{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,30]],"date-time":"2026-06-30T14:43:00Z","timestamp":1782830580326,"version":"3.54.5"},"reference-count":63,"publisher":"American Society for Microbiology","issue":"24","license":[{"start":{"date-parts":[[2013,12,15]],"date-time":"2013-12-15T00:00:00Z","timestamp":1387065600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2013,12,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Type 3 fimbriae are adhesive organelles found in enterobacterial pathogens. The fimbriae promote biofilm formation on biotic and abiotic surfaces; however, the exact identity of the receptor for the type 3 fimbriae adhesin, MrkD, remains elusive. We analyzed naturally occurring structural and functional variabilities of the MrkD adhesin from\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Klebsiella pneumoniae<\/jats:named-content>\n            and\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Escherichia coli<\/jats:named-content>\n            isolates of diverse origins. We identified a total of 33 allelic variants of\n            <jats:italic>mrkD<\/jats:italic>\n            among 90\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">K. pneumoniae<\/jats:named-content>\n            isolates and 10 allelic variants among 608\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. coli<\/jats:named-content>\n            isolates, encoding 11 and 9 protein variants, respectively. Based on the level of accumulated silent variability between the alleles,\n            <jats:italic>mrkD<\/jats:italic>\n            was acquired a relatively long time ago in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">K. pneumoniae<\/jats:named-content>\n            but recently in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. coli<\/jats:named-content>\n            . However, unlike\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">K. pneumoniae<\/jats:named-content>\n            ,\n            <jats:italic>mrkD<\/jats:italic>\n            in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. coli<\/jats:named-content>\n            is actively evolving under a strong positive selection by accumulation of mutations, often targeting the same positions in the protein. Several naturally occurring MrkD protein variants from\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. coli<\/jats:named-content>\n            were found to be significantly less adherent when tested in a mannan-binding assay and showed reduced biofilm-forming capacity. Functional examination of the MrkD adhesin in flow chamber experiments determined that it interacts with\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Saccharomyces cerevisiae<\/jats:named-content>\n            cells in a shear-dependent manner, i.e., the binding is catch-bond-like and enhanced under increasing shear conditions. Homology modeling strongly suggested that MrkD has a two-domain structure, comprising a pilin domain anchoring the adhesin to the fimbrial shaft and a lectin domain containing the binding pocket; this is similar to structures found in other catch-bond-forming fimbrial adhesins in enterobacteria.\n          <\/jats:p>","DOI":"10.1128\/jb.00753-13","type":"journal-article","created":{"date-parts":[[2013,10,12]],"date-time":"2013-10-12T01:21:53Z","timestamp":1381540913000},"page":"5602-5613","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":29,"title":["Structural and Population Characterization of MrkD, the Adhesive Subunit of Type 3 Fimbriae"],"prefix":"10.1128","volume":"195","author":[{"given":"Steen G.","family":"Stahlhut","sequence":"first","affiliation":[{"name":"Department of Microbiology and Infection Control, Statens Serum Institut, Copenhagen, Denmark"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sujay","family":"Chattopadhyay","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Washington School of Medicine, Seattle, Washington, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dagmara I.","family":"Kisiela","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Washington School of Medicine, Seattle, Washington, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kristian","family":"Hvidtfeldt","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Infection Control, Statens Serum Institut, Copenhagen, Denmark"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven","family":"Clegg","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Iowa College of Medicine, Iowa City, Iowa, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carsten","family":"Struve","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Infection Control, Statens Serum Institut, Copenhagen, Denmark"},{"name":"WHO Collaborating Centre for Reference and Research on Escherichia and Klebsiella, Statens Serum Institut, Copenhagen, Denmark"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Evgeni V.","family":"Sokurenko","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Washington School of Medicine, Seattle, Washington, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karen A.","family":"Krogfelt","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Infection Control, Statens Serum Institut, Copenhagen, Denmark"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.38.1.306-315.1982"},{"key":"e_1_3_2_3_2","first-page":"2175","article-title":"Fimbrial haemagglutinins in Enterobacter species","volume":"129","author":"Adegbola RA","year":"1983","unstructured":"AdegbolaRAOldDC. 1983. 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