Bacteriophage infecting s. hominis

Abstract

The present invention relates to a method and a composition for the prevention or treatment of malodour, specifically body malodour. Specifically, the invention relates to a novel S. hominis lytic bacteriophages or lytic bacteriophage-derived endolysins. The invention further relates to compositions for targeting body malodour.

Description

[0001]Bacteriophage infecting S. hominis Field of Invention The present invention relates to a method and a composition for the prevention or treatment of malodour, specifically body malodour. Specifically, the invention relates to a novel S. hominis bacteriophage and phage-derived endolysins. The invention further relates to compositions for targeting body malodour. Background of Invention Human body malodour is produced, amongst other regions, in the axilla. The odour is the result of bacterial transformation of naturally secreted non-odorous molecules, typically found in sweat, into a number of chemicals, including thioalcohols. Thioalcohols have a noticeable odour. Specifically in the underarm (axilla), malodour arises due to biotransformation by the microbiota of dipeptide-conjugated thioalcohols, particularly S-[1-(2-hydroxyethyl)-1- methylbutyl]-(L)-cysteinylglycine (Cys-Gly-3M3SH), which is transformed into themalodorous thioalcohol 3-methyl-3-sulfanylhexan-1-ol (3M3SH). Staphylococcus hominis, Staphylococcus haemolyticus and Staphylococcus lugdunensis are particularly efficient Cys-Gly-3M3SH transformers (as detailed in Bawdon et. al., 2015, FEMS Microbiol. Lett., 362(16), 2015, fnv 111). These bacterial species possess the C-S β-lyase enzyme, which is responsible for the conversion of Cys-Gly-3M3SH to 3M3SH. Staphylococcus hominis (S. hominis), is one of the most common commensal organisms colonising the human axilla. It has been established that there is a significant positive correlation between the body malodour intensity and the relative abundance of S. hominis (as detailed in Lam et al., 2018, Microbiome, 6(1):213). Body malodour has a strong social and psychological impact on affected subjects. There is, therefore, a need to reduce the body malodour produced by compounds found on the surface of the human body. WO 2018 / 065279 discloses a method of reducing malodour on the surface of the human body comprising the application of an inhibitor of peptide EEK12089 in its function as a transporter of a precursor of the thiol 3-methyl-3-sulfanylhexan-1-ol (3M3SH). Another solution to address the issue is to preferentially target S. hominis bacteria in the axilla, so as to prevent and treat body malodour. Bacteriophages (phages) are viruses that infect and replicate within bacteria. Phages are thought to exist for all species of bacteria, and they infect either a single bacterial species, or sub-sets of strains within a species. Their use to treat bacterial infection has been known for years. The life cycle of bacteriophages is normally either a lytic or lysogenic cycle. Lytic phages infect their hosts, before immediately replicating and lysing the cell wall, resulting in death of the host cell. In contrast, temperate phages, infect their host, before integrating the viral DNA into the host genome. The viral DNA is then replicated along with the host DNA. The virus typically remains dormant until host conditions deteriorate, at which point the endogenous phages (known as prophages) become active and initiate the reproduction cycle, resulting in lysis of the host cell. Bacteriophages have shown great potential as novel antimicrobials. Phage therapy, the use of phages or phage-encoded lytic enzymes (endolysins) to treat bacterial diseases, have been shown to be a useful method of targeting bacteria in a number of persistent bacterial infections. WO 2020 / 207884 discloses an antimicrobial composition for specifically targeting S. hominis bacteria comprising S. hominis phage-derived endolysins or nucleic acid molecules encoding the same. The document discloses the use of bacteriophage derived endolysin isolated from the STB12 temperate bacteriophage. It would be advantageous to provide an alternative method of targeting bacteria in the axilla, such as Staphylococcus hominis (S. hominis) to prevent and treat body malodour. Summary of Invention The inventors have determined a method of preventing and treating body malodour by using lytic bacteriophages or lytic bacteriophage-derived endolysins to target and lyse bacteria in the axilla, such as Staphylococcus hominis (S. hominis), S. lugdunesis and / or S. haemolyticus. According to a first aspect of the present invention, there is provided a bacteriophage lytic for at least multiple strains of S. hominis, wherein the bacteriophage comprises a genome that has at least 70% sequence identity with a sequence as set forth in SEQ ID NO: 1. Optionally, the bacteriophage of the first aspect of the present invention may comprise a genome that has at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with a sequence as set forth in SEQ ID NO: 1. Optionally, the bacteriophage is a lytic bacteriophage. Optionally, the bacteriophage of the first aspect of the present invention may comprise at least one open reading frame encoding an endolysin. Optionally, the bacteriophage of the first aspect of the present invention may comprise at least two open reading frames, wherein each open reading frame encodes an endolysin. Suitably, there is provided a nucleic acid sequence capable of encoding a first and second endolysin, designated herein as endolysins, 1 (shown in bold) and 2 (shown in underline), the nucleic acid sequence set comprising: acgataacgtagaatcagatagtaagcctgagtcagaaaaatcagataaccctaaagggtaaaatggagtggatatgaatggt aaaatattctgaatattggaatggtgttcctgtacgttttgatttattacctttcggtacaagacgttatggacaaaaattaaga aaaggtaagcctgaatttttagtagcacatgatacaggtaatatcaatacaactgctcaaaataacattgattattatagaa atacttataatattgcttgggattatgtagcaagtgcacatatctttgttgatgataaagaatgtgtaatttgtattcctgctaac gaagtggcttggcatgtactattaaatgctactttagataacttatggtatggtgttgacgctaactatggtgcagttggagtt gaaggttgttactttgaaaatagagaacgaactaaaaaatctttagataatatggctcgtgtattagcttatctatgtgattac tggaaaattgattacaaaacacaaatgcctggacatcaagacattcaagctaataaacaagacccaggtaatatcttagc ttatgctggttacggtcgtgctactagtaacttagataaattagtaggtaaatatgtaggaaaatctacaactaaaccagta agtaaatctaaagaaactaagactgttactgaaacagcaaaagcaggacaaattaccccacaagctaaacatactaaa ccaaaaactacttggaactggtctggtgtgttctatcctaatacaactattaaggtacgtaaatcaccaggattaaaaggtg cagtagtggatagaaattcttggttatacaataagaatgactgggttaaatttgaccaagttattaaaaaagacggttattg gtggattcgatttaaatatcaagcacctggctctagtaaagaccatttctattgtgcagtatgtaaaatgactgataaaaaa ggtcgtattaaagcagaaaaatattggggtcgtattgactggaaataagattgggggtatactaaatgtatgctaaattaactc gaagtgagtttttatctgtattaaatcaatctgttggtagaaaatatgacatggataactatgcaggatttcaatgctttgactacgctaa ctatggttggaataaattatttggttataatttagctggtaatggtgctaaagatattccaagtcctaaatggaataactttacaggaaa agctactgtatataaaaatacacctagctttttaccagaacctggtgaccttgttgtttggggtagtcaaatgggtaacggttggggtc acgttgcttgggtagttagtgctacacttaatcagattgttgttatcgaacagaactggttgggtggtggctggactactggtgacgctt atcatgcatggggttgggaatgtgctacaagacgtgtacattcttataacaaccctatgtggttcattagacctaactttaaaccagaa aaaccccaaccaaaaacaacttggaattggtctggagtgtttactgctaactctactatcaaagtacgtgttaaacctggattaaga ggtagagtagtagataaaggttcatggatatacgaaaaccaatgggttaaatttgtaagtatcactaagaaagatggttattggtgg ggtaaatttaaatatccaactaatccatcaagtggatatttctacatggctcttggtgagattacagataaaaaaggtcgtatcaaaa aagagaaaaaattatatggtcgtattaaatggttataacattttagactagg (SEQ ID NO: 6) or a variant or fragment thereof, wherein the fragment encodes an amino acid with endolysin activity. Optionally, there is provided a nucleic acid comprising at least 70%, at least 75%, at least 80%, at least 85%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity as set forth by SEQ ID NO: 6. Optionally, the bacteriophage or nucleic acid as set forth by SEQ ID NO: 6 or which has sequence identity of at least 70% to that nucleic acid sequence set forth by SEQ ID NO: 1 or SEQ ID NO: 6 is lytic for S. hominis, S. epidermidis and S. lugdunensis. Suitably, there is provided a nucleic acid comprising a nucleic acid sequence encoding an endolysin, designated herein as endolysin 1, or a nucleic acid sequence that has at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with a nucleic acid sequence set forth in: