{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T02:23:14Z","timestamp":1777515794320,"version":"3.51.4"},"reference-count":0,"publisher":"American Society for Microbiology","issue":"11","license":[{"start":{"date-parts":[[1992,11,1]],"date-time":"1992-11-01T00:00:00Z","timestamp":720576000000},"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":["Infect Immun"],"published-print":{"date-parts":[[1992,11]]},"abstract":"<jats:p>Escherichia coli and other members of the family Enterobacteriaceae express surface fibrillar structures, fimbriae, that promote bacterial adhesion to host receptors. Type 1 fimbriae possess a lectinlike component, FimH, that is commonly thought to cause binding to mannose-containing oligosaccharides of host receptors. Since adhesion of type 1 fimbriated organisms are inhibited by mannose, the reactions are described as mannose sensitive (MS). We have studied the adhesion of the type 1 fimbriated CSH-50 strain of E. coli (which expresses only type 1 fimbriae) to fibronectin (FN). E. coli CSH-50 does not bind detectable amounts of soluble FN but adheres well to immobilized plasma or cellular FN. This adhesion was inhibited by mannose-containing saccharides. By using purified domains of FN, it was found that E. coli CSH-50 adheres primarily to the amino-terminal and gelatin-binding domains, only one of which is glycosylated, in an MS fashion. Binding of the mannose-specific lectin concanavalin A to FN and ovalbumin was eliminated or reduced, respectively, by incubation with periodate or endoglycosidase. Adhesion of E. coli CSH-50 to ovalbumin was reduced by these treatments, but adhesion to FN was unaffected. E. coli CSH-50 also adheres to a synthetic peptide copying a portion of the amino-terminal FN domain (FNsp1) in an MS fashion. Purified CSH-50 fimbriae bound to immobilized FN and FNsp1 in an MS fashion and inhibited adhesion of intact organisms. However, fimbriae purified from HB101 (pPKL4), a recombinant strain harboring the entire type 1 fim gene locus and expressing functional type 1 fimbriae, neither bound to FN or FNsp1 nor inhibited E. coli adhesion to immobilized FN or FNsp1. These novel findings suggest that there are two forms of type 1 MS fimbriae. One form exhibits only the well-known MS lectinlike activity that requires a substratum of mannose-containing glycoproteins. The other form exhibits not only the MS lectinlike activity but also binds to nonglycosylated regions of proteins in an MS manner.<\/jats:p>","DOI":"10.1128\/iai.60.11.4709-4719.1992","type":"journal-article","created":{"date-parts":[[2020,1,3]],"date-time":"2020-01-03T13:27:12Z","timestamp":1578058032000},"page":"4709-4719","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":78,"title":["Functional heterogeneity of type 1 fimbriae of Escherichia coli"],"prefix":"10.1128","volume":"60","author":[{"given":"E V","family":"Sokurenko","sequence":"first","affiliation":[{"name":"Department of Anatomy and Neurobiology, University of Tennessee, Memphis 38104."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"H S","family":"Courtney","sequence":"additional","affiliation":[{"name":"Department of Anatomy and Neurobiology, University of Tennessee, Memphis 38104."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"S N","family":"Abraham","sequence":"additional","affiliation":[{"name":"Department of Anatomy and Neurobiology, University of Tennessee, Memphis 38104."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"P","family":"Klemm","sequence":"additional","affiliation":[{"name":"Department of Anatomy and Neurobiology, University of Tennessee, Memphis 38104."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"D L","family":"Hasty","sequence":"additional","affiliation":[{"name":"Department of Anatomy and Neurobiology, University of Tennessee, Memphis 38104."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","container-title":["Infection and Immunity"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/iai.60.11.4709-4719.1992","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/iai.60.11.4709-4719.1992","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,3,4]],"date-time":"2022-03-04T23:23:35Z","timestamp":1646436215000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/iai.60.11.4709-4719.1992"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1992,11]]},"references-count":0,"journal-issue":{"issue":"11","published-print":{"date-parts":[[1992,11]]}},"alternative-id":["10.1128\/iai.60.11.4709-4719.1992"],"URL":"https:\/\/doi.org\/10.1128\/iai.60.11.4709-4719.1992","relation":{},"ISSN":["0019-9567","1098-5522"],"issn-type":[{"value":"0019-9567","type":"print"},{"value":"1098-5522","type":"electronic"}],"subject":[],"published":{"date-parts":[[1992,11]]},"assertion":[{"value":"1992-11-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}