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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.
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.
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.
1-chain integrin antagonists or inactivation of the gene
encoding the
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
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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