acgataacgtagaatcagatagtaagcctgagtcagaaaaatcagataaccctaaagggtaaaatggagtggatat gaatggtaaaatattctgaatattggaatggtgttcctgtacgttttgatttattacctttcggtacaagacgttatggacaaa aattaagaaaaggtaagcctgaatttttagtagcacatgatacaggtaatatcaatacaactgctcaaaataacattga ttattatagaaatacttataatattgcttgggattatgtagcaagtgcacatatctttgttgatgataaagaatgtgtaatttgt attcctgctaacgaagtggcttggcatgtactattaaatgctactttagataacttatggtatggtgttgacgctaactatgg tgcagttggagttgaaggttgttactttgaaaatagagaacgaactaaaaaatctttagataatatggctcgtgtattagc ttatctatgtgattactggaaaattgattacaaaacacaaatgcctggacatcaagacattcaagctaataaacaagac ccaggtaatatcttagcttatgctggttacggtcgtgctactagtaacttagataaattagtaggtaaatatgtaggaaaat ctacaactaaaccagtaagtaaatctaaagaaactaagactgttactgaaacagcaaaagcaggacaaattaccc cacaagctaaacatactaaaccaaaaactacttggaactggtctggtgtgttctatcctaatacaactattaaggtacgt aaatcaccaggattaaaaggtgcagtagtggatagaaattcttggttatacaataagaatgactgggttaaatttgacc aagttattaaaaaagacggttattggtggattcgatttaaatatcaagcacctggctctagtaaagaccatttctattgtgc agtatgtaaaatgactgataaaaaaggtcgtattaaagcagaaaaatattggggtcgtattgactggaaataa (SEQ ID NO: 4), or a fragment thereof which is functionally active as an endolysin. Suitably, there is provided a nucleic acid comprising a nucleic acid sequence encoding an endolysin, designated herein as endolysin 1, having a nucleic acid sequence: atggtaaaatattctgaatattggaatggtgttcctgtacgttttgatttattacctttcggtacaagacgttatggacaaaaa ttaagaaaaggtaagcctgaatttttagtagcacatgatacaggtaatatcaatacaactgctcaaaataacattgatta ttatagaaatacttataatattgcttgggattatgtagcaagtgcacatatctttgttgatgataaagaatgtgtaatttgtatt cctgctaacgaagtggcttggcatgtactattaaatgctactttagataacttatggtatggtgttgacgctaactatggtgc agttggagttgaaggttgttactttgaaaatagagaacgaactaaaaaatctttagataatatggctcgtgtattagcttat ctatgtgattactggaaaattgattacaaaacacaaatgcctggacatcaagacattcaagctaataaacaagaccc aggtaatatcttagcttatgctggttacggtcgtgctactagtaacttagataaattagtaggtaaatatgtaggaaaatct acaactaaaccagtaagtaaatctaaagaaactaagactgttactgaaacagcaaaagcaggacaaattacccca caagctaaacatactaaaccaaaaactacttggaactggtctggtgtgttctatcctaatacaactattaaggtacgtaa atcaccaggattaaaaggtgcagtagtggatagaaattcttggttatacaataagaatgactgggttaaatttgaccaa gttattaaaaaagacggttattggtggattcgatttaaatatcaagcacctggctctagtaaagaccatttctattgtgcag tatgtaaaatgactgataaaaaaggtcgtattaaagcagaaaaatattggggtcgtattgactggaaataa (SEQ ID NO: 7 (fragment of SEQ ID NO: 4)), or a fragment thereof which is functionally active as an endolysin. Suitably there is provided a nucleic acid comprising a nucleic acid sequence encoding an endolysin, designated herein as endolysin 2, or a nucleic acid with a nucleic acid sequence that has at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with: gattgggggtatactaaatgtatgctaaattaactcgaagtgagtttttatctgtattaaatcaatctgttggtagaaaatat gacatggataactatgcaggatttcaatgctttgactacgctaactatggttggaataaattatttggttataatttagctggt aatggtgctaaagatattccaagtcctaaatggaataactttacaggaaaagctactgtatataaaaatacacctagct ttttaccagaacctggtgaccttgttgtttggggtagtcaaatgggtaacggttggggtcacgttgcttgggtagttagtgct acacttaatcagattgttgttatcgaacagaactggttgggtggtggctggactactggtgacgcttatcatgcatggggt tgggaatgtgctacaagacgtgtacattcttataacaaccctatgtggttcattagacctaactttaaaccagaaaaacc ccaaccaaaaacaacttggaattggtctggagtgtttactgctaactctactatcaaagtacgtgttaaacctggattaa gaggtagagtagtagataaaggttcatggatatacgaaaaccaatgggttaaatttgtaagtatcactaagaaagatg gttattggtggggtaaatttaaatatccaactaatccatcaagtggatatttctacatggctcttggtgagattacagataa aaaaggtcgtatcaaaaaagagaaaaaattatatggtcgtattaaatggttataacattttagactagg (SEQ ID NO: 5), or a fragment thereof which is functionally active as an endolysin. Suitably there is provided a nucleic acid comprising a nucleic acid sequence encoding an endolysin, designated herein as endolysin 2, having a nucleic acid sequence: atgtatgctaaattaactcgaagtgagtttttatctgtattaaatcaatctgttggtagaaaatatgacatggataactatgc aggatttcaatgctttgactacgctaactatggttggaataaattatttggttataatttagctggtaatggtgctaaagatat tccaagtcctaaatggaataactttacaggaaaagctactgtatataaaaatacacctagctttttaccagaacctggtg accttgttgtttggggtagtcaaatgggtaacggttggggtcacgttgcttgggtagttagtgctacacttaatcagattgtt gttatcgaacagaactggttgggtggtggctggactactggtgacgcttatcatgcatggggttgggaatgtgctacaa gacgtgtacattcttataacaaccctatgtggttcattagacctaactttaaaccagaaaaaccccaaccaaaaacaa cttggaattggtctggagtgtttactgctaactctactatcaaagtacgtgttaaacctggattaagaggtagagtagtag ataaaggttcatggatatacgaaaaccaatgggttaaatttgtaagtatcactaagaaagatggttattggtggggtaa atttaaatatccaactaatccatcaagtggatatttctacatggctcttggtgagattacagataaaaaaggtcgtatcaa aaaagagaaaaaattatatggtcgtattaaatggttataa (SEQ ID NO: 8 (fragment of SEQ ID NO: 5)), or a fragment thereof which is functionally active as an endolysin. Suitably, an endolysin as discussed herein is functionally active as an endolysin in for at least S. hominis. Suitable tests to determine endolysin activity would be known in the art and are as discussed in the examples provided herein. Suitably an endolysin as disclosed herein or a fragment thereof may be fused to another functional sequence, such as a tag for purification or detection, for example green fluorescent protein (GFP), or an enzyme. Suitably there is provided a nucleic acid sequence encoding an endolysin as discussed herein fused to a nucleic acid encoding another functional sequence, such as a tag for purification or detection, for example green fluorescent protein (GFP), or an enzyme. Surprisingly the inventors have determined that bioinformatic analysis of the bacteriophage lytic for at least S. hominis, wherein the bacteriophage comprises a nucleic acid sequence as set forth by SEQ ID NO: 1 (also referred to as the endolysin 1 genome herein) revealed two separate genes, each encoding endolysins and it is considered these endolysins have huge potential as enzybiotics. The respective endolysins are discussed herein as endolysin 1 (AA2 endolysin A) and endolysin 2 (AA2 endolysin B). According to a second aspect of the present invention, there is provided one or more endolysins and variants thereof, wherein the one or more endolysins and variants thereof comprise an amino acid sequence that has at least 70% sequence identity with an amino acid sequence as set forth by SEQ ID NO: 2 or 3. Suitably the one or more endolysins are bacteriophage-derived endolysins. Optionally, the one or more endolysins, variant thereof or bacteriophage-derived endolysins of the second aspect of the invention may comprise an amino acid sequence that has at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with SEQ ID NO: 2. Optionally, the one or more endolysins, variant thereof or bacteriophage-derived endolysins of the second aspect of the invention may comprise an amino acid sequence that has at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with SEQ ID NO: 3. Optionally, the one or more endolysins, variant thereof or bacteriophage-derived endolysins of the second aspect of the invention may comprise an amino acid sequence which is a fragment of SEQ ID NO:2, which is functionally equivalent to an endolysin with the sequence SEQ ID NO: 2. Optionally, such a fragment may have a sequence similarity of at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% to a corresponding fragment of SEQ ID NO: 2. Optionally, the one or more endolysins, variant thereof or bacteriophage-derived endolysins of the second aspect of the invention may comprise an amino acid sequence which is a fragment of SEQ ID NO: 3, which is functionally equivalent to an endolysin with the sequence SEQ ID NO: 3. Optionally, such a fragment may have a sequence similarity of at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% to a corresponding fragment of SEQ ID NO: 3. Suitably an endolysin, designated herein as endolysin 1 has an amino acid sequence comprising or consisting of an amino acid sequence as set forth by: MVKYSEYWNGVPVRFDLLPFGTRRYGQKLRKGKPEFLVAHDTGNINTTAQ NNIDYYRNTYNIAWDYVASAHIFVDDKECVICIPANEVAWHVLLNATLDN LWYGVDANYGAVGVEGCYFENRERTKKSLDNMARVLAYLCDYWKIDYKTQ MPGHQDIQANKQDPGNILAYAGYGRATSNLDKLVGKYVGKSTTKPVSKSK ETKTVTETAKAGQITPQAKHTKPKTTWNWSGVFYPNTTIKVRKSPGLKGA VVDRNSWLYNKNDWVKFDQVIKKDGYWWIRFKYQAPGSSKDHFYCAVCKM TDKKGRIKAEKYWGRIDWK (SEQ ID NO: 3) Suitably an endolysin, designated herein as endolysin 2 has an amino acid sequence comprising or consisting of an amino acid sequence as set forth by: MYAKLTRSEFLSVLNQSVGRKYDMDNYAGFQCFDYANYGWNKLFGYNLAG NGAKDIPSPKWNNFTGKATVYKNTPSFLPEPGDLVVWGSQMGNGWGHVAW VVSATLNQIVVIEQNWLGGGWTTGDAYHAWGWECATRRVHSYNNPMWFIR