{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T18:38:43Z","timestamp":1792780723143,"version":"4.5.0"},"reference-count":48,"publisher":"Public Library of Science (PLoS)","issue":"10","license":[{"start":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T00:00:00Z","timestamp":1792713600000},"content-version":"am","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32573364"],"award-info":[{"award-number":["32573364"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Jilin Province Science and Technology Development Plan Project","award":["20260602058RC"],"award-info":[{"award-number":["20260602058RC"]}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    <jats:italic>Streptococcus suis<\/jats:italic>\n                    (\n                    <jats:italic>S. suis<\/jats:italic>\n                    ) is an encapsulated zoonotic pathogen that can form recalcitrant biofilms. Bacteriophage-derived endolysins and depolymerases represent promising antibiofilm agents, but currently, no report has described protein which displays both of lytic and capsule degradation activities simultaneously. Here, we mined the porcine gut virome and identified Lys33795, a dual-activity antibacterial protein that degrades both capsule and peptidoglycan of\n                    <jats:italic>S. suis<\/jats:italic>\n                    . Lys33795 consists of an N-terminal GH25_muramidase domain and a C-terminal cell wall binding domain (CBD). However, translational reinitiation at an internal start codon (M\n                    <jats:sub>217<\/jats:sub>\n                    ) in the Lys33795 sequence generates an additional CBD that may assembles with the full-length protein to form an oligomeric complex. Interestingly, the GH25 muramidase truncation fragment of Lys33795 not only retains its classical function as a peptidoglycan hydrolase for degrading bacterial cell walls but also exhibits degradation activity towards capsule. This discovery contrasts sharply with the traditional functional understanding of the GH25 family. In addition, the CBD alone has a stable dimer and, as a nonstandard depolymerase without any classical polysaccharide-degrading catalytic domains, retains its degradation activity against\n                    <jats:italic>S. suis<\/jats:italic>\n                    capsule. We elucidated the molecular mechanism of Lys33795 exhibiting dual activity by combining mutagenesis, lysis, and capsule degradation activity assays. In addition, the results of\n                    <jats:italic>in vitro<\/jats:italic>\n                    and\n                    <jats:italic>in vivo<\/jats:italic>\n                    experiments showed that Lys33795 can effectively prevent and clear\n                    <jats:italic>S. suis<\/jats:italic>\n                    biofilms, and is more effective than single active mutants, and has a enhance effect when used in combination with antibiotics. This study describes the first multimeric bacteriophage protein with dual activities of lysis and capsule degradation against\n                    <jats:italic>S. suis<\/jats:italic>\n                    , encoded by a single gene. These findings provide valuable insights for designing potent antibacterial proteins targeting encapsulated pathogens.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1014741","type":"journal-article","created":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T17:46:44Z","timestamp":1792777604000},"page":"e1014741","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":0,"title":["Dual activities of lysis and capsule degradation enable the bacteriophage protein Lys33795 to effectively disrupt Streptococcus suis biofilms"],"prefix":"10.1371","volume":"22","author":[{"given":"Yalu","family":"Ji","sequence":"first","affiliation":[{"name":"State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, Institute of Zoonosis, and College of Veterinary Medicine, Jilin University","place":["Changchun, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Meimei","family":"Zhang","sequence":"additional","affiliation":[{"name":"State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, Institute of Zoonosis, and College of Veterinary Medicine, Jilin University","place":["Changchun, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Liran","family":"Song","sequence":"additional","affiliation":[{"name":"State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, Institute of Zoonosis, and College of Veterinary Medicine, Jilin University","place":["Changchun, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hui","family":"Ning","sequence":"additional","affiliation":[{"name":"State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, Institute of Zoonosis, and College of Veterinary Medicine, Jilin University","place":["Changchun, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Li","family":"Wang","sequence":"additional","affiliation":[{"name":"State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, Institute