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Some gut bacteria utilize mucus as a nutrient source and can under certain conditions damage the protective barrier it forms, increasing disease susceptibility. We investigated how\n                      <jats:italic toggle=\"yes\">Ruminococcus torques\u2014<\/jats:italic>\n                      a known mucin degrader that has been implicated in inflammatory bowel diseases (IBDs)\u2014degrades mucin glycoproteins or their component\n                      <jats:italic toggle=\"yes\">O<\/jats:italic>\n                      -linked glycans to understand its effects on the availability of mucin-derived nutrients for other bacteria. We found that\n                      <jats:italic toggle=\"yes\">R. torques<\/jats:italic>\n                      utilizes both mucin glycoproteins and released oligosaccharides from gastric and colonic mucins, degrading these substrates with a panoply of mostly constitutively expressed, secreted enzymes. Investigation of mucin oligosaccharide degradation by\n                      <jats:italic toggle=\"yes\">R. torques<\/jats:italic>\n                      revealed strong \u03b1-L-fucosidase, sialidase and \u03b21,4-galactosidase activities. There was a lack of detectable sulfatase and weak \u03b21,3-galactosidase degradation, resulting in accumulation of glycans containing these structures on mucin polypeptides. While the Gram-negative symbiont,\n                      <jats:italic toggle=\"yes\">Bacteroides thetaiotaomicron<\/jats:italic>\n                      grows poorly on mucin glycoproteins, we demonstrate a clear ability of\n                      <jats:italic toggle=\"yes\">R. torques<\/jats:italic>\n                      to liberate products from mucins, making them accessible to\n                      <jats:italic toggle=\"yes\">B. thetaiotaomicron<\/jats:italic>\n                      . This work underscores the diversity of mucin-degrading mechanisms in different bacterial species and the probability that some species are contingent on others for the ability to more fully access mucin-derived nutrients. The ability of\n                      <jats:italic toggle=\"yes\">R. torques<\/jats:italic>\n                      to directly degrade a variety of mucin and mucin glycan structures and unlock released glycans for other species suggests that it is a keystone mucin degrader, which might contribute to its association with IBD.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        An important facet of maintaining healthy symbiosis between host and intestinal microbes is the mucus layer, the first defense protecting the epithelium from lumenal bacteria. Some gut bacteria degrade the various components of intestinal mucins, but detailed mechanisms used by different species are still emerging. It is imperative to understand these mechanisms as they likely dictate interspecies interactions and may illuminate species associated with bacterial mucus damage and subsequent disease susceptibility.\n                        <jats:italic toggle=\"yes\">Ruminococcus torques<\/jats:italic>\n                        is positively associated with IBD in multiple studies. We identified mucin glycan-degrading enzymes in\n                        <jats:italic toggle=\"yes\">R. torques<\/jats:italic>\n                        and found that it shares mucin degradation products with another species of gut bacteria,\n                        <jats:italic toggle=\"yes\">Bacteroides thetaiotaomicron<\/jats:italic>\n                        . Our findings underscore the importance of understanding mucin degradation mechanisms in different gut bacteria and their consequences on interspecies interactions, which may identify keystone bacteria that disproportionately affect mucus damage and could therefore be key players in effects that result from reductions in mucus integrity.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/mbio.00039-24","type":"journal-article","created":{"date-parts":[[2024,7,8]],"date-time":"2024-07-08T09:01:14Z","timestamp":1720429274000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":120,"title":["<i>Ruminococcus torques<\/i>\n                    is a keystone degrader of intestinal mucin glycoprotein, releasing oligosaccharides used by\n                    <i>Bacteroides thetaiotaomicron<\/i>"],"prefix":"10.1128","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2037-5913","authenticated-orcid":false,"given":"Sadie R.","family":"Schaus","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology, University of Michigan","place":["Ann Arbor, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7937-474X","authenticated-orcid":false,"given":"Gabriel","family":"Vasconcelos Pereira","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, University of Michigan","place":["Ann Arbor, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana S.","family":"Luis","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, University of Michigan","place":["Ann Arbor, USA"]},{"name":"Department of Medical Biochemistry and Cell Biology, University of Gothenburg","place":["Gothenburg, 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