PNFKPEKPQPKTTWNWSGVFTANSTIKVRVKPGLRGRVVDKGSWIYENQW VKFVSITKKDGYWWGKFKYPTNPSSGYFYMALGEITDKKGRIKKEKKLYG RIKWL (SEQ ID NO: 2) Optionally, the one or more bacteriophage-derived endolysins may be derived from an S. hominis bacteriophage. Optionally the one or more bacteriophage-derived endolysins may be derived from the bacteriophage of the first aspect of the invention. Optionally, the one or more bacteriophage-derived endolysins may be encoded by the genome of the bacteriophage of the first aspect of the invention. Suitably the endolysins may be recombinant. Suitably a recombinant endolysin may be produced in E. coli or another suitable organism as would be known in the art. Optionally, the endolysins exhibit lytic activity against one or more strains of S. hominis. Optionally the endolysins exhibit lytic activity against one or more strains of Rothia, a species associated with human breath malodour. Optionally the endolysins exhibit activity against one or more strains of Staphylococcus spp associated with human body malodour, S. aureus and also S. pseudintermedius, a species causing dermatitis in dogs. Optionally the endolysins exhibit activity against one or more strains of Bacillus isolated from human skin. In embodiments it is considered that a combination of the two phage-encoded endolysins designated herein as endolysin 1 and endolysin 2 would have broader activity than a single endolysin. Suitably, one or both of the endolysins designated herein as endolysin 1 and endolysin 2 or variants or fragments thereof can be used as active components of antibacterial deodorants and other cosmetic and hygienic products and may also be considered as antibacterials to treat S. pseudintermedius- associated dermatitis in dogs. Optionally, the one or more endolysins, variant thereof or bacteriophage-derived endolysins of the second aspect of the invention or recombinant endolysins as discussed herein may comprise a cell binding domain. Optionally, the cell binding domain may be located at or near the C-terminal end of the endolysin. Optionally, the one or more bacteriophage-derived endolysins of the second aspect of the invention may comprise a cell wall binding domain. Optionally, the cell wall binding domain may be located at or near the C-terminal end of the endolysin. Optionally, the one or more bacteriophage-derived endolysins of the second aspect of the invention may comprise a peptidoglycan cell wall binding domain. Optionally, the peptidoglycan cell wall binding domain may be located at or near the C-terminal end of the endolysin. Optionally, the one or more endolysins, variant thereof or bacteriophage-derived endolysins of the second aspect of the invention may comprise one or more enzymatic activity domain. Optionally, the enzymatic activity domain may be located at or near the N-terminal end of the endolysin. Optionally, the one or more endolysins, variant thereof or bacteriophage-derived endolysins of the second aspect of the invention may comprise an N-acetylmuramidase (lysozyme) domain. Optionally, the N- acetylmuramidase (lysozyme) domain may be located at or near the N-terminal end of the endolysin. Optionally, the one or more endolysins, variant thereof or bacteriophage-derived endolysins of the second aspect of the invention may comprise an N-acetyl-β-d-glucosaminidase (glycosylase) domain. Optionally, the N-acetyl-β-d- glucosaminidase (glycosylase) domain may be located at or near the N-terminal end of the endolysin. Optionally, the one or more endolysins, variant thereof or bacteriophage-derived endolysins of the second aspect of the invention may comprise an N-acetylmuramoyl-l-alanine amidase domain. Optionally, the N-acetylmuramoyl-l- alanine amidase domain may be located at or near the N-terminal end of the endolysin. Optionally, the one or more endolysins, variant thereof or bacteriophage-derived endolysins of the second aspect of the invention may comprise an l-alanoyl-d- glutamate endopeptidase domain. Optionally, the l-alanoyl-d-glutamate endopeptidase domain may be located at or near the N-terminal end of the endolysin. Optionally, the one or more endolysins, variant thereof or bacteriophage-derived endolysins of the second aspect of the invention may comprise an interpeptide bridge- specific endopeptidase domain. Optionally, the interpeptide bridge-specific endopeptidase domain may be located at or near the N-terminal end of the endolysin. Optionally, the one or more endolysins, variant thereof or bacteriophage-derived endolysins of the second aspect of the invention may comprise a cysteine, histidine- dependent amidohydrolases / peptidases (CHAP) domain. Optionally, the CHAP domain may be located at or near the N-terminal end of the endolysin. Optionally, the one or more endolysins, variant thereof or bacteriophage-derived endolysins of the second aspect of the invention may comprise an amidase CHAP domain. Optionally, the amidase CHAP domain may be located at or near the N-terminal end of the endolysin. As will be appreciated by those of skill in the art, fragments of the endolysins may be created to include or not include specific domains as discussed herein. Optionally, the one or more endolysins, variant thereof or bacteriophage-derived endolysins of the second aspect of the invention may comprise two or more of the enzymatic activity domains, wherein the enzymatic activity domains are selected from an N-acetylmuramidase (lysozyme) domain, an N-acetyl-β-d-glucosaminidase (glycosylase) domain, an N-acetylmuramoyl-l-alanine amidase domain, an l-alanoyl- d-glutamate endopeptidase domain, an interpeptide bridge-specific endopeptidase domain, a CHAP domain and an amidase CHAP domain. Optionally, there may be provided two or more endolysins, variants thereof or bacteriophage-derived endolysins in the second aspect of the invention. Optionally, the two or more endolysins, variants thereof or bacteriophage-derived endolysins may each comprise a cell binding domain, which may be located at or towards the C- terminal end of each endolysin. Optionally, the two or more endolysins, variants thereof or bacteriophage-derived endolysins may each comprise one or more enzymatic activity domains at or towards the N-terminal end of each endolysin. Optionally, the two or more endolysins, variants thereof or bacteriophage-derived endolysins may comprise identical enzymatic activity domains. Optionally, the two or more endolysins, variants thereof or bacteriophage-derived endolysins may comprise enzymatic activity domains which are distinct from one another. Optionally, the two or more endolysins, variants thereof or bacteriophage-derived endolysins may comprise one or more enzymatic activity domains selected from an N-acetylmuramidase (lysozyme) domain, an N-acetyl-β-d-glucosaminidase (glycosylase) domain, an N- acetylmuramoyl-l-alanine amidase domain, an l-alanoyl-d-glutamate endopeptidase domain, an interpeptide bridge-specific endopeptidase domain, a CHAP domain and an amidase CHAP domain. Optionally, the two or more endolysins, variants thereof or bacteriophage-derived endolysins may form a complex. Optionally, the endolysins, variants thereof or bacteriophage-derived endolysins may exist and function as monomers. Aspects of the second aspect of the invention may be combined with aspects of the first aspect of the invention. According to a third aspect of the present invention, there is provided a composition comprising: i. a panel comprising one or more bacteriophages lytic for at least S. hominis, wherein at least one of the one or more bacteriophages comprises a genome that has at least 95% sequence identity with SEQ ID NO: 1; and ii. a carrier. Optionally, the panel of bacteriophages exhibit is lytic activity in one or more strains of S. hominis, S. haemolyticus, S. lugdunensis, Rothia, S. aureus and S. pseudintermedius. Optionally the endolysins exhibit activity against at least two of a combination of S. hominis, S. haemolyticus, S. lugdunensis, Rothia, S. aureus and S. pseudintermedius. Optionally the endolysins exhibit activity against at least three of a combination of S. hominis, S. haemolyticus, S. lugdunensis, Rothia, S. aureus and S. pseudintermedius. Optionally the endolysins exhibit activity against at least four of a combination of S. hominis, S. haemolyticus, S. lugdunensis, Rothia, S. aureus