of Zoonosis, and College of Veterinary Medicine, Jilin University","place":["Changchun, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0006-2156-7497","authenticated-orcid":true,"given":"Cao","family":"Qiu","sequence":"additional","affiliation":[{"name":"State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, Institute of Zoonosis, and College of Veterinary Medicine, Jilin University","place":["Changchun, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3522-195X","authenticated-orcid":true,"given":"Jingmin","family":"Gu","sequence":"additional","affiliation":[{"name":"State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, Institute of Zoonosis, and College of Veterinary Medicine, Jilin University","place":["Changchun, China"]},{"name":"Jiangsu Co-Innovation Center for the Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou University","place":["Yangzhou, China"]},{"name":"Yunnan Provincial Key Laboratory of Zoonosis Control and Prevention","place":["Kunming, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2026,10,23]]},"reference":[{"key":"ppat.1014741.ref001","doi-asserted-by":"crossref","first-page":"101098","DOI":"10.1016\/j.onehlt.2025.101098","article-title":"Streptococcus suis: Epidemiology and resistance evolution of an emerging zoonotic bacteria","volume":"21","author":"F Liu","year":"2025","journal-title":"One Health"},{"issue":"3","key":"ppat.1014741.ref002","article-title":"Current prevalence and therapeutic strategies for porcine Streptococcus suis in China","volume":"91","author":"R Lv","year":"2025","journal-title":"Appl Environ Microbiol"},{"key":"ppat.1014741.ref003","doi-asserted-by":"crossref","first-page":"110005","DOI":"10.1016\/j.vetmic.2024.110005","article-title":"Rethinking the control of Streptococcus suis infection: Biofilm formation","volume":"290","author":"H Wang","year":"2024","journal-title":"Vet 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(Basel)"},{"issue":"6","key":"ppat.1014741.ref007","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.3390\/microorganisms13061197","article-title":"Population Genomics, Virulence Traits, and Antimicrobial Resistance of Streptococcus suis Isolated in China","volume":"13","author":"Y Li","year":"2025","journal-title":"Microorganisms"},{"issue":"8","key":"ppat.1014741.ref008","doi-asserted-by":"crossref","first-page":"1765","DOI":"10.3390\/microorganisms9081765","article-title":"Update on the Mechanisms of Antibiotic Resistance and the Mobile Resistome in the Emerging Zoonotic Pathogen Streptococcus suis","volume":"9","author":"M Dech\u00eane-Tempier","year":"2021","journal-title":"Microorganisms"},{"key":"ppat.1014741.ref009","doi-asserted-by":"crossref","first-page":"146159","DOI":"10.1016\/j.ijbiomac.2025.146159","article-title":"Phage-encoded depolymerases and endolysins as prospective strategies to combat multidrug-resistant Klebsiella pneumoniae","volume":"321","author":"Y Zhang","year":"2025","journal-title":"Int J Biol Macromol"},{"issue":"12","key":"ppat.1014741.ref010","doi-asserted-by":"crossref","first-page":"1771","DOI":"10.3390\/ph18121771","article-title":"Bacteriophages and Their Enzymes: Allies Against Microbial Biofilms","volume":"18","author":"FM Husain","year":"2025","journal-title":"Pharmaceuticals (Basel)"},{"issue":"7","key":"ppat.1014741.ref011","article-title":"Phage and Endolysin Therapy Against Antibiotics Resistant Bacteria: From Bench to Bedside","volume":"6","author":"M Taati Moghadam","year":"2025","journal-title":"MedComm (2020)"},{"key":"ppat.1014741.ref012","article-title":"Bacteriophage lysins as programmable antimicrobials: mechanisms, engineering, and translational advances","author":"W Ma","year":"2026","journal-title":"Probiotics Antimicrob Proteins"},{"issue":"1","key":"ppat.1014741.ref013","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.01923-17","article-title":"Are Phage Lytic Proteins the Secret Weapon To Kill Staphylococcus aureus?","volume":"9","author":"D Guti\u00e9rrez","year":"2018","journal-title":"mBio"},{"issue":"2","key":"ppat.1014741.ref014","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1111\/j.1574-6976.2007.00099.x","article-title":"Bacterial peptidoglycan (murein) hydrolases","volume":"32","author":"W Vollmer","year":"2008","journal-title":"FEMS Microbiol Rev"},{"key":"ppat.1014741.ref015","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/j.sbi.2017.01.001","article-title":"Carbohydrate recognition and lysis by bacterial peptidoglycan hydrolases","volume":"44","author":"M Alcorlo","year":"2017","journal-title":"Curr Opin Struct Biol"},{"issue":"1","key":"ppat.1014741.ref016","doi-asserted-by":"crossref","first-page":"2568","DOI":"10.1038\/s41598-019-39097-2","article-title":"Identification of the first endolysin Cell Binding Domain (CBD) targeting Paenibacillus larvae","volume":"9","author":"SB Santos","year":"2019","journal-title":"Sci 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