{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"institution":[{"name":"bioRxiv"}],"indexed":{"date-parts":[[2026,3,27]],"date-time":"2026-03-27T20:06:04Z","timestamp":1774641964427,"version":"3.50.1"},"posted":{"date-parts":[[2026,3,24]]},"group-title":"Microbiology","reference-count":79,"publisher":"openRxiv","license":[{"start":{"date-parts":[[2026,3,24]],"date-time":"2026-03-24T00:00:00Z","timestamp":1774310400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.biorxiv.org\/about\/FAQ#license"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["R01DK136875"],"award-info":[{"award-number":["R01DK136875"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000928","name":"Welch Foundation","doi-asserted-by":"crossref","award":["AT-2030-20200401"],"award-info":[{"award-number":["AT-2030-20200401"]}],"id":[{"id":"10.13039\/100000928","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2026,3,24]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                <jats:p>\n                  To establish infection, uropathogens must overcome several host defenses including the glycosaminoglycan (GAG) layer coating the apical surface of the bladder urothelium. GAGs are thought to protect against urinary tract infection (UTI) by serving as scaffolding sites for commensals, providing barrier function and preventing uropathogen adherence. However, the ability of uropathogens to degrade and utilize GAGs and the contribution of these activities toward UTI progression is largely unknown. We previously discovered that the uropathogen\n                  <jats:italic>Proteus mirabilis,<\/jats:italic>\n                  a common cause of catheter-associated UTI (CAUTI), degrades the GAG chondroitin sulfate (CS). In this study we sought to define the kinetics and regulation of CS degradation by diverse\n                  <jats:italic>P. mirabilis<\/jats:italic>\n                  strains clinically isolated from both recurrent UTI and CAUTI patients. We found variation in CS degradation kinetics between\n                  <jats:italic>P. mirabilis<\/jats:italic>\n                  strains and media types. However, CS degradation depended on conserved putative chondroitin sulfate ABC endo- and exolyases in all strains. Furthermore, we found that CS degradation in Pm123 was repressed by urea and that this repression was dependent on\n                  <jats:italic>P. mirabilis<\/jats:italic>\n                  urease activity. Complementation of the Pm123 endolyase into urea-insensitive HI4320 resulted in a urea-sensitive CS degradation phenotype suggesting functional differences between the Pm123 and HI4320 endolyases. Sequence alignment and structural modeling analysis identified two unique point mutations within the Pm123 endolyase that may contribute to urea sensitivity. Finally, unlike urea-insensitive\n                  <jats:italic>P. mirabilis<\/jats:italic>\n                  strains, Pm123 demonstrated attenuated swarming and loss of chondroitin endolyase activity had no effect on Pm123 virulence in a mouse CAUTI model. Our results suggest that the kinetics and regulation of CS degradation differ between\n                  <jats:italic>P. mirabilis<\/jats:italic>\n                  strains and in urea-sensitive strains, thus reduces the contribution of CS degradation to urovirulence during murine CAUTI.\n                <\/jats:p>\n                <jats:sec>\n                  <jats:title>Importance<\/jats:title>\n                  <jats:p>\n                    This work demonstrates that the ability to degrade a common component of bladder mucosal surfaces, chondroitin sulfate, is a phenotype that is shared by multiple strains of the common catheter-associated UTI (CAUTI) pathogen\n                    <jats:italic>P. mirabilis<\/jats:italic>\n                    . We find that this activity is dependent on encoded chondroitin ABC endo- and exolyases, first described in\n                    <jats:italic>Proteus vulgaris<\/jats:italic>\n                    . Additionally, we discovered that for\n                    <jats:italic>P. mirabilis<\/jats:italic>\n                    strain Pm123, degradation of CS is negatively regulated by the presence of urea, a major component of urine. The repression of CS degradation by urea is dependent on the activity of the\n                    <jats:italic>P. mirabilis<\/jats:italic>\n                    urease enzyme, which breaks down urea producing ammonia which raises pH. We found expression of the Pm123 CS endolyase was sufficient to confer a urea-sensitive CS-degradation phenotype and identified two unique mutations within the Pm123 enzyme that may contribute to urea sensitivity. Finally, we find that while CS-degradation plays a role in progression and severity of murine CAUTI model in urea-insensitive\n                    <jats:italic>P. mirabilis,<\/jats:italic>\n                    there was not significant difference in CAUTI outcomes between the urea-sensitive Pm123 wild-type and chondroitinase knockout strains. This study represents a major step forward in understanding the diversity of CS degradation activity and regulation among clinical strains of the critically important CAUTI pathogen\n                    <jats:italic>P. mirabilis<\/jats:italic>\n                    as well as its contribution to urovirulence.\n                  <\/jats:p>\n                <\/jats:sec>","DOI":"10.64898\/2026.03.23.713754","type":"posted-content","created":{"date-parts":[[2026,3,24]],"date-time":"2026-03-24T15:26:47Z","timestamp":1774366007000},"source":"Crossref","is-referenced-by-count":0,"title":["Strain level variation in\n                  <i>Proteus mirabilis<\/i>\n                  chondroitin sulfate degradation kinetics and regulation by urea"],"prefix":"10.64898","author":[{"given":"Brianna M.","family":"Shipman","sequence":"first","affiliation":[{"name":"Department of Biological Sciences, The University of Texas at Dallas, Richardson TX"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Serena","family":"Zhou","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, The University of Texas at Dallas, Richardson TX"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Benjamin","family":"Hunt","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, State University of New York at Buffalo, Buffalo, New York"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Vitus","family":"Brix","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, State University of New York at Buffalo, Buffalo, New York"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ibrahim","family":"Salaudeen","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, The University of Texas at Dallas, Richardson TX"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anna N.","family":"Evers","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, The University of Texas at Dallas, Richardson TX"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Brian S.","family":"Learman","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, State University of New York at Buffalo, Buffalo, New York"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nicholas A.","family":"Dillon","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, The University of Texas at Dallas, Richardson TX"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Philippe E.","family":"Zimmern","sequence":"additional","affiliation":[{"name":"Department of Urology, The University of Texas Southwestern Medical Center, Dallas TX"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chelsie E.","family":"Armbruster","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, State University of New York at Buffalo, Buffalo, New York"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7670-5301","authenticated-orcid":false,"given":"Nicole J.","family":"De Nisco","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, The University of Texas at Dallas, Richardson TX"},{"name":"Department of Urology, The University of Texas Southwestern Medical Center, Dallas TX"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"54368","reference":[{"key":"2026032712450570000_2026.03.23.713754v1.1","doi-asserted-by":"publisher","DOI":"10.1056\/NEJMcp1104429"},{"key":"2026032712450570000_2026.03.23.713754v1.2","doi-asserted-by":"publisher","DOI":"10.1007\/s11908-008-0081-0"},{"key":"2026032712450570000_2026.03.23.713754v1.3","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1038\/s41585-025-01065-z","article-title":"CAUTIon \u2014 not all UTIs are the same","volume":"22","year":"2025","journal-title":"Nat Rev Urol"},{"key":"2026032712450570000_2026.03.23.713754v1.4","doi-asserted-by":"publisher","DOI":"10.1086\/675718"},{"key":"2026032712450570000_2026.03.23.713754v1.5","doi-asserted-by":"crossref","unstructured":"Letica-kriegel AS , Salmasian H , Vawdrey DK , Youngerman BE , Green RA , Furuya EY , Calfee DP . 2019. 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