cytosine; a 6-azo thymine; a pseudouracil; a 4-thiouracil; an 8-halo; an 8-amino; an 8-thiol; an 8-thioalkyl; an 8- hydroxyl; a 5-halo; a 5-bromo; a 5-trifluoromethyl; a 5-substituted uracil; a 5-substituted cytosine; a 7-methylguanine; a 7-methyladenine; a 2-F-adenine; a 2-amino-adenine; an 8- azaguanine; an 8-azaadenine; a 7-deazaguanine; a 7-deazaadenine; a 3-deazaguanine; a 3- deazaadenine; a tricyclic pyrimidine; a phenoxazine cytidine; a phenothiazine cytidine; a substituted phenoxazine cytidine; a carbazole cytidine; a pyridoindole cytidine; a 7-deaza- adenine; a 7-deazaguanosine; a 2-aminopyridine; a 2-pyridone; a 5-substituted pyrimidine; a 6-azapyrimidine; an N-2, N-6 or O-6 substituted purine; a 2-aminopropyladenine; a 5- propynyluracil; or a 5-propynylcytosine. In some embodiments, the mRNA comprises a non-naturally occurring or a non-natural internucleoside linkage selected from the group of a phosphorothioate, a phosphoramidate, a non-phosphodiester, a heteroatom, a chiral phosphorothioate, a phosphorodithioate, a phosphotriester, an aminoalkylphosphotriester, a 3'-alkylene phosphonates, a 5'-alkylene phosphonate, a chiral phosphonate, a phosphinate, a 3'-amino phosphoramidate, an aminoalkylphosphoramidate, a phosphorodiamidate, a thionophosphoramidate, a thionoalkylphosphonate, a thionoalkylphosphotriester, a selenophosphate, or a boranophosphate. Provided herein are, inter alia, cells comprising a nucleic acid encoding an endolysin described herein. Cells include, but are not limited to eukaryotic and prokaryotic cells, such as strains of E. coli, Pseudomonas, Bacillus, Streptomyces, probiotic bacteria, fungi such as yeasts, and animal cells, such as CHO, R1.1, B—W and L-M cells, African Green Monkey kidney cells (e.g., COS 1, COS 7, BSC1, BSC40, and BMT10), insect cells (e.g., Sf9), and human cells and plant cells in tissue culture. In some embodiments, the cells express the endolysins described herein. In some embodiments, a method of identifying a phage endolysin specific for a microbial species is provided, the method comprising: contacting a sample comprising a microbial species and a phage with a DNA crosslinking reagent under conditions that allow crosslinking of DNA of the microbial species with DNA of the phage; digesting the crosslinked DNA with one or more restrictions enzymes, wherein the digesting produces crosslinked DNA molecules and results in free DNA ends on the crosslinked DNA molecules; ligating the free DNA ends with a ligase, thereby connecting the free DNA ends of the crosslinked DNA molecule; sequencing the ligated DNA; and analyzing the DNA sequences for the microbial species and the phage; thereby determining the microbial species and the phage present in the sample. Attorney Docket No.061817-503001WO In some embodiments, the method further comprises analyzing the DNA sequences to identify phage endolysins. In some embodiments, an endolysin identified by the methods of the disclosure is provided. In some embodiments, the endolysin identified by the methods of the disclosure is selected from Table 1A or Table 1B. Pharmaceutical Compositions The disclosure provides pharmaceutical compositions comprising the endolysins or the chimeric lysin of the disclosure and a pharmaceutically acceptable diluent, carrier or excipient. In some embodiments, the pharmaceutical composition is for use as a medicament in the treatment of a bacterial infection. In some embodiments, the bacterial infection is an infection of the skin. In some embodiments, the pharmaceutical composition comprises an effective amount of an isolated endolysin or the chimeric lysin of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of two or more isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of three or more isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of four or more isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of five or more isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of six or more isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of seven or more isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of eight or more isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of nine or more isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of 10 or more isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of at least 10 isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of at least 20 isolated Attorney Docket No.061817-503001WO endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of at least 30 isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of at least 40 isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of at least 50 isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of at least 60 isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of at least 70 isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of at least 80 isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of at least 90 isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of at least 100 isolated endolysins or the chimeric lysins of the disclosure. In some embodiments, the pharmaceutical composition comprises an effective amount of an isolated endolysin or a chimeric lysin comprising an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity to an endolysin sequence selected from the group consisting of an amino acid sequence of Table 1A or Table 1B, or an active fragment or a functional variant thereof. In some embodiments, the pharmaceutical composition comprises an effective amount of two or more isolated endolysins or the chimeric lysins comprising an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity to an endolysin sequence selected from the group consisting of an amino acid sequence of Table 1A or Table 1B, or an active fragment or a functional variant thereof. Such compositions may comprise buffers such as neutral buffered saline, phosphate buffered saline and the like; carbohydrates such as glucose, mannose, sucrose or dextrans, mannitol; proteins; polypeptides or amino acids such as glycine; antioxidants; chelating agents such as EDTA or glutathione; and preservatives. The pharmaceutical composition may be suitable for topical, nasal, inhaled, rectal, endoscopical, enteral, parenteral, or oral administration. Attorney Docket No.061817-503001WO Formulations of a pharmaceutical composition suitable for parenteral administration typically generally comprise the endolysins or the chimeric lysins of the disclosure combined with a pharmaceutically acceptable carrier, such as sterile water or sterile isotonic saline. Such formulations may be prepared, packaged, or sold in a form suitable for bolus administration or for continuous administration. Injectable formulations may be prepared, packaged, or sold in unit dosage form, such as in ampoules or in multi- dose containers containing a preservative. Formulations for parenteral administration include, but are not limited to, suspensions, solutions, emulsions in oily or aqueous vehicles, pastes, and the like. Such formulations may further comprise one or more additional ingredients including, but not limited to, suspending, stabilizing, or dispersing agents. Parenteral formulations also include aqueous solutions which may contain excipients such as salts, carbohydrates and buffering agents. Illustrative parenteral administration forms include solutions or suspensions in sterile aqueous solutions, for example, aqueous propylene glycol or dextrose solutions. Such dosage forms can be suitably buffered, if desired. Formulations for parenteral administration may be formulated to be immediate and / or modified release. Modified release formulations include delayed-, sustained-, pulsed-, controlled-, targeted and programmed release. In some embodiments, the formulated composition comprising the endolysin or the chimeric lysin is suitable for administration via injection. In some embodiments, the formulated composition comprising the endolysin or the chimeric lysin is suitable for administration via infusion. In some embodiments, the formulated composition comprising the endolysin or the chimeric lysin is suitable for administration via topical administration. In some embodiments, the formulated composition comprising the endolysin or the chimeric lysin is suitable for administration via a spray. In some embodiments, the formulated composition comprising the endolysin or the chimeric lysin is suitable for administration via inhalhation. In some embodiments, the formulated composition comprising the endolysin or the chimeric lysin is suitable for administration via rectal administration. In