[HTML][HTML] The cell-binding domain of intimin from enteropathogenic Escherichia coli binds to β1 integrins
G Frankel, O Lider, R Hershkoviz, AP Mould… - Journal of Biological …, 1996 - ASBMB
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 β 1 integrins was
investigated. Solid-phase binding assays revealed binding of the carboxyl-terminal 280
amino acids of intimin (Int280) to α 4 β 1 and α 5 β 1 integrins. The binding required divalent
ions (in particular, it was enhanced by Mn 2+) and was inhibited by an RGD-containing …
tissues and evade immunological detection. Herein, the ability of intimin, an outer
membrane protein from enteropathogenic Escherichia coli, to bind β 1 integrins was
investigated. Solid-phase binding assays revealed binding of the carboxyl-terminal 280
amino acids of intimin (Int280) to α 4 β 1 and α 5 β 1 integrins. The binding required divalent
ions (in particular, it was enhanced by Mn 2+) and was inhibited by an RGD-containing …