and S. pseudintermedius. Optionally the endolysins exhibit activity against of a combination of each of S. hominis, S. haemolyticus, S. lugdunensis, Rothia, S. aureus and S. pseudintermedius. Optionally, when the panel comprises two or more bacteriophages the two or more bacteriophages may be any suitable bacteriophage for targeting body malodour. It would be understood by the skilled person that the term panel of bacteriophage is synonymous with the term preparation of isolated bacteriophage. The use of the term isolate requires that bacteriophages of the present invention have been isolated and / or purified from their natural environment. Optionally, when the panel of bacteriophage comprises two or more bacteriophages, the bacteriophages may be prepared for separate, sequential or simultaneous administration. Suitably a panel may comprise two or more bacteriophages wherein the two or more bacteriophages are two or more lytic bacteriophages or a mixture of lytic and temperate bacteriophages. Optionally, the carrier may be any suitable topical or transdermal carrier. The carrier may be any suitable gel, cream, emulsion, lotion or ointment. Optionally, the topical carrier may be any suitable carrier for application to human skin. Optionally, the composition may be delivered to a human subject’s skin using an aerosol spray. Optionally, the composition may be delivered to a human subject’s skin directly, using any suitable applicator. Aspects of the third aspect of the invention may be combined with aspects of the first aspect and / or second aspect of the invention. According to a fourth aspect of the present invention, there is provided a composition comprising: i. one or more endolysins, wherein the one or more endolysins comprise an amino acid sequence that has at least 70% sequence identity with SEQ ID NO: 2 or 3; and ii. a carrier. As will be appreciated by those of the skill in the art, the one or more endolysins may be a bacterially derived endolysin as discussed herein, or may be a recombinantly provided endolysin encoded by a nucleic acid with a sequence as set forth in the nucleic acid sequences as discussed herein, or a protein with an amino sequence as set forth by the sequences discussed herein. Optionally, the one or more endolysins of the fourth aspect of the invention may comprise an amino acid sequence that has at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with SEQ ID NO: 2. Optionally, the one or more endolysins of the fourth aspect of the invention may comprise an amino acid sequence that has at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with SEQ ID NO: 3. Optionally, the one or more endolysins of the second aspect of the invention may comprise an amino acid sequence which is a fragment of SEQ ID NO:2 which is functionally equivalent to an endolysin with the sequence SEQ ID NO: 2. Optionally, such a fragment may have a sequence similarity of at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% to a corresponding fragment of SEQ ID NO: 2. Optionally, the one or more endolysins of the second aspect of the invention may comprise an amino acid sequence which is a fragment of SEQ ID NO:3 which is functionally equivalent to an endolysin with the sequence SEQ ID NO: 3. Optionally, such a fragment may have a sequence similarity of at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% to a corresponding fragment of SEQ ID NO: 3. Optionally, the one or more endolysins may be derived from an S. hominis bacteriophage. Optionally the one or more endolysins may be derived from the bacteriophage of the first aspect of the invention. Optionally, the one or more bacteriophage-derived endolysins may be encoded by the genome of the bacteriophage of the first aspect of the invention. Optionally, the one or more endolysins exhibit lytic activity against one or more strains of S. hominis. Optionally, the one or more endolysins comprise aspects disclosed in the second aspect of the invention. Optionally, the carrier may be any suitable topical or transdermal carrier. The carrier may be any suitable gel, cream, emulsion, lotion or ointment. Optionally, the topical carrier may be any suitable carrier for application to human skin. Optionally, the composition may be delivered to a human subject’s skin using an aerosol spray. Optionally, the composition may be delivered to a human subject’s skin directly, using any suitable applicator. Aspects of the fourth aspect of the invention may be combined with aspects of the first aspect, second aspect and / or third aspect of the invention. According to a fifth aspect of the present invention, there is provided a method of lysing S. hominis bacteria, the method comprising applying the composition of the third aspect or the fourth aspect to the desired skin surface of the user. Optionally, the composition may be applied directly to the user’s skin by application of the composition in a gel, lotion, cream or ointment form. Optionally, the composition can be sprayed onto the user’s skin using an aerosol. Optionally, the method comprises applying the composition of the third and fourth aspects to the axilla area of a user’s skin. According to a sixth aspect of the present invention, there is provided a nucleic acid molecule encoding one or more endolysins, wherein the nucleic acid molecule has at least 70% sequence identity with SEQ ID NO: 4 or 5. Detailed Description of Invention Brief Description of the Figures Figure 1 – Demonstrates the genome sequence of the bacteriophage AA002 (SEQ ID NO: 1). Figure 2 – Demonstrates the amino acid sequence of endolysin 1 (SEQ ID NO: 2). Figure 3 – Demonstrates the amino acid sequence of endolysin 2 (SEQ ID NO: 3). Figure 4 – Demonstrates a plaque assay to assess the effect of the AA002 bacteriophage on S. hominis strain 311A susceptible to infection by the AA002 phage. AA002 bacteriophage was titrated to a range of concentrations and applied to S. hominis lawn. Clear zones of lysis are demonstrated on the bacterial lawn, which increase in size relative to the increased concentration of AA002 bacteriophage. Figure 5 – SDS-PAGE gel analysis of GST-tagged recombinant endolysin proteins, endolysin 1 and endolysin 2. DNA samples encoding the amino acid sequences SEQ ID NO: 2 (endolysin 1) and SEQ ID NO: 3 (endolysin 2) were amplified by PCR and each cloned into pLEICS-14 vector (https: / / le.ac.uk / mcb / facilities-and- technologies / protex / available-vectors), to yield plasmids, each encoding respective endolysin with an N-terminal GST tag. Endolysin-encoding plasmids were then transformed into E. coli BL21 strain After induction with IPTG (250 ml culture, induced at OD6000.6, and incubated for 18h at 16oC), the E. coli cells were precipitated by centrifugation and lysed by sonication, and the soluble and insoluble cell fractions were analysed using by SDS-PAGE. Figure 5 shows the gel stained with Coomassie blue to detect the recombinant proteins. This analysis shows that both GST-tagged endolysin 1 and endolysin 2 are expressed by E. coli but are retained in the insoluble fraction after cell lysis. Figure 6 – Solubilised recombinant AA002 phage-derived endolysin 1 and endolysin 2 can effectively lyse S. hominis, but not S. epidermidis. Samples of the insoluble protein fractions containing recombinant endolysin 1 and endolysin 2, as shown in Fig. 5, were solubilised using 2M urea and subjected to a rapid freeze-thaw protocol as detailed in Singhvi et al., 2021, Front. Microbiol., 12, doi: The activity of the crude preparations containing solubilised endolysins 1 and 2, either fused to GST-tag or treated with TEV to remove the tag (10 µl per spot), was then assessed using the semi-solid (0.5% agar) biofilm model for their ability to lyse S. hominis 311A and S. epidermidis SFHA. 2M urea solution was used as a control to demonstrate that the growth of S. hominis and S. epidermidis strains was not affected by the solubilising agent. The presence of zones of lysis indicates that both endolysins lysed S. hominis, but S. epidermidis was relatively resistant to lysis by AA002-derived endolysins. Figure 7 - The effect of the AA002 bacteriophage and the AA002 bacteriophage- derived recombinant endolysins 1 and 2 solubilised in 2M urea on S. hominis AAT6 strain which is not susceptible to the productive infection by the