some embodiments, the formulated composition comprising the endolysin or the chimeric lysin is suitable for administration via an oral delivery. In some embodiments, the formulated composition comprising the endolysin or the chimeric lysin is suitable for topical, oral, intratracheobronchial, pulmonary, and / or nasal administration delivery. The pharmaceutical compositions of the present disclosure, which may conveniently be presented in unit dosage form, may be prepared according to conventional Attorney Docket No.061817-503001WO techniques well known in the pharmaceutical industry. Such techniques include the step of bringing into association the endolysin with the pharmaceutical carrier(s) or excipient(s), such as liquid carriers. Aqueous suspensions may further contain substances that increase the viscosity of the suspension including, for example, sodium carboxymethylcellulose, sorbitol and / or dextran. The suspension may also contain stabilizers. The compositions of the present disclosure may additionally contain other adjunct components conventionally found in pharmaceutical compositions. Thus, for example, the compositions may contain additional, compatible, pharmaceutically-active materials such as, for example, antipruritics, astringents, local anesthetics or anti-inflammatory agents, or may contain additional materials useful in physically formulating various dosage forms of the compositions of the present disclosure, such as dyes, preservatives, antioxidants, opacifiers, thickening agents and stabilizers. However, such materials, when added, should not unduly interfere with the biological activities of the endolysin of the compositions of the present disclosure. The formulation or composition may also contain more than one active ingredient useful for the particular indication, disease, or condition being treated with the endolysin, where the respective activities do not adversely affect one another. Such active ingredients are suitably present in combination in amounts that are effective for the purpose intended. Thus, in some embodiments, the pharmaceutical composition further includes other pharmaceutically active agents or drugs, such as antibiotic agents. The pharmaceutical composition in some aspects can employ time-released, delayed release, and sustained release delivery systems such that the delivery of the composition occurs prior to, and with sufficient time to cause, sensitization of the site to be treated. Many types of release delivery systems are available and known. Such systems can avoid repeated administrations of the composition, thereby increasing convenience to the subject and the physician. Administration can be effected in one dose, continuously or intermittently throughout the course of treatment. Single or multiple administrations can be carried out with the dose level and pattern being selected by the treating physician. The pharmaceutical composition in some embodiments contains the endolysin or the chimeric lysin in amounts effective to treat or prevent a bacterial infection, such as a therapeutically effective or prophylactically effective amount. Therapeutic or prophylactic efficacy in some embodiments is monitored by periodic assessment of treated subjects. For Attorney Docket No.061817-503001WO repeated administrations over days, weeks or months, depending on the condition, the treatment can be repeated until a desired suppression of bacterial infection signs or symptoms occurs. However, other dosage regimens may be useful and can be determined. The desired dosage can be delivered by a single bolus administration or infusion of the composition or by multiple bolus administrations or infusions of the composition. Methods for Producing Endolysin Polypeptides In an aspect, the disclosure includes methods for producing endolysin or the chimeric lysin polypeptides of the present disclosure. In some embodiments, endolysin polypeptides can be produced with methods for manufacturing proteins known in the art, for example by expression in a cell, cell free expression methods, or by chemical synthesis. In some embodiments, the method comprises culturing a host cell comprising an endolysin polynucleotide encoding one or more endolysin polypeptides under suitable conditions to express the said polypeptide. To obtain high level of endolysin polypeptide expression, endolysin polynucleotide sequences are typically expressed by operatively linking them to an expression control sequence in an appropriate expression vector and employing that expression vector to transform an appropriate cellular host. Such operative linking of a polynucleotide sequences encoding endolysin polypeptides of the present disclosure to an expression control sequence, includes, the provision of an initiation codon, ATG, in the correct reading frame upstream of the polynucleotide (DNA) sequence. Generally, any system or vector suitable to maintain, propagate or express polynucleotides and / or to express a polypeptide in a host may be used for expression of endolysin polypeptides. The appropriate DNA / polynucleotide sequence may be inserted into the expression system by any of a variety of well-known and routine techniques, such as, for example, those set forth in Sambrook et al., Molecular Cloning, A Laboratory Manual. Additionally, tags can also be added to endolysin polypeptides to provide convenient methods of isolation, e.g., c-myc, biotin, poly-His, etc. Kits for such expression systems are commercially available. A wide variety of host / expression vector combinations may be employed in expressing the polynucleotude sequences encoding endolysin polypeptides of the present disclosure. Large numbers of suitable vectors are known to those of skill in the art, and are commercially available. Examples of suitable vectors are provided in Sambrook et al, eds., Molecular Cloning: A Laboratory Manual (3rd Ed.), Vols.1-3, Cold Spring Harbor Attorney Docket No.061817-503001WO Laboratory (2001). Such vectors include, among others, chromosomal, episomal and virus-derived vectors, e.g., vectors derived from bacterial plasmids, from bacteriophage, from transposons, from yeast episomes, from insertion elements, from yeast chromosomal elements, from viruses such as baculoviruses, papova viruses, such as SV40, vaccinia viruses, adenoviruses, fowl pox viruses, pseudorabies viruses and retroviruses, and vectors derived from combinations thereof, such as those derived from plasmid and bacteriophage genetic elements, such as cosmids and phagemids. Furthermore, said vectors may provide for the constitutive or inducible expression of endolysin polypeptides of the present disclosure. More specifically, suitable vectors include but are not limited to derivatives of SV40 and known bacterial plasmids, e.g., E. coli plasmids colE1, pCR1, pBR322, pMB9 and their derivatives, plasmids such as RP4, pBAD24 and pBAD-TOPO; phage DNAS,A&C&$ NDA IOHALJOM @ALEP=NEPAM JB KD=CA W$ A&C&$ 76 / . / $ =I@ JNDAL KD=CA 370$ A&C&$ 6)+and filamentous single stranded phage DNA; yeast plasmids such as the 2 D plasmid or derivatives thereof; vectors useful in eukaryotic cells, such as vectors useful in insect or mammalian cells; vectors derived from combinations of plasmids and phage DNAs, such as plasmids that have been modified to employ phage DNA or other expression control sequences; and the like. Many of the vectors mentioned above are commercially available from vendors such as New England Biolabs, Addgene, Clontech, Life Technologies etc many of which also provide suitable host cells). Additionally, vectors may comprise various regulatory elements (including promoter, ribosome binding site, terminator, enhancer, various cis-elements for controlling the expression level) wherein the vector is constructed in accordance with the host cell. Any of a wide variety of expression control sequences (sequences that control the expression of a polynucleotide sequence operatively linked to it) may be used in these vectors to express the polynucleotide sequences encoding endolysin polypeptides. Useful control sequences include, but are not limited to: the early or late promoters of SV40, CMV, vaccinia, polyoma or adenovirus, the lac system, the trp system, the TAC system,NDA ;:2 MSMNAH$ NDA 5;: MSMNAH$ NDA H=FJL JKAL=NJL =I@ KLJHJNAL LACEJIM JB KD=CA W$ NDAcontrol regions of fd coat protein, the promoter for 3-phosphoglycerate kinase or other glycolytic enzymes, the promoters of acid phosphatase (e.g., Pho5), the promoters of the yeast-mating factors, E. coli promoter for expression in bacteria, and other promoter sequences known