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Infection and Immunity, July 1999, p. 3302-3307, Vol. 67, No. 7
Department of Medical Microbiology and Immunology,
University of Alberta, Edmonton, Alberta T6G 2H7, Canada
Received 23 December 1998/Returned for modification 24 February
1999/Accepted 12 April 1999
Previously, we found that asialo-lactosamine sequences served as
receptors for enteropathogenic Escherichia coli (EPEC)
binding to Chinese hamster ovary (CHO) cells. In the present report, we have extended these earlier results by examining the ability of lactosamine- or fucosylated lactosamine-bovine serum albumin (BSA) glycoconjugates to inhibit EPEC, strain E2348/69, binding to HEp-2 cells. We found that, consistent with our previous findings with CHO
cells, N-acetyllactosamine-BSA was the most effective
inhibitor of EPEC localized adherence to HEp-2 cells, with Lewis X-BSA
being the next best inhibitor. Further investigation revealed that
coincubating EPEC E2348/69 with these BSA glycoconjugates alone caused
a decrease in the expression of the bundle-forming pilus structural
subunit (BfpA) and intimin by the bacteria. BfpA and intimin expression were reduced to the greatest extent by
N-acetyllactosamine-BSA and Lewis X-BSA, respectively.
These results suggest that the glycoconjugate inhibition of EPEC
binding to HEp-2 cells might be achieved, wholly or in part, by an
active mechanism that is distinct from simple competitive antagonism of
receptor-adhesin interactions.
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Role of Lactosyl Glycan Sequences in Inhibiting
Enteropathogenic Escherichia coli Attachment
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Corresponding author. Mailing address: Medical
Microbiology and Immunology, 1-21 Medical