phage, assessed using the semi-solid (0.5% w / v agar) biofilm model. Only the undiluted AA002 sample shows a sign of lysis of S. hominis, probably by the “lysis from without” mechanism; however, solubilised endolysins 1 and 2 are both capable of lysing this strain, as demonstrated by the appearance of clear zones of lysis where solubilised recombinant endolysins were spotted. Figure 8. AA002-derived endolysin 1 and endolysin 2 preferentially lyse malodour- associated Staphylococcus species. Solubilised recombinant endolysin proteins were concentrated using concentrator spin columns and their activity was then assessed using the semi-solid (0.5% w / v agar) biofilm model on a selection of bacterial strains associated with production of body malodour (S. hominis, S. lugdunesis and S. haemolyticus) and S. epidermidis, a species believed to be a benign or beneficial member of healthy skin microbiota. Equal amount of the crude concentrated recombinant endolysin-containing lysate was spotted on the different bacterial lawn in each case. Both AA002-derived endolysin 1 and endolysin 2 preferentially lysed malodour-associated species, as judged by the size and appearance of the zone of lysis. Methods of alignment of sequences for comparison are well known in the art. Thus, the determination of percent identity between any two sequences can be accomplished using a mathematical algorithm. Non-limiting examples of such mathematical algorithms are the algorithm of Myers and Miller (1988) CABIOS 4: 11- 17; the local homology algorithm of Smith et al. (1981) Adv. Appl. Math.2: 482; the homology alignment algorithm of Needleman and Wunsch (1970) J Mol. Biol. 48: 443-453; the search-for-similarity-method of Pearson and Lipman (1988) Proc. Natl. Acad. Sci.85: 2444-2448; the algorithm of Karlin and Altschul (1990) Proc. Natl. Acad. Sci. USA 872264, modified as in Karlin and Altschul (1993) Proc. Natl. Acad Sci. USA 90: 5873-5877. Computer implementations of these mathematical algorithms can be utilized for comparison of sequences to determine sequence identity. Such implementations include, but are not limited to: CLUSTAL in the PC / Gene program (available from Intelligenetics, Mountain View, California); the ALIGN program (Version 2.0) and GAP, BESTFIT, BLAST, FASTA, and TFASTA in the Wisconsin Genetics Software Package, Version 8 (available from Genetics Computer Group (GCG), 575 Science Drive, Madison, Wisconsin, USA). Alignments using these programs can be performed using the default parameters. The CLUSTAL program is well described by Higgins et al. (1988) Gene 73: 237-244 (1988); Higgins et al. (1989) CABIOS 5: 151- 153; Corpet et al. (1988) Nucleic Acids Res.16 : 10881-90; Huang et al. (1992) CABIOS 8: 155-65 ; and Pearson et al. (1994) Meth. Mol. Biol.24: 307-331. The ALIGN program is based on the algorithm of Myers and Miller (1988) supra. A PAM120 weight residue table, a gap length penalty of 12, and a gap penalty of 4 can be used with the ALIGN program when comparing amino acid sequences. The BLAST programs of Altschul et al (1990) J. Mol. Biol.215: 403 are based on the algorithm of Karlin and Altschul (1990) supra. BLAST nucleotide searches can be performed with the BLASTN program, score = 100, wordlength = 12, to obtain nucleotide sequences homologous to a nucleotide sequence encoding a protein of the invention. BLAST protein searches can be performed with the BLASTX program, score = 50, wordlength = 3, to obtain amino acid sequences homologous to a protein or polypeptide of the invention. To obtain gapped alignments for comparison purposes, Gapped BLAST (in BLAST 2.0) can be utilized as described in Altschul et al. (1997) Nucleic Acids Res.25: 3389. Alternatively, PSI-BLAST (in BLAST 2.0) can be used to perform an iterated search that detects distant relationships between molecules. See Altschul et al. (1997) supra. When utilizing BLAST, Gapped BLAST, PSI-BLAST, the default parameters of the respective programs (e. g., BLASTN for nucleotide sequences, BLASTX for proteins) can be used. See http: / / www. ncbi. hlm. nih. gov. Alignment may also be performed manually by inspection. Alignment may also be performed manually by inspection. As used herein, "sequence identity" or "identity" in the context of two nucleic acid or amino acid / polypeptide sequences makes reference to the residues in the two sequences that are the same when aligned for maximum correspondence over a specified comparison window. When percentage of sequence identity is used in reference to proteins it is recognized that residue positions which are not identical often differ by conservative amino acid substitutions, where amino acid residues are substituted for other amino acid residues with similar chemical properties (e. g., charge or hydrophobicity) and therefore do not change the functional properties of the molecule. When sequences differ in conservative substitutions, the percent sequence identity may be adjusted upwards to correct for the conservative nature of the substitution. Sequences that differ by such conservative substitutions are said to have "sequence similarity" or "similarity". Means for making this adjustment are well known to those of skill in the art. Typically this involves scoring a conservative substitution as a partial rather than a full mismatch, thereby increasing the percentage sequence identity. Thus, for example, where an identical amino acid is given a score of 1 and a non-conservative substitution is given a score of zero, a conservative substitution is given a score between zero and 1. Each document, reference, patent application or patent cited in this text is expressly incorporated herein in their entirety by reference, which means it should be read and considered by the reader as part of this text. That the document, reference, patent application or patent cited in the text is not repeated in this text is merely for reasons of conciseness. Throughout the specification, unless the context demands otherwise, the terms ‘comprise’ or ‘include’, or variations such as ‘comprises’ or ‘comprising’, ‘includes’ or ‘including’ will be understood to imply the includes of a stated integer or group of integers, but not the exclusion of any other integer or group of integers. The use of the term "nucleotide sequences" or nucleic acid sequence herein is not intended to limit the present invention to nucleotide constructs comprising DNA. Those of ordinary skill in the art will recognize that nucleotide constructs, particularly polynucleotides and oligonucleotides, comprised of ribonucleotides and combinations of ribonucleotides and deoxyribonucleotides may also be employed in the methods disclosed herein. The nucleotide constructs, nucleotide molecules and nucleotide sequences of the invention also encompass all forms of nucleotide constructs including, but not limited to, single-stranded forms, double-stranded forms, hairpins, stem-and-loop structures and the like. Additional sequence modifications are known to enhance gene expression in a particular recombinant host. These include elimination of sequences encoding spurious polyadenylation signals, exon-intron splice site signals, repeats, and other such well-characterized sequences that may be deleterious to gene expression. The G-C content of the sequence may be adjusted to levels average for a given recombinant host, as calculated by reference to known genes expressed in the host cell. The invention encompasses isolated or substantially purified nucleic acid or protein compositions. An "isolated" or "purified" nucleic acid molecule or protein, or biologically active portion thereof, is substantially free of other cellular material, or culture medium when produced by recombinant techniques, or substantially free of chemical precursors or other chemicals when chemically synthesized. By "fragment" is intended a portion of the nucleotide sequence or a portion of the amino acid sequence and hence protein encoded thereby. Fragments of a nucleotide sequence may encode protein fragments that retain the biological of the native protein. By "variant" endolysin or protein is intended a protein derived from the native endolysin or protein by deletion (so-called truncation) or addition of one or more amino acids to the N- terminal and / or C-terminal end of the native endolysin / protein. A