to control the expression of genes of prokaryotic or eukaryotic cells or their viruses, and various combinations thereof. Attorney Docket No.061817-503001WO A wide variety of host cells are useful in expressing the endolysin polypeptides of present disclosure. Nonlimiting examples of host cells suitable for expression of endolysin polypeptides of the present disclosure include well known eukaryotic and prokaryotic hosts, such as strains of E. coli, Pseudomonas, Bacillus, Streptomyces, fungi such as yeasts, and animal cells, such as CHO, R1.1, B—W and L-M cells, African Green Monkey kidney cells (e.g., COS 1, COS 7, BSC1, BSC40, and BMT10), insect cells (e.g., Sf9), and human cells and plant cells in tissue culture. While the expression host may be any known expression host cell, in a preferred embodiment the expression host is one of the strains of E. coli These include, but are not limited to commercially available E. coli strains such as Top10 (Thermo Fisher Scientific), DH5c (Thermo Fisher Scientific), XL1-Blue (Agilent Technologies), SCS110 (Stratagene), JM109 (Promega), LMG194 (ATCC), and BL21 (Thermo Fisher Scientific). There are several advantages of using E. coli as a host system including: fast growth kinetics, where under the optimal environmental conditions, its doubling time is about 20 min (Sezonov et al., J. Bacteriol. 1898746-8749 (2007)), easily achieved high density cultures, easy and fast transformation with exogenous DNA, etc. Details regarding protein expression in E. coli, including plasmid selection as well as strain selection are discussed in details by Rosano, G. and Ceccarelli, E., Front Microbiol., 5: 172 (2014). Efficient expression of endolysin polypeptides and vectors thereof depends on a variety of factors such as optimal expression signals (both at the level of transcription and translation), correct protein folding, and cell growth characteristics. Regarding methods for constructing the vector and methods for transducing the constructed recombinant vector into the host cell, conventional methods known in the art can be utilized. While it is understood that not all vectors, expression control sequences, and hosts will function equally well to express the polynucleotide sequences encoding endolysin peptides of the present disclosure, one skilled in the art will be able to select the proper vectors, expression control sequences, and hosts without undue experimentation to accomplish the desired expression without departing from the scope of this disclosure. In some embodiments, the present inventors have found a correlation between level of expression and activity of the expressed polypeptide; in E. coli expression systems in particular, moderate levels of expression (for example between about 1 and 10 mg / liter) have produced endolysin polypeptides with higher levels of activity than those that were expressed at higher levels in in E. coli (for example between about 20 and about 100 mg / liter), the latter having sometimes produced wholly inactive polypeptides. Attorney Docket No.061817-503001WO Endolysin or chimeric lysin polypeptides of the present disclosure can be recovered and purified from recombinant cell cultures by well-known methods including ammonium sulfate or ethanol precipitation, acid extraction, anion or cation exchange chromatography, phosphocellulose chromatography, hydrophobic interaction chromatography, affinity chromatography, hydroxylapatite chromatography, metal affinity chromatography (IMAC), and lectin chromatography. High performance liquid chromatography can also employed for endolysin polypeptide purification. In some embodiments, endolysin polypeptide is purified by nickel chromatography. Alternatively, the vector system used for the production of endolysin polypeptides of the present disclosure may be a cell free expression system. Various cell free expression systems are commercially available, including, but are not limited to those available from Promega, LifeTechnologies, Clonetech, etc. In some embodiments, the endolysin or the chimeric lysin is expressed in a probiotic bacteria. In some embodiments, the probiotic bacteria are a lactic acid bacteria. In some embodiments, the probiotic bacteria are a Lactobacillus or a Bifidobacterium. In some embodiments, the probiotic bacteria expressing the endolysin is located in or on a subject. Methods of Use Provided herein are methods of using the endolysins or chimeric lysins of the disclosure. In one aspect, a method for inhibiting the growth of a microbial species is provided, the method comprising contacting the microbial species with an endolysin specific for the microbial species selected from the endolysins and microbial species in Table 1A or Table 1B. In one aspect, a method killing a microbial species is provided, the method comprising contacting the microbial species with an endolysin specific for the microbial species selected from the endolysins and microbial species in Table 1A or Table 1B. In one aspect, a method for reducing the growth of a population of microbial species population is provided, the method comprising contacting the microbial species with an endolysin specific for the microbial species selected from the endolysins and microbial species in Table 1A or Table 1B. In one embodiment, the microbial species is a Gram-negative bacteria or a Gram- positive bacteria. Attorney Docket No.061817-503001WO In one aspect, a method of inhibiting the growth, or reducing the population is provided, or killing of at least one species of Gram-negative bacteria, the method comprising contacting the bacteria with a composition containing an effective amount of a endolysin comprising an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity to a endolysin sequence selected from the group consisting of an amino acid sequence of Table 1A or Table 1B, or active fragments thereof. In one aspect, a method of treating a bacterial infection caused by a Gram-negative bacteria is provided, comprising administering to a subject diagnosed with, at risk for, or exhibiting symptoms of a bacterial infection, a composition containing an effective amount of an endolysin comprising an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity to a endolysin sequence selected from Table 1A or Table 1B, or an active fragment thereof. In one aspect, a method of treating a bacterial infection caused by a Gram-positive bacteria is provided, comprising administering to a subject diagnosed with, at risk for, or exhibiting symptoms of a bacterial infection, a composition containing an effective amount of an endolysin comprising an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity to a endolysin sequence selected from Table 1A or Table 1B, or an active fragment thereof. In a further aspect, a method of inhibiting the growth, or reducing the population, or killing of at least one species of Gram-positive bacteria, the method comprising contacting the bacteria with a composition containing an effective amount of a chimeric endolysin comprising an enzymatic activity domain of a first endolysin sequence selected from Table 1A or Table 1B, and a cell wall binding domain of a second endolysin sequence selected from Table 1A or Table 1B, wherein the first and the second endolysins are different endolysin seqeuences is provided. In some embodiments, a method of inhibiting the growth, or reducing the population, or killing of at least one species of Gram-positive bacteria, the method comprising contacting the bacteria with a composition containing an effective amount of a chimeric endolysin comprising a first and a second enzymatic activity domain of a first and a second endolysin and a third cell-wall binding domain of a third endolysin, wherein the first, second and the third endolysins are selected from Table 1A or Table 1B is provided. Attorney Docket No.061817-503001WO In some embodiments, a method of inhibiting the growth, or reducing the population, or killing of at least one species of Gram-positive bacteria, the method comprising contacting the bacteria with a composition containing an effective amount of a chimeric endolysin comprising a first and a second cell wall binding domain of a first and a second endolysin and a third enzymatic activity domain of a third endolysin, wherein the first, second and the third endolysins are selected from Table 1A or Table 1B is provided. In a yet further aspect, a method of treating a bacterial infection caused by a Gram-negative bacteria, comprising administering to a subject diagnosed with, at risk for, or exhibiting symptoms of a bacterial infection, a