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Infection and Immunity, April 1999, p. 2045-2049, Vol. 67, No. 4
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

beta 1-Chain Integrins Are Not Essential for Intimin-Mediated Host Cell Attachment and Enteropathogenic Escherichia coli-Induced Actin Condensation

Hui Liu, Loranne Magoun, and John M. Leong*

Department of Molecular Genetics and Microbiology, University of Massachusetts Medical Center, Worcester, Massachusetts 01655

Received 8 October 1998/Returned for modification 24 November 1998/Accepted 6 January 1999

Intimin is a bacterial outer membrane protein required for intimate attachment of enterohemorrhagic and enteropathogenic Escherichia coli (EHEC and EPEC) to mammalian cells. beta 1-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. beta 1-chain integrin antagonists or inactivation of the gene encoding the beta 1-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 beta 1-chain integrins are not essential for intimin-mediated cell attachment or EPEC-mediated actin polymerization.

* Corresponding author. Mailing address: Department of Molecular Genetics and Microbiology, University of Massachusetts Medical Center, 55 Lake Ave. North, Worcester, MA 01655. Phone: (508) 856-4059. Fax: (508) 856-5920. E-mail: john.leong{at}banyan.ummed.edu.

Infection and Immunity, April 1999, p. 2045-2049, Vol. 67, No. 4
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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