biologically active variant of an endolysin / protein of the invention may differ from that protein by as few as 1-15 amino acid residues, as few as 1-10, such as 6-10, as few as 5, as few as 4, 3, 2, or even 1 amino acid residue. Nucleotide sequences of the invention include both the naturally occurring sequences as well as mutant forms. Likewise, the amino acid sequences / proteins of the invention encompass both naturally occurring amino acids as well as variations and modified forms thereof. Such variants will continue to possess the desired endolysin activity. The deletions, insertions, and substitutions of the amino acid sequences encompassed herein are not expected to produce radical changes in the characteristics of the endolysin. However, when it is difficult to predict the exact effect of the substitution, deletion, or insertion in advance of doing so, one skilled in the art will appreciate that the effect will be evaluated by routine screening assays. Examples Example 1 – Isolation and characterisation of AA002 Bacteriophage The AA002 Bacteriophage was isolated using a modified phage enrichment protocol. Axilla skin swab samples were provided by a range of volunteers (of different ages, sexes and ethnicities). The swab samples were mixed with sterile LB medium and incubated overnight at 37oC; after which the samples were filtered through 0.2 µm filter and spotted onto lawns of several S. hominis bacterial strains. One sample produced a few individual plaques on lawns from several S. hominis strains. The bacteriophage obtained from these plaques was named AA002. AA002 was purified by the repeated single plaque sub-culturing (5x). The phage was then amplified using pooled plaques method (Clokie, Martha (2009). Bacteriophages: Methods and Protocols. Springer Protocols.ISBN 978-1-60327-564-4.)The AA002 bacteriophage DNA was isolated using phenol / chloroform extraction and sequenced using Illumina sequencing. Sequence analysis revealed that the AA002 bacteriophage had a genomic sequence of SEQ ID NO: 1. Analysis of the sequence determined that the genome encodes two distinct endolysin proteins (termed endolysin 1 (SEQ ID NO: 2) and endolysin 2 (SEQ ID NO: 3)). Sequence analysis of each endolysin revealed that each endolysin contained a putative cell wall binding domain and an enzymatic activity domain. Unexpectedly, it was discovered that both the enzymatic activity domains and cell wall binding domains of the two endolysins were distinct from one another. Analysis of endolysin 1 (SEQ ID NO: 2) revealed an amidase CHAP domain (cysteine, histidine-dependent amidohydrolases / peptidases domain) in the N-terminal half of the protein. The C-terminal half of the protein included a peptidoglycan binding domain. Analysis of the endolysin 2 (SEQ ID NO: 3) revealed an N-acetylmuramoyl-L-alanine amidase domain as a catalytic domain located in its N-terminal half; with a peptidoglycan-binding domain in the C-terminal half. Without wishing to be bound by the theory, the inventors consider that the two endolysin proteins may oligomerise and function as a complex. Whilst it is known in the art that Staphylococcal phages can have modular endolysins, it is normally the case that one of the expressed endolysin proteins contains both a cell wall binding domain and one or two enzyme domains, whilst the second endolysin protein in the modular complex only possesses a cell wall binding domain (Pinto D, Gonçalo R, Louro M, Silva MS, Hernandez G, Cordeiro TN, Cordeiro C, São-José C. On the Occurrence and Multimerization of Two-Polypeptide Phage Endolysins Encoded in Single Genes. Microbiol Spectr.2022 Aug 31;10(4)) It is therefore, unexpected, in this instance to derive a bacteriophage which encodes two endolysins, each with a distinct catalytic domain. Example 2 – Characterisation of bacteriophage AA002 activity To assess activities of the AA002 bacteriophage, a plaque assay using semi-solid (0.5% agar) biofilm was used to mimic the growth of non‐surface‐attached bacteria similar to observations from clinical specimens of human skin (as detailed in Crone et al.; 2015; J Wound Care; 24(2):64, 66-9, 72). Various bacterial strains, previously isolated from human skin, were inoculated into the molten agar, and the soft agar mixture was laid over a hard agar base. After the agar was solidified, AA002 phage was spotted, in 10-fold dilutions (10-1, 10-2, 10-3, 10-4, 10-5, 10-6, 10-7, 10-8, 10-9, 10-10, 10-11), 10 µl of each sample, on top of the S. hominis seeded agar overlay. The plates were then incubated at 37oC overnight. The results of the assay demonstrated that the AA002 bacteriophage was capable of preventing bacterial growth and biofilm formation of S. hominis strains susceptible to phage infection (4 out of 19 tested). This can be seen in Figure 4, as judged by the clear zones of lysis on the bacterial lawns (a typical figure is shown, using S. hominis 311A as an example). No zones of lysis were observed when bacterial strains non- susceptible to AA002 phage infection were utilised, including several strains of S. hominis (15 out of 19 tested) and all tested strains of S. epidermidis (4 strains). Example 3 – Testing anti-S. hominis activity of endolysins encoded by bacteriophage AA002 To assess the scope of the anti-S. hominis activity of the endolysins encoded by the AA002 bacteriophage, the genes encoding endolysin 1 and endolysin 2 were cloned into a plasmid and expressed in E. coli. The cells were lysed and sonicated. Centrifugation was then used to obtain soluble and insoluble fractions. Finally, protein separation of each fraction was carried out using an SDS-PAGE gel. Figure 5 demonstrates that both the recombinant endolysin 1 and endolysin 2 proteins are highly expressed by E. coli, but remain in the insoluble fraction after cell lysis, indicating the proteins are deposited in inclusion bodies. So as to solubilise the recombinant endolysin proteins, the insoluble fraction samples were treated with 2M urea and subjected to a rapid freeze-thaw protocol as detailed in Singhvi et al., 2021, Front. Microbiol., 12, doi: https: / / doi.org / 10.3389 / fmicb.2021.618559. The activity of solubilised proteins was then assessed using the semi-solid (0.5% w / v agar) biofilm model, as described in Example 2. Each of the solubilised recombinant AA002 endolysins was capable of inhibiting biofilm formation of all tested S. hominis strains, whether or not they were susceptible to lysis by the AA002 phage (Figures 6 and 7). A relatively minor inhibition of biofilm of S. epidermidis was also observed (Fig.6), but to a lesser extent than that for S. hominis. Surprisingly, the inventors discovered that the endolysins were active and capable of targeting the bacteria even though dissolved in 2M urea (2M urea itself did not affect the growth of S. hominis in this model system). Example 4 – Testing lytic activity of endolysins encoded by bacteriophage AA002 on a wider range of strains isolated from human skin. To assess specificity of AA002-derived endolysins lytic activity, samples of solubilised recombinant endolysin proteins were concentrated using concentrator spin columns and their activity was then assessed using the semi-solid (0.5% agar) biofilm model, as described in Example 2 on a selection of malodour-associated Staphylococcus strains (S. hominis, S. lugdunesis and S. haemolyticus) and S. epidermidis, a species believed to be a benign or beneficial member of healthy skin microbiota. Equal amount of the crude concentrated recombinant endolysin-containing lysate was spotted on the different bacterial lawn in each case. The result of this experiment revealed that both AA002-derived endolysin 1 and endolysin 2 preferentially lysed malodour-associated species (Fig 8). The inventors have thus discovered a novel phage AA002 capable of infecting a sub- set of S. hominis strains isolated from human skin, and AA002 phage-derived endolysins, which are capable of lytic activity in S. hominis strains, irrespectively of their susceptibility to productive infection by AA002 phage. Furthermore, AA002 derived endolysins were capable of lysing other human skin Staphylococci species associated with production of malodour, such as S. lugdunesis and S. haemolyticus – preferentially over S. epidermidis, a beneficial member of the skin microbiota.