composition containing an effective amount of an endolysin comprising a chimeric endolysin further comprising an enzymatic activity domain of a first endolysin sequence selected from Table 1A or Table 1B, and a cell-wall binding domain of a second endolysin sequence selected from Table 1A or Table 1B, wherein the first and the second endolysins are different endolysin seqeuences is provided. In some embodiments, a method of treating a bacterial infection caused by a Gram-negative bacteria, comprising administering to a subject diagnosed with, at risk for, or exhibiting symptoms of a bacterial infection, a composition containing an effective amount of an endolysin comprising a chimeric endolysin further comprising a first and a second enzymatic activity domain of a first and a second endolysin and a third cell-wall binding domain of a third endolysin, wherein the first, second and the third endolysins are selected from Table 1A or Table 1B is provided. In some embodiments, a method of treating a bacterial infection caused by a Gram-negative bacteria, comprising administering to a subject diagnosed with, at risk for, or exhibiting symptoms of a bacterial infection, a composition containing an effective amount of an endolysin comprising a chimeric endolysin further comprising a first and a second cell-wall binding domain of a first and a second endolysin and a third enzymatic activity domain of a third endolysin, wherein the first, second and the third endolysins are selected from Table 1A or Table 1B is provided. In one aspect, a method of treating a subject diagnosed with, at risk for, or exhibiting symptoms of a bacterial infection is provided, the method comprising, administering at least one endolysin of the disclosure, a nucleic acid of the disclosure, a vector of the disclosure, or a pharmaceutical composition of the disclosure to the subject. Attorney Docket No.061817-503001WO In one aspect, a method for inhibiting the growth of a microbial species is provided, the method comprising contacting the microbial species with a nucleic acid encoding an endolysin of the disclosure, a vector encoding an endolysin of the disclosure, or a cell expressing an endolysin of the disclosure. In some embodiments, the method additionally comprises administering an accessory protein, wherein the accessory protein enhances the activity of the endolysin or the chimeric lysin. In some embodiments, the accessory protein is a spanin, holin, or a lipopolysaccharide disruption protein. In some embodiments, the subject is a human. In some embodiments, the infection is an infection of the skin. In some embodiments, the composition is administered topically, nasally, inhaled, rectally, endoscopically, enterally, parenterally, or orally. In one aspect, a method for delivering an endolysin or the chimeric lysin selected from Table 1A or Table 1B to a patient in need thereof is provided, the method comprising administering an effective amount of the endolysin to the patient in need thereof. In some embodiments, the deliving comprises topical, oral, intratracheobronchial, pulmonary, and / or nasal administration delivery. In one aspect, a method of treating a bacterial infection caused by a microbial species is provided comprising co-administering to a subject diagnosed with, at risk for, or exhibiting symptoms of a bacterial infection, a composition containing an effective amount of a endolysin or the chimeric lysin specific for the microbial species selected from the endolysins and microbial species in Table 1A or Table 1B comprising an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity to a endolysin sequence selected from Table 1A or Table 1B, or an active fragment thereof and an antibiotic or bacteriostatic therapy. In one aspect, a method for reducing or inhibiting the colonization or growth of a microbial species on a surface is provided, comprising contacting said surface with an endolysin specific for the microbial species selected from the endolysins or the chimeric lysins, and microbial species in Table 1A or Table 1B. In one embodiment, the surface is the skin or a mucus membrane of a mammal. Inone embodiment, the surface is the surface of a hospital apparatus or a piece of hospitalequipment. In one embodiment, the apparatus or equipment is a surgical apparatus or pieceof surgical equipment. Attorney Docket No.061817-503001WO In one embodiment, the endolysin or the chimeric lysins is administered by delivering to the subject a probiotic bacteria expressing the endolysin. In one embodiment, the endolysin or the chimeric lysins is administered by delivering to the subject a mRNA encoding the endolysin or the chimeric lysins. In one embodiment, the mRNA is encapsulated in an LNP. The endolysins or the chimeric lysins of the present disclosure can be co- administered with standard care antibiotics or with antibiotics of last resort, individually or in various combinations as within the skill of the art.In one embodiment, the present disclosure relates to the prevention, reduction, treatment, or removal of Gram-negative or Gram-positive bacterial contamination of medical devices, surfaces such as floors, stairs, walls and countertops in hospitals and other health related or public use buildings and surfaces of equipment in operating rooms, emergency rooms, hospital rooms, clinics, and bathrooms and the like. Examples of medical devices that can be protected using compositions described herein include but are not limited to tubings and other surface medical devices, such as urinary catheters, mucous extraction catheters, suction catheters, umbilical cannulae, contact lenses, intrauterine devices, intravaginal and intraintestinal devices, endotracheal tubes, bronchoscopes, dental prostheses and orthodontic devices, surgical instruments, dental instruments, tubings, dental water lines, fabrics, paper, indicator strips (e.g., paper indicator strips or plastic indicator strips), adhesives (e.g., hydrogel adhesives, hot-melt adhesives, or solvent-based adhesives), bandages, tissue dressings or healing devices and occlusive patches, and any other surface devices used in the medical field. The devices may include electrodes, external prostheses, fixation tapes, compression bandages, and monitors of various types. Medical devices can also include any device which can be placed at the insertion or implantation site such as the skin near the insertion or implantation site, and which can include at least one surface which is susceptible to colonization by Gram-negative or Gram-positive bacteria. Antibiotics in clinical practice include several which commonly affect cell wall peptidoglycan biosynthesis in Gram positive bacteria. These include glycopeptides, which as a class inhibit peptidoglycan synthesis by preventing the incorporation of N- acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) peptide subunits into the peptidoglycan matrix. Available glycopeptides include vancomycin and teicoplanin, with vancomycin a primary drug of choice and clinical application in bacteremia, particularly Staphylococcal infections. Penicillins act by inhibiting the formation of peptidoglycan cross-links. Common penicillins include oxacillin, ampicillin and cloxacillin. Linezolid Attorney Docket No.061817-503001WO (Zyvox) is a protein synthesis inhibitor and in a class of antibacterials called oxazolidinones (Ford C W et al (1996) Antimicrob Agents Chemoth 40(6):1508-1513; Swaney S M et al (1998) Antimicrob Agents Chemoth 42(12):3251-3255; U.S. Pat. No. 6,444,813). In one embodiment, the endolysin or the chimeric lysin polypeptides of the present disclosure are used for preserving food against Gram-negative or Gram-positive bacterial contamination comprising adding to the food the compositions of the present disclosure comprising endolysin polypeptides. Examples of such food products are meat products (cured and / or uncured, fresh and / or cooked), salads and other vegetable products, drinks and dairy products, semi-processed foods, convenient foods as e.g., ready-to-eat meals and dried food products, etc. One of the problems that bacteria pose towards humans is the formation of biofilms. Biofilm formation occurs when microbial cells adhere to each other and are embedded in a matrix of extracellular polymeric substance (EPS) on a surface. The growth of microbes in such a protected environment that is enriched with biomacromolecules (e.g. polysaccharides, nucleic acids and proteins) and nutrients allow for enhanced microbial cross-talk and increased virulence. As biofilm may develop in any supporting environment, a method