{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,25]],"date-time":"2026-02-25T17:07:21Z","timestamp":1772039241460,"version":"3.50.1"},"reference-count":30,"publisher":"Microbiology Society","issue":"2","license":[{"start":{"date-parts":[[2026,2,25]],"date-time":"2026-02-25T00:00:00Z","timestamp":1771977600000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"crossref","award":["RGPIN-2021-03208"],"award-info":[{"award-number":["RGPIN-2021-03208"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"crossref"}]},{"name":"National Science Foundation","award":["EFMA-2223785"],"award-info":[{"award-number":["EFMA-2223785"]}]},{"DOI":"10.13039\/100000009","name":"Foundation for the National Institutes of Health","doi-asserted-by":"crossref","award":["R01GM130971"],"award-info":[{"award-number":["R01GM130971"]}],"id":[{"id":"10.13039\/100000009","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,2,25]]},"abstract":"<jats:p>\n                    The bacterial cell wall is a covalently linked meshwork of peptidoglycan (PG) that helps maintain cell shape and prevents osmotic lysis. This structure must be flexible enough to accommodate transenvelope protein complexes, but strong enough to withstand high intracellular pressure. To elongate and divide, cells must remodel the cell wall through the concerted action of PG synthesis and degradation. Endopeptidases, a class of PG-degrading enzymes, facilitate cell growth by hydrolysing PG crosslinks.\n                    <jats:italic>Vibrio cholerae<\/jats:italic>\n                    encodes several functionally redundant endopeptidases, two of which are nearly identical: ShyA and ShyC. To investigate the differential roles of these enzymes, we assessed the growth and morphology\n                    <jats:italic>of shyA<\/jats:italic>\n                    and\n                    <jats:italic>shyC<\/jats:italic>\n                    mutants. We found that native levels of ShyA, but not ShyC, facilitate adaptation to low-osmolarity medium. Cells lacking\n                    <jats:italic>shyA<\/jats:italic>\n                    exhibited a longer lag phase and aberrant morphology during adaptation. Lastly, our experiments revealed that cells lacking ShyA\u2019s LysM domain exhibited more severe defects than cells lacking\n                    <jats:italic>shyA<\/jats:italic>\n                    altogether, implicating the LysM domain in the proper regulation of ShyA activity.\n                  <\/jats:p>","DOI":"10.1099\/mic.0.001671","type":"journal-article","created":{"date-parts":[[2026,2,25]],"date-time":"2026-02-25T16:16:50Z","timestamp":1772036210000},"source":"Crossref","is-referenced-by-count":0,"title":["Differential endopeptidase requirements during adaptation to changing growth conditions in Vibrio cholerae"],"prefix":"10.1099","volume":"172","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6416-1730","authenticated-orcid":false,"given":"Kelly","family":"Rosch","sequence":"first","affiliation":[{"name":"Department of Molecular Biology and Genetics, Cornell University, Ithaca, USA"},{"name":"Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, 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