Claims

Claims 1. A bacteriophage lytic for at least multiple strains of S. hominis, wherein the bacteriophage comprises a nucleic acid sequence that has at least 70% sequence identity with a sequence as set forth by SEQ ID NO:

1.

2. The bacteriophage of claim 1 comprising a nucleic acid sequence that has at least 95% sequence identity with a sequence as set forth by SEQ ID NO:

1.

3. The bacteriophage of claim 1 comprising a nucleic acid sequence as set forth by of SEQ ID NO:

1.

4. A nucleic acid sequence capable of encoding a first and second endolysin, the nucleic acid sequence comprising a sequence as set forth by: acgataacgtagaatcagatagtaagcctgagtcagaaaaatcagataaccctaaagggtaaaatggagtggatatgaatggt aaaatattctgaatattggaatggtgttcctgtacgttttgatttattacctttcggtacaagacgttatggacaaaaattaaga aaaggtaagcctgaatttttagtagcacatgatacaggtaatatcaatacaactgctcaaaataacattgattattatagaa atacttataatattgcttgggattatgtagcaagtgcacatatctttgttgatgataaagaatgtgtaatttgtattcctgctaac gaagtggcttggcatgtactattaaatgctactttagataacttatggtatggtgttgacgctaactatggtgcagttggagtt gaaggttgttactttgaaaatagagaacgaactaaaaaatctttagataatatggctcgtgtattagcttatctatgtgattac tggaaaattgattacaaaacacaaatgcctggacatcaagacattcaagctaataaacaagacccaggtaatatcttagc ttatgctggttacggtcgtgctactagtaacttagataaattagtaggtaaatatgtaggaaaatctacaactaaaccagta agtaaatctaaagaaactaagactgttactgaaacagcaaaagcaggacaaattaccccacaagctaaacatactaaa ccaaaaactacttggaactggtctggtgtgttctatcctaatacaactattaaggtacgtaaatcaccaggattaaaaggtg cagtagtggatagaaattcttggttatacaataagaatgactgggttaaatttgaccaagttattaaaaaagacggttattg gtggattcgatttaaatatcaagcacctggctctagtaaagaccatttctattgtgcagtatgtaaaatgactgataaaaaa ggtcgtattaaagcagaaaaatattggggtcgtattgactggaaataagattgggggtatactaaatgtatgctaaattaactc gaagtgagtttttatctgtattaaatcaatctgttggtagaaaatatgacatggataactatgcaggatttcaatgctttgactacgctaa ctatggttggaataaattatttggttataatttagctggtaatggtgctaaagatattccaagtcctaaatggaataactttacaggaaa agctactgtatataaaaatacacctagctttttaccagaacctggtgaccttgttgtttggggtagtcaaatgggtaacggttggggtc acgttgcttgggtagttagtgctacacttaatcagattgttgttatcgaacagaactggttgggtggtggctggactactggtgacgctt atcatgcatggggttgggaatgtgctacaagacgtgtacattcttataacaaccctatgtggttcattagacctaactttaaaccagaa aaaccccaaccaaaaacaacttggaattggtctggagtgtttactgctaactctactatcaaagtacgtgttaaacctggattaaga ggtagagtagtagataaaggttcatggatatacgaaaaccaatgggttaaatttgtaagtatcactaagaaagatggttattggtgg ggtaaatttaaatatccaactaatccatcaagtggatatttctacatggctcttggtgagattacagataaaaaaggtcgtatcaaaa aagagaaaaaattatatggtcgtattaaatggttataacattttagactagg (SEQ ID NO:6).

5. A nucleic acid encoding an endolysin, the nucleic acid comprising a nucleotide sequence with a sequence identity of at least 95% to a sequence as set forth by: acgataacgtagaatcagatagtaagcctgagtcagaaaaatcagataaccctaaagggtaaaatggagtggatat gaatggtaaaatattctgaatattggaatggtgttcctgtacgttttgatttattacctttcggtacaagacgttatggacaaa aattaagaaaaggtaagcctgaatttttagtagcacatgatacaggtaatatcaatacaactgctcaaaataacattga ttattatagaaatacttataatattgcttgggattatgtagcaagtgcacatatctttgttgatgataaagaatgtgtaatttgt attcctgctaacgaagtggcttggcatgtactattaaatgctactttagataacttatggtatggtgttgacgctaactatgg tgcagttggagttgaaggttgttactttgaaaatagagaacgaactaaaaaatctttagataatatggctcgtgtattagc ttatctatgtgattactggaaaattgattacaaaacacaaatgcctggacatcaagacattcaagctaataaacaagac ccaggtaatatcttagcttatgctggttacggtcgtgctactagtaacttagataaattagtaggtaaatatgtaggaaaat ctacaactaaaccagtaagtaaatctaaagaaactaagactgttactgaaacagcaaaagcaggacaaattaccc cacaagctaaacatactaaaccaaaaactacttggaactggtctggtgtgttctatcctaatacaactattaaggtacgt aaatcaccaggattaaaaggtgcagtagtggatagaaattcttggttatacaataagaatgactgggttaaatttgacc aagttattaaaaaagacggttattggtggattcgatttaaatatcaagcacctggctctagtaaagaccatttctattgtgc agtatgtaaaatgactgataaaaaaggtcgtattaaagcagaaaaatattggggtcgtattgactggaaataa (SEQ ID NO: 4) or a fragment thereof which is functionally active as an endolysin.