or composition that can prevent or remove biofilm formation is needed. Pseudomonas aeruginosa has been shown to form biofilms on a variety of living and non-living surfaces such as the mucus plugs of the CF lung, contaminated catheters, contact lenses, etc (Sharma et al. Biologicals, 42(1):1-7 (2014)). Thus, in one embodiment, the endolysin polypeptides of the present disclosure can be used for prevention, control, disruption, and treatment of a bacterial biofilm. EXAMPLES The following examples are put forth so as to provide those of ordinary skill in the art with a complete disclosure and description of how to make and use the methods and compositions featured in the invention, and are not intended to limit the scope of what the inventors regard as their invention. Efforts have been made to ensure accuracy with respect to numbers used (e.g., amounts, temperature, etc.) but some experimental errors and deviations should be accounted for. Unless indicated otherwise, parts are parts by weight, molecular weight is average molecular weight, temperature is in degrees Centigrade, and pressure is at or near atmospheric. Attorney Docket No.061817-503001WO Example 1: Methods for Endolysin Identification and Characterization This example describes the identification of phage-derived endolysins and the bacterial species that is targeted by the endolysin using proximity ligation metagenomics. Proximity ligation metagenomics allows the discovery of endolysins directly in their natural environment, and without isolating them or their hosts, even if the hosts are difficult / impossible to culture. A general method proximity ligation is described in Press et al., https: / / www.biorxiv.org / content / 10.1101 / 198713v1, which is incorporated by reference. This could be a specific strain, species, genus, family, order, class, or phylum or a combination of taxa from one or more lineages at one or more taxonomic ranks of microbial species. This could also be a specific genome in the Phase Genomics Database. These genomes could also be strains with known resistance genes (e.g., Enterococcus genomes with vancomycin-resistance = vancomycin-resistant enterococci). Briefly, the target microbial taxa of interest were selected and phage genome assemblies within a database that are associated with specified microbial taxa through Hi- C linkages. Methods for preparing an exemplary database are described in Uritskiy, Gherman, et al. "Accurate viral genome reconstruction and host assignment with proximity-ligation sequencing." BioRxiv (2021): 2021-06. Hi-C measures the frequency (as an average over a cell population) at which two DNA fragments physically associate in 3D space, linking chromosomal structure directly to the genomic sequence. Additional phage genome filtering steps can be performed. Information about the type of sample or environment from which a sample was obtained may be useful for candidate selection. Characteristics about the assigned target microbial genomes (e.g. completeness or AMR gene content) may also be used to filter candidate selection. For each phage genome, open reading frames were predicted using Prodigal-GV, an updated version of the widely accepted gene calling software Prodigal1 that has improved performance on gene calling in viruses. Predicted coding sequences were then annotated using homology based searches against two or more reference databases. The HMMER package2 was used to query the Prokaryotic Virus Remote Homologous Groups (PHROG) database3, a manually curated set of protein cluster Hidden Markov Model (HMM) profiles created from reference phage genomes. The rpsblast algorithm was used to query the Conserved Domain Database4 (CDD), which includes a curated set of full protein sequence and protein domain profiles derived from internal NCBI collections and external sources such as Pfam and TIGRFAMs. Domain annotation serves to confirm protein level annotations and also Attorney Docket No.061817-503001WO increase sensitivity for detecting endolysins that may not score above thresholds in whole protein alignment based queries, but may possess homologous catalytic or binding domains. Exemplary endolysin sequences and microbial target cells are listed in Table 1A or Table 1B. Annotation results were manually examined for significant alignments to endolysin genes and / or domains. Putative endolysin genes were selected for further phylogenetic analysis. First, a multiple sequence alignment (MSA) was created, for example by using muscle. Then a phylogenetic tree was constructed using FastTree or other appropriate software. Additional examination of candidate endolysin sequences can be performed using protein structure prediction. Using sequences identified, DNA constructs were synthesized on expression plasmids with purification tag (e.g., 6x His), proteins were expressed in E. coli expression strain or other appropriate platform, and the proteins were affinity purified. The recombinant endolysin activity was tested using a number of methods, including minimum inhibitory concentration, growth curves using optical density, spot plates, plaque assays, etc. Additional search strategy for identification of endolysins: Identify clusters of homologous phage genes using sequence clustering using the Linclust method in the Mmseqs2 package and / or phylogenetic analysis through multiple sequence alignment and tree building. Select clusters for profile construction. These may be large clusters without functional annotations, clusters with minimal annotation (only one or a fraction of genes were annotated using prior homology based approaches). Construct HMM profiles2 from cluster MSA. Perform profile-profile searches for high sensitivity of protein annotation and identification of more distant homologs. Phage-bacterial host pairs can be also identified by manual isolation of through plaque assays or similar. Phage-bacterial host pairs can be also identified by prediction of viral hosts from sequencing data of isolates or metagenomes: Phage Genome Analysis: Analyzing the genomic sequences of phages can provide insights into their potential hosts. Specific genes or motifs associated with host recognition, such as tail fiber proteins or receptor-binding proteins, can be identified. CRISPR-Cas Systems: Examining CRISPR spacer sequences in bacterial genomes can Attorney Docket No.061817-503001WO reveal historical interactions between bacteria and phages. Matching spacers with phage sequences can suggest potential host ranges. However, CRISPR spacer matches are more like a “memory” of past infection than an indication of present host range. Host Prediction Algorithms: Developing or utilizing machine learning algorithms trained on known phage- host interactions can help predict potential hosts for new phages based on genomic features. Some examples include VirHostMatcher, iPHoP, HostFinder, DeepHost, PHIAF, etc. Phage Receptor Prediction Models: Some models focus on predicting the receptors on bacterial surfaces that phages may target, aiding in the identification of potential hosts. Example 2: Determination of Lysin Activity on Bacteria This example described the determination of endolysin activity on Lactococcus and Enterococcus bacterial strains. Briefly, phages targeting Lactococcus sp. were identified in a database, and annotated endolysin protein sequences (SEQ ID NOs: 311 and 313) were produced as codon-optimized nucleotide sequences in pET-29b(+) plasmid vectors. Previously published sequences LysP008, Lysc2, and Lys1358 were produced in the same method, as positive controls (see for example Oechslin, Frank, et al. "Phage endolysins are adapted to specific hosts and are evolutionarily dynamic." PLoS biology 20.8 (2022): e3001740. Lysin proteins and control proteins were expressed and purified from E. coli strain BL21 / DE3 was transformed with plasmid a plasmid encoding the endolysin or a control. Lysins were tested for antibacterial activity on spot tests. Briefly, endolysin activity against L. cremoris was tested in a spot test.10 µL of endolysin and control protein eluate from protein purification was spotted directly on a lawn of Lactococcus cremoris and cultured overnight on MRS medium. The results show, that the endolysins with the sequences SEQ ID NOs: 311 and 313 have antibacterial activity against Lactococcus cremoris. Lysins were tested for growth inhibition and / or lysis of L. cremoris by endolysin C2-NP. Overnight Lactococcus cremoris sub-cultured 1:4 in 250 µL fresh MRS medium until OD600 = approx.0.35.25 µL of purified endolysin C2-NP, or negative control elution