{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,9]],"date-time":"2026-03-09T04:05:42Z","timestamp":1773029142025,"version":"3.50.1"},"reference-count":54,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2026,2,15]],"date-time":"2026-02-15T00:00:00Z","timestamp":1771113600000},"content-version":"vor","delay-in-days":14,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,2,1]],"date-time":"2026-02-01T00:00:00Z","timestamp":1769904000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["APMIS"],"published-print":{"date-parts":[[2026,2]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>Streptococcus pneumoniae<\/jats:italic>\n                    <\/jats:styled-content>\n                    , which imposes the highest burden on children under 2\u2009years of age, immunocompromised individuals and the elderly in developing countries, causes a range of diseases including pneumonia, meningitis, bacteraemia and septicaemia. Its virulence is driven by an array of surface proteins categorised into four families: non\u2010classical surface proteins, LPXTG\u2010sequence proteins, lipoproteins and choline\u2010binding proteins. The different choline\u2010binding proteins include LytA, LytB, LytC, PspA, CbpA, CbpD, CbpL and CbpF, each with varying numbers of choline\u2010binding repeats in their domains. This review focuses on \u03b2\u2010endo\u2010acetylglucosaminidase (LytB), a non\u2010autolytic peptidoglycan hydrolase, emphasising its pivotal role in the pathogenic mechanisms of\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>S. pneumoniae<\/jats:italic>\n                    <\/jats:styled-content>\n                    . LytB, with its multiple functional domains (CB, SH3B, WW and GH73), facilitates adhesion to host tissues, promoting initial colonisation, immune evasion and subsequent bacterial dissemination. These functions enable the bacterium to establish invasive diseases. LytB's interactions with host cells and extracellular matrix components underscore its importance in\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>S. pneumoniae<\/jats:italic>\n                    <\/jats:styled-content>\n                    pathogenicity. In summary, LytB is a multifaceted choline\u2010binding protein critical to pneumococcal virulence. A detailed understanding of its mechanisms and domain\u2010specific interactions offers promising avenues for the development of novel chemical and plant\u2010based therapeutic strategies, including drugs and vaccines, to combat pneumococcal infections.\n                  <\/jats:p>","DOI":"10.1111\/apm.70162","type":"journal-article","created":{"date-parts":[[2026,2,16]],"date-time":"2026-02-16T09:22:43Z","timestamp":1771233763000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Pathogenic Role of \u03b2\u2010Endo\u2010N\u2010Acetylglucosaminidase (\n                    <scp>LytB<\/scp>\n                    ) in\n                    <scp>\n                      <i>Streptococcus pneumoniae<\/i>\n                    <\/scp>\n                    : Functional Insights Into a Choline\u2010Binding Cell Wall Hydrolase"],"prefix":"10.1111","volume":"134","author":[{"ORCID":"https:\/\/orcid.org\/0009-0005-7375-0421","authenticated-orcid":false,"family":"Divya","sequence":"first","affiliation":[{"name":"Department of Biotechnology Motilal Nehru National Institute of Technology Allahabad  Uttar Pradesh India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7982-5026","authenticated-orcid":false,"given":"Anjana","family":"Pandey","sequence":"additional","affiliation":[{"name":"Department of Biotechnology Motilal Nehru National Institute of Technology Allahabad  Uttar Pradesh India"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2026,2,15]]},"reference":[{"key":"e_1_2_15_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0140-6736(09)61114-4"},{"key":"e_1_2_15_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0140-6736(09)61204-6"},{"key":"e_1_2_15_4_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.2041-1014.2012.00655.x"},{"key":"e_1_2_15_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.ab.2011.11.026"},{"key":"e_1_2_15_6_1","doi-asserted-by":"publisher","DOI":"10.1089\/mdr.2012.0026"},{"key":"e_1_2_15_7_1","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro2677"},{"key":"e_1_2_15_8_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2011.07871.x"},{"key":"e_1_2_15_9_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6976.2007.00099.x"},{"key":"e_1_2_15_10_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1997.4101774.x"},{"key":"e_1_2_15_11_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2003.03945.x"},{"key":"e_1_2_15_12_1","doi-asserted-by":"publisher","DOI":"10.4049\/jimmunol.127.4.1287"},{"key":"e_1_2_15_13_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.67.5.2327-2333.1999"},{"key":"e_1_2_15_14_1","doi-asserted-by":"publisher","DOI":"10.3390\/vaccines9020181"},{"key":"e_1_2_15_15_1","doi-asserted-by":"publisher","DOI":"10.3390\/vaccines9020181"},{"key":"e_1_2_15_16_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.68.10.5690-5695.2000"},{"key":"e_1_2_15_17_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M910189199"},{"key":"e_1_2_15_18_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)42162-5"},{"key":"e_1_2_15_19_1","volume-title":"Peptidoglycan Hydrolases: Sub\u2010Cellular Localization of Pneumococcal LytA and LytB (Doctoral Dissertation)","author":"Pedroso R. 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