beta1-chain integrins are not essential for intimin-mediated host cell attachment and enteropathogenic Escherichia coli-induced actin condensation
Graduate School of Biomedical Sciences; Department of Molecular Genetics and Microbiology
Medical Subject Headings
Actins; *Adhesins, Bacterial; Antigens, CD29; Bacterial Adhesion; Bacterial Outer Membrane Proteins; *Carrier Proteins; Escherichia coli; *Escherichia coli Proteins; Humans; Tumor Cells, Cultured
Life Sciences | Medicine and Health Sciences
Intimin is a bacterial outer membrane protein required for intimate attachment of enterohemorrhagic and enteropathogenic Escherichia coli (EHEC and EPEC) to mammalian cells. beta1-chain integrins have been proposed as candidate receptors for intimin. We found that binding of mammalian cells to immobilized intimin was not detectable unless mammalian cells were preinfected with EPEC or EHEC. beta1-chain integrin antagonists or inactivation of the gene encoding the beta1-chain did not affect binding of preinfected mammalian cells to intimin or the actin condensation associated with the attachment of EPEC. The results indicate that beta1-chain integrins are not essential for intimin-mediated cell attachment or EPEC-mediated actin polymerization.
Rights and Permissions
Citation: Infect Immun. 1999 Apr;67(4):2045-9.
Infection and immunity
Liu, Hui; Magoun, Loranne; and Leong, John M., "beta1-chain integrins are not essential for intimin-mediated host cell attachment and enteropathogenic Escherichia coli-induced actin condensation" (1999). GSBS Student Publications. 772.