Functional heterogeneity of type 1 fimbriae of Escherichia coli

E. V. Sokurenko, H. S. Courtney, S. N. Abraham, P. Klemm, D. L. Hasty

Research output: Contribution to journalArticle

68 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)4709-4719
Number of pages11
JournalInfection and Immunity
Volume60
Issue number11
StatePublished - 1992

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Mannose
Fibronectins
Escherichia coli
Ovalbumin
Mannose-Binding Lectins
Bacterial Adhesion
Glycoside Hydrolases
Enterobacteriaceae
Gelatin
Concanavalin A
Oligosaccharides
Glycoproteins

All Science Journal Classification (ASJC) codes

  • Immunology

Cite this

Sokurenko, E. V., Courtney, H. S., Abraham, S. N., Klemm, P., & Hasty, D. L. (1992). Functional heterogeneity of type 1 fimbriae of Escherichia coli. Infection and Immunity, 60(11), 4709-4719.

Functional heterogeneity of type 1 fimbriae of Escherichia coli. / Sokurenko, E. V.; Courtney, H. S.; Abraham, S. N.; Klemm, P.; Hasty, D. L.

In: Infection and Immunity, Vol. 60, No. 11, 1992, p. 4709-4719.

Research output: Contribution to journalArticle

Sokurenko, EV, Courtney, HS, Abraham, SN, Klemm, P & Hasty, DL 1992, 'Functional heterogeneity of type 1 fimbriae of Escherichia coli', Infection and Immunity, vol. 60, no. 11, pp. 4709-4719.
Sokurenko EV, Courtney HS, Abraham SN, Klemm P, Hasty DL. Functional heterogeneity of type 1 fimbriae of Escherichia coli. Infection and Immunity. 1992;60(11):4709-4719.
Sokurenko, E. V. ; Courtney, H. S. ; Abraham, S. N. ; Klemm, P. ; Hasty, D. L. / Functional heterogeneity of type 1 fimbriae of Escherichia coli. In: Infection and Immunity. 1992 ; Vol. 60, No. 11. pp. 4709-4719.
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