buffer was added and cells were incubated at 37ºC for 5 hours. The results show, that the endolysins has antibacterial activity against Lactococcus cremoris. Next, lysin activity of purified lysin PGL_0260 from a scaled production was checked in spot test on lawns of different clinical isolates of E. faecium. Exemplary PGL- 0260 lysin set forth by SEQ ID NO: 260 was produced as codon-optimized nucleotide Attorney Docket No.061817-503001WO sequences in pET-29b(+) plasmid vector. An E. coli strain BL21 / DE3 was transformed with the plasmid encoding the endolysin. The endolysin was subsequently purified by Nickel Chromatography. FIG.2A shows that E. coli expressing Enc-01-HIS lysin is found in both soluble and insoluble pellet fractions of E. coli lysates. FIG.2B shows that purified PGL_0260 forms stable dimers and trimers as observed for other lysins. To test the activity of the purified lysin on E. faecium, a bacterial lawn was prepared by mixing 250 µl of overnight E. faecium culture from different clinical isolates with 3 ml of 0.7% melted agar and pouring the mixture on top of BHI nutirent plate. Similarly, bacterial lawns were prepared for vancomycin resistant (vanR) or multidrug resistant (MDR) E. faecium. The resulting plates were dried at room temperature with?GJMA@ GE@ BJL +( HEI& 0 @LJK JB )( TG JB NDA GSMEI 945<(*-( "(&*, IC'XG# Q=M KEKANNA@?=LABOGGS JI NDA @LEA@ >=?NALE=G G=QI& ;DA M=HA Q=S$ P=I?JHS?EI "+(( IC'XG#$ IJI%transformed BL21 lysate, or water were spotted on the lawn as controls. The plates were incubated at 37oC overnight. The appearance of cleared zones in the spotted area against the turbid bacterial lawn indicated the successful lytic activity. As shown in FIG.2C, all strains regardless of characterized vancomycin or multidrug (including vancomycin) resistance demonstrated clearing when treated with the endolysin. While some variability in vancomycin sensitivity was observed, this is common at high concentrations. The results show that scaled and purified endolysins of the disclosure have antibacterial activity against Enterococcus feacium. Example 3: Retention of Lysin Activity Under Different Conditions This example describes the activity of an endolysin of the disclosure against E. faecium under different physiological conditions as determined in a turbidity reduction test. Turbidimetric determination is a method to analyze trends in bacterial growth using a spectrophotometer to track changes in the optical density (OD) at 600nm over time. Briefly, E. faecium cell pellets were collected from 150 µl overnight culture by centrifugation at 5,000 x g for 5 minutes. The pellet was resuspended in 300 µl of the treated lysin mixtures. The OD600 of the resuspended pellets were monitored with spectrophotometer for 15 minutes. A reduction in OD600confirms the lytic activity of the lysin. To test retention of lysin activity of PGL_0260 in human serum, purified Enc-01 was mixed with human serum (Sigma Millipore) to a final concentration of 12 ng / µl in 90% serum. The resulting serum-lysin mixture was incubated at room temperature and Attorney Docket No.061817-503001WO collected at 0 hr, 1 hr and 19 hr time points. The 0h OD600 was measured for each time point of incubation. The serum-lysin mixture was then additionally incubated in serum containing E. faecium for 15 minutes, which was determined as the experimental end- point. FIG. 3 demonstrates that Enc-01 retains its activity against E. faecium in human serum. Next, lysin activity of PGL_0260 lysin was evaluated at different pH levels. PGL_0260 lysin was diluted at a final concentration of 8 ng / µl in 100 mM of sodium phosphate buffers (Thermo Scientific) of different pH, such as, 4.4, 6.5, 7.0, 8.0 and 9.5. This mixture was incubated at room temperature for 15 min and then was tested for its activity against E. faecium in a turbidity reduction test as described above. As shown in FIGs.4A and 4B, Enc-01 retains its activity against at a range of pH levels tested. Finally, lysin activity of PGL_0260 lysin was tested against E. faecium in PBS at different concentrations. PGL_0260 lysin was diluted at a final concentrations of 0, 0.5, 1, 2, 4, 8, 16, or 32 µg / ml and was added to E. faecium culture in PBS. The 0h OD600 was measured for each concentration. OD600 was monitored every 15 minutes for 1h. FIG.5 shows that increasing doses of PGL_0260 caused a dose-dependent decrease in OD600. In sum, these results show that endolysins has antibacterial activity against Enterococcus faecium across different physiological and environmental conditions. Example 4: Determination of Activity of a Chimeric Lysin This example describes lysin activity of a chimeric lysin produced synthetically by domain-switching of the enzymatically active domains (EAD) and the cell wall-binding domains (CBD) from two independent lysins of the disclosure. The goal of this study is to evaluate the extension the spectrum of lysin targets. In this study, two chimeric lysins were generated by domain-switching and thus comprised either the EAD and CBD from PGL_0260 or PGL_0314 lysin. Table 3 provides Conserved Domain Database (CDD) annotations for the domains for the exemplary chimeric lysins. Specifically, Lysin CHI_0314_0260 contains binding domain from PGL_0260 and catalytic domain from PGL_0314. Lysin CHI_0260_0314 contains binding domain from PGL_0314 and catalytic domain from PGL_0260. FIG.6A shows the predicted structures of lysins identified in the Phase Genomic database (PGL_0260 and PGL_0314) and chimeras exchanging EADs and CBDs. FIG.6B demonstrates that these chimeric lysins can be produced and purified from E. coli as previously described in Example 2. Attorney Docket No.061817-503001WO Spectrum testing of chimeric lysins including vancomycin and elution buffer (negative control) as positive and negative control was performed using spot testing as described previously in Example 2. FIG.6C shows that the chimeric lysin CHI_0314_0260 exhibited killing activity against S. aureus where the native proteins PGL_0260 or PGL_0314 did not. In sum, results from this study show that chimeric lysins generated by domain-swapping of EAD and CBD of the lysins of the disclosure facilitates the expansion of spectrum of target bacterial species. Table 3: Conserved Domain Database (CDD) Annotations for the Exemplary Chimeric Lysins REFERENCES 1. Hyatt, D. et al. Prodigal: prokaryotic gene recognition and translation initiation site identification. BMC Bioinformatics 11, 119 (2010). 2. Eddy, S. R. Accelerated Profile HMM Searches. PLOS Comput. Biol.7, e1002195 (2011). 3. Terzian, P. et al. PHROG: families of prokaryotic virus proteins clustered using remote homology. NAR Genomics Bioinforma.3, lqab067 (2021). 4. Yang, M., Derbyshire, M. K., Yamashita, R. A. & Marchler-Bauer, A. NCBI’s Conserved Domain Database and Tools for Protein Domain Analysis. Curr. Protoc. Bioinforma.69, e90 (2020). 5. Mistry, J. et al. Pfam: The protein families database in 2021. Nucleic Acids Res. 49, D412–D419 (2020). 6. Haft, D. H. et al. TIGRFAMs: a protein family resource for the functional identification of proteins. Nucleic Acids Res.29, 41–43 (2001). 7. Edgar, R. C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792–1797 (2004). 8. Price, M. N., Dehal, P. S. & Arkin, A. P. FastTree 2 – Approximately Maximum- Likelihood Trees for Large Alignments. PLOS ONE 5, e9490 (2010). 9. Steinegger, M. & Söding, J. Clustering huge protein sequence sets in linear time. Nat. Commun.9, 2542 (2018). Attorney Docket No.061817-503001WO 10. Steinegger, M. & Söding, J. MMseqs2 enables sensitive protein sequence searching for the analysis of massive data sets. Nat. Biotechnol.35, 1026–1028 (2017). 11. Steinegger, M. et al. HH-suite3 for fast remote homology detection and deep protein annotation. BMC Bioinformatics 20, 473 (2019). 12. Remmert, M., Biegert, A., Hauser, A. & Söding, J. HHblits: lightning-fast iterative protein sequence searching by HMM-HMM alignment. Nat. Methods 9, 173–175 (2012). 13. Söding, J. Protein homology detection by HMM–HMM comparison. Bioinformatics 21, 951–960 (2005). EQUIVALENTS The invention may be embodied in other specific forms without departing from the spirit or essential characteristics thereof. The foregoing embodiments are therefore to be considered in all respects illustrative rather than limiting on the invention described herein. The scope of the invention is thus indicated by the appended claims rather than by the foregoing description, and all changes that come within the meaning and range of equivalency of the claims are intended to be embraced therein.

