The cell-binding domain of intimin from enteropathogenic Escherichia coli binds to β1 integrins

Gad Frankel*, Ofer Lider, Rami Hershkoviz, A. Paul Mould, Sylvia G. Kachalsky, David C.A. Candy, Liora Cahalon, Martin J. Humphries, Gordon Dougan

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Bacteria interact with mammalian cells surface molecules, such as integrins, to colonize tissues and evade immunological detection. Herein, the ability of intimin, an outer membrane protein from enteropathogenic Escherichia coli, to bind β1 integrins was investigated. Solid-phase binding assays revealed binding of the carboxyl-terminal 280 amino acids of intimin (Int280) to α4β1 and α5β1 integrins. The binding required divalent ions (in particular, it was enhanced by Mn2+) and was inhibited by an RGD-containing peptide. Nonderivatized Int280, but not Int280CS (like Int280 but with Cys-937 replaced by Ser) blocked the binding of biotinylated Int280 to integrins. Int280 did not efficiently inhibit β1 integrin binding of invasin from Yersinia pseudotuberculosis. Both intimin and invasin, immobilized on plastic surfaces, mediated adherence of resting or phorbol 12- myristate 13-acetate-activated human CD4+ T cells, whereas fibronectin mediated the adherence of only activated T cells. T cell binding to intimin and invasin was integrin mediated because it was specifically blocked by an RGD-containing peptide and by antibodies directed against the integrin subunits β1, α4, and α5. These results demonstrate a specific integrin binding activity for intimin that is related to, but distinct from, that of invasin.

Original languageEnglish
Pages (from-to)20359-20364
Number of pages6
JournalJournal of Biological Chemistry
Issue number34
StatePublished - 1996
Externally publishedYes


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