GSBS Student Publications


beta1-chain integrins are not essential for intimin-mediated host cell attachment and enteropathogenic Escherichia coli-induced actin condensation

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Molecular Genetics and Microbiology



Document Type


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.

Related Resources

Link to article in PubMed

Journal Title

Infection and immunity

PubMed ID