Claims

Attorney Docket No.061817-503001WO CLAIMS What is claimed is:

1. A method for inhibiting the growth of a microbial species, the methodcomprising contacting the microbial species with an endolysin specific for the microbial species selected from the endolysins and microbial species in Table 1A or Table 1B.

2. A method killing a microbial species, the method comprising contacting themicrobial species with an endolysin specific for the microbial species selected from the endolysins and microbial species in Table 1A or Table 1B.

3. A method for reducing the growth of a population of microbial speciespopulation, the method comprising contacting the microbial species with an endolysin specific for the microbial species selected from the endolysins and microbial species in Table 1A or Table 1B.

4. The method of any one of claims 1-3, wherein the microbial species is aGram-negative bacteria or a Gram-positive bacteria.

5. A method of inhibiting the growth, or reducing the population, or killing ofat least one species of Gram-negative bacteria, the method comprising contacting the bacteria with a composition containing an effective amount of an endolysin comprising an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity to an endolysin sequence selected from the group consisting of an amino acid sequence of Table 1A or Table 1B, or active fragments thereof.

6. A method of inhibiting the growth, or reducing the population, or killing ofat least one species of Gram-positive bacteria, the method comprising contacting the bacteria with a composition containing an effective amount of an endolysin comprising an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity to an endolysin sequence selected from Table 1A or Table 1B, or active fragments thereof.

7. A method of treating a bacterial infection caused by a Gram-negativebacteria, comprising administering to a subject diagnosed with, at risk for, or exhibiting symptoms of a bacterial infection, a composition containing an effective amount of an endolysin comprising an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95%Attorney Docket No.061817-503001WO identity to an endolysin sequence selected from Table 1A or Table 1B, or an active fragment thereof.

8. A method of treating a bacterial infection caused by a Gram-positivebacteria, comprising administering to a subject diagnosed with, at risk for, or exhibiting symptoms of a bacterial infection, a composition containing an effective amount of an endolysin comprising an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity to an endolysin sequence selected from Table 1A or Table 1B, or an active fragment thereof.

9. A method of inhibiting the growth, or reducing the population, or killing ofat least one species of Gram-positive bacteria, the method comprising contacting the bacteria with a composition containing an effective amount of a chimeric endolysin comprising an N-terminal enzymatic activity domain of a first endolysin sequence selected from Table 1A or Table 1B, and a C-terminal cell wall binding domain of a second endolysin sequence selected from Table 1A or Table 1B, wherein the first and the second endolysins are different endolysin seqeuences.

10. A method of treating a bacterial infection caused by a Gram-negativebacteria, comprising administering to a subject diagnosed with, at risk for, or exhibiting symptoms of a bacterial infection, a composition containing an effective amount of an endolysin comprising a chimeric endolysin further comprising an N-terminal enzymatic activity domain of a first endolysin sequence selected from Table 1A or Table 1B, and a C-terminal cell wall binding domain of a second endolysin sequence selected from Table 1A or Table 1B, wherein the first and the second endolysins are different endolysin seqeuences.