6. A nucleic acid encoding an endolysin as claimed by claim 5, the nucleic acid comprising a nucleotide sequence with a sequence as set forth by: atggtaaaatattctgaatattggaatggtgttcctgtacgttttgatttattacctttcggtacaagacgttatggacaaaaa ttaagaaaaggtaagcctgaatttttagtagcacatgatacaggtaatatcaatacaactgctcaaaataacattgatta ttatagaaatacttataatattgcttgggattatgtagcaagtgcacatatctttgttgatgataaagaatgtgtaatttgtatt cctgctaacgaagtggcttggcatgtactattaaatgctactttagataacttatggtatggtgttgacgctaactatggtgc agttggagttgaaggttgttactttgaaaatagagaacgaactaaaaaatctttagataatatggctcgtgtattagcttat ctatgtgattactggaaaattgattacaaaacacaaatgcctggacatcaagacattcaagctaataaacaagaccc aggtaatatcttagcttatgctggttacggtcgtgctactagtaacttagataaattagtaggtaaatatgtaggaaaatct acaactaaaccagtaagtaaatctaaagaaactaagactgttactgaaacagcaaaagcaggacaaattacccca caagctaaacatactaaaccaaaaactacttggaactggtctggtgtgttctatcctaatacaactattaaggtacgtaa atcaccaggattaaaaggtgcagtagtggatagaaattcttggttatacaataagaatgactgggttaaatttgaccaa gttattaaaaaagacggttattggtggattcgatttaaatatcaagcacctggctctagtaaagaccatttctattgtgcag tatgtaaaatgactgataaaaaaggtcgtattaaagcagaaaaatattggggtcgtattgactggaaataa or a fragment thereof which is functionally active as an endolysin.

7. A nucleic acid encoding an endolysin, the nucleic acid comprising a nucleotide sequence with at least 95% sequence identity to a sequence as set forth by gattgggggtatactaaatgtatgctaaattaactcgaagtgagtttttatctgtattaaatcaatctgttggtag aaaatatgacatggataactatgcaggatttcaatgctttgactacgctaactatggttggaataaattatttgg ttataatttagctggtaatggtgctaaagatattccaagtcctaaatggaataactttacaggaaaagctactg tatataaaaatacacctagctttttaccagaacctggtgaccttgttgtttggggtagtcaaatgggtaacggtt ggggtcacgttgcttgggtagttagtgctacacttaatcagattgttgttatcgaacagaactggttgggtggtg gctggactactggtgacgcttatcatgcatggggttgggaatgtgctacaagacgtgtacattcttataacaa ccctatgtggttcattagacctaactttaaaccagaaaaaccccaaccaaaaacaacttggaattggtctgg agtgtttactgctaactctactatcaaagtacgtgttaaacctggattaagaggtagagtagtagataaaggtt catggatatacgaaaaccaatgggttaaatttgtaagtatcactaagaaagatggttattggtggggtaaatt taaatatccaactaatccatcaagtggatatttctacatggctcttggtgagattacagataaaaaaggtcgt atcaaaaaagagaaaaaattatatggtcgtattaaatggttataacattttagactagg (SEQ ID NO: 5) or a fragment thereof which is functionally active as an endolysin.

8. A nucleic acid comprising a nucleic acid sequence encoding an endolysin as claimed in claim 7 having a nucleic acid sequence of: atgtatgctaaattaactcgaagtgagtttttatctgtattaaatcaatctgttggtagaaaatatgacatggataactatgc aggatttcaatgctttgactacgctaactatggttggaataaattatttggttataatttagctggtaatggtgctaaagatat tccaagtcctaaatggaataactttacaggaaaagctactgtatataaaaatacacctagctttttaccagaacctggtg accttgttgtttggggtagtcaaatgggtaacggttggggtcacgttgcttgggtagttagtgctacacttaatcagattgtt gttatcgaacagaactggttgggtggtggctggactactggtgacgcttatcatgcatggggttgggaatgtgctacaa gacgtgtacattcttataacaaccctatgtggttcattagacctaactttaaaccagaaaaaccccaaccaaaaacaa cttggaattggtctggagtgtttactgctaactctactatcaaagtacgtgttaaacctggattaagaggtagagtagtag ataaaggttcatggatatacgaaaaccaatgggttaaatttgtaagtatcactaagaaagatggttattggtggggtaa atttaaatatccaactaatccatcaagtggatatttctacatggctcttggtgagattacagataaaaaaggtcgtatcaa aaaagagaaaaaattatatggtcgtattaaatggttataa or a fragment thereof which is functionally active as an endolysin.

9. An endolysin comprising an amino acid sequence that has at least 70% sequence identity with SEQ ID NO: 2 or 3MYAKLTRSEFLSVLNQSVGRKYDMDNYAGFQCFDYANYGWNKLFGYNLAG NGAKDIPSPKWNNFTGKATVYKNTPSFLPEPGDLVVWGSQMGNGWGHVAW VVSATLNQIVVIEQNWLGGGWTTGDAYHAWGWECATRRVHSYNNPMWFIR PNFKPEKPQPKTTWNWSGVFTANSTIKVRVKPGLRGRVVDKGSWIYENQW VKFVSITKKDGYWWGKFKYPTNPSSGYFYMALGEITDKKGRIKKEKKLYG RIKWL (SEQ ID NO: 2) or MVKYSEYWNGVPVRFDLLPFGTRRYGQKLRKGKPEFLVAHDTGNINTTAQ NNIDYYRNTYNIAWDYVASAHIFVDDKECVICIPANEVAWHVLLNATLDN LWYGVDANYGAVGVEGCYFENRERTKKSLDNMARVLAYLCDYWKIDYKTQ MPGHQDIQANKQDPGNILAYAGYGRATSNLDKLVGKYVGKSTTKPVSKSK ETKTVTETAKAGQITPQAKHTKPKTTWNWSGVFYPNTTIKVRKSPGLKGA VVDRNSWLYNKNDWVKFDQVIKKDGYWWIRFKYQAPGSSKDHFYCAVCKM TDKKGRIKAEKYWGRIDWK (SEQ ID NO: 3) 10. An endolysin, comprising an amino acid sequence of: MVKYSEYWNGVPVRFDLLPFGTRRYGQKLRKGKPEFLVAHDTGNINTTAQ NNIDYYRNTYNIAWDYVASAHIFVDDKECVICIPANEVAWHVLLNATLDN LWYGVDANYGAVGVEGCYFENRERTKKSLDNMARVLAYLCDYWKIDYKTQ MPGHQDIQANKQDPGNILAYAGYGRATSNLDKLVGKYVGKSTTKPVSKSK ETKTVTETAKAGQITPQAKHTKPKTTWNWSGVFYPNTTIKVRKSPGLKGA VVDRNSWLYNKNDWVKFDQVIKKDGYWWIRFKYQAPGSSKDHFYCAVCKM TDKKGRIKAEKYWGRIDWK (SEQ ID NO: 3) 11. An endolysin comprising an amino acid sequence of: MYAKLTRSEFLSVLNQSVGRKYDMDNYAGFQCFDYANYGWNKLFGYNLAG NGAKDIPSPKWNNFTGKATVYKNTPSFLPEPGDLVVWGSQMGNGWGHVAW VVSATLNQIVVIEQNWLGGGWTTGDAYHAWGWECATRRVHSYNNPMWFIR PNFKPEKPQPKTTWNWSGVFTANSTIKVRVKPGLRGRVVDKGSWIYENQW VKFVSITKKDGYWWGKFKYPTNPSSGYFYMALGEITDKKGRIKKEKKLYG RIKWL (SEQ ID NO: 2) 12. A composition comprising:a panel of one or more bacteriophages lytic for at least S. hominis, wherein at least one of the one or more bacteriophages comprises a genome that has at least 95% sequence identity with SEQ ID NO: 1; and a carrier.

13. A composition comprising: i. one or more endolysins, wherein the one or more endolysins comprise an amino acid sequence that has at least 70% sequence identity with SEQ ID NO: 2 or 3; and ii. a carrier.

14. A method of lysing S. hominis bacteria, the method comprising applying the composition of claim 12 or claim 13 to a desired skin surface of a user.

15. A nucleic acid molecule encoding one or more endolysins, wherein the nucleic acid molecule has at least 70% sequence identity with SEQ ID NO: 4 or 5.

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