Title
beta1-chain integrins are not essential for intimin-mediated host cell attachment and enteropathogenic Escherichia coli-induced actin condensation
Academic Program
Biochemistry & Molecular Pharmacology
UMMS Affiliation
Graduate School of Biomedical Sciences; Department of Molecular Genetics and Microbiology
Publication Date
1999-03-20
Document Type
Article
Disciplines
Life Sciences | Medicine and Health Sciences
Abstract
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.
Source
Infect Immun. 1999 Apr;67(4):2045-9.
Journal/Book/Conference Title
Infection and immunity
Related Resources
PubMed ID
10085058
Repository Citation
Liu H, Magoun L, Leong JM. (1999). beta1-chain integrins are not essential for intimin-mediated host cell attachment and enteropathogenic Escherichia coli-induced actin condensation. GSBS Student Publications. Retrieved from https://escholarship.umassmed.edu/gsbs_sp/772