11. The method of any one of claims 4-10, wherein the Gram-negative bacteriaor the Gram-positive bacteria is present in a biofilm.

12. The method of any one of claim 11, wherein the biofilm is present on asubject or a device.

13. An isolated and / or recombinant endolysin selected from Table 1A orTable 1B, or a functional variant thereof, optionally having an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity thereto.Attorney Docket No.061817-503001WO14. An isolated and / or recombinant chimeric endolysin comprising an N-terminal enzymatic activity domain of a first endolysin sequence selected from Table 1A or Table 1B, and a C-terminal cell wall binding domain of a second endolysin sequence selected from Table 1A or Table 1B, wherein the first and the second endolysins are different endolysin seqeuences.

15. The endolysin of claim 13 or claim 14, wherein the endolysin is a chimericendolysin.

16. The endolysin of claim 13 or claim 14, where the endolysin is virionassociated.

17. The endolysin of claim 13 or claim 14, wherein the endolysin is cysteinemodified.

18. The endolysin of claim 13 or claim 14, wherein the endolysin is proteaseresistant.

19. The endolysin of claim 13 or claim 14, wherein the endolysin is modifiedto reduce immunogenicity.

20. A fusion protein comprising the endolysin of any one of claims 13-19.

21. The fusion protein of claim 20, wherein the endolysin is fused with abacteriocin.

22. A nucleic acid encoding an endolysin selected from Table 1A or Table1B, or a functional variant thereof, optionally having an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity thereto; or encoding the endolysin of any one of claims 14-19 or the fusion protein of claim 20 or 2123. The nucleic acid of claim 22, wherein the nucleic acid is DNA or RNA.

24. The RNA of claim 23, wherein the RNA is a mRNA.

25. A vector comprising a nucleic acid encoding an endolysin selected fromTable 1A or Table 1B, or a functional variant thereof, optionally having an amino acid sequence having at least 80%, or at least 85%, or at least 90%, or at least 95% identity thereto; or a nucleic encoding the endolysin of any one of claims 13-19 or the fusion protein of claim 20 or 21.

26. A cell comprising a nucleic acid encoding an endolysin selected fromTable 1A or Table 1B, or a functional variant thereof; or a chimeric endolysin comprising an N-terminal enzymatic activity domain of a first endolysin sequence selected from Table 1A or Table 1B, and a C-terminalAttorney Docket No.061817-503001WO cell wall binding domain of a second endolysin sequence selected from Table 1A or Table 1B, wherein the first and the second endolysin sequences are different endolysin sequences, or encoding the endolysin of any one of claims 13-19 or the fusion protein of claim 20 or 21.

27. A pharmaceutical composition comprising an effective amount of theendolysin of any one of claims 13-19 or the fusion protein of claim 20 or 21.

28. A method for inhibiting the growth of a microbial species, the methodcomprising contacting the microbial species with the nucleic acid of any one of claims 22-24, the vector of claim 25, or the cell of claim 26.

29. A method of treating a subject diagnosed with, at risk for, or exhibitingsymptoms of a bacterial infection, the method comprising, administering at least one endolysin of claim 14, nucleic acid of claim 22, vector of claim 24, or the pharmaceutical composition of claim 26 to the subject.

30. The method of claim 28 or 29, additionally comprising administering anaccessory protein, wherein the accessory protein enhances the activity of the endolysin.

31. The method of claim 30, wherein accessory protein is a spanin, holin, or alipopolysaccharide disruption protein.

32. The method of claim 29, wherein the subject is a human.

33. The method of claim 29, wherein the infection is an infection of the skin.

34. The method of claim 29, wherein the composition is administered topically,nasally, inhaled, rectally, endoscopically, enterally, parenterally, or orally.

35. A method for delivering an endolysin of claim 13 or claim 14 to a patient inneed thereof, the method comprising administering an effective amount of the endolysin to the patient in need thereof.

36. The method of claim 35, wherein the deliving comprises topical, oral,intratracheobronchial, pulmonary, and / or nasal administration delivery.

37. A method of treating a bacterial infection caused by a microbial speciescomprising co-administering to a subject diagnosed with, at risk for, or exhibiting symptoms of a bacterial infection, a composition containing an effective amount of a endolysin of claim 13 or claim 14 specific for the microbial species in Table 1A or Table 1B comprising an amino acidsequence having at least 80%, or at least 85%, or at least 90%, or at leastAttorney Docket No.061817-503001WO 95% identity to a endolysin sequence selected from Table 1A or Table 1B, or an active fragment thereof and an antibiotic or bacteriostatic therapy.

38. The method of any one of claims 28-31, wherein the endolysin is expressedin a probiotic bacteria.

39. A method for reducing or inhibiting the colonization or growth of amicrobial species on a surface comprising contacting said surface with an endolysin specific for the microbial species selected from the endolysins of claim 13 or claim 14 and microbial species in Table 1A or Table 1B.

40. The method of claim 39, wherein the surface is the skin or a mucusmembrane of a mammal.

41. The method of claim 39, wherein said surface is the surface of a hospitalapparatus or a piece of hospital equipment.

42. The method of claim 41, wherein said apparatus or equipment is a surgicalapparatus or piece of surgical equipment.

43. A method of identifying a phage endolysin specific for a microbial species,the method comprising: contacting a sample comprising a microbial species and a phage with a DNA crosslinking reagent under conditions that allow crosslinking of DNA of the microbial species with DNA of the phage; digesting the crosslinked DNA with one or more restrictions enzymes, wherein the digesting produces crosslinked DNA molecules and results in free DNA ends on the crosslinked DNA molecules; ligating the free DNA ends with a ligase, thereby connecting the free DNA ends of the crosslinked DNA molecule; sequencing the ligated DNA; and analyzing the DNA sequences for the microbial species and the phage; thereby determining the microbial species and the phage present in the sample.

44. The method of claim 43, the method further comprising analyzing the DNAsequences to identify phage endolysins.

45. An endolysin discovered by the method of claim 44.

46. The endolysin of claim 45, wherein the endolysin is selected from Table1A or Table 1B.Attorney Docket No.061817-503001WO47. The endolysin of claim 45, wherein the endolysin is a chimeric endolysincomprising an N-terminal enzymatic activity domain of a first endolysin sequence selected from Table 1A or Table 1B, and a C-terminal cell wall binding domain of a second endolysin sequence selected from Table 1A or Table 1B, wherein the first and the second endolysin sequences are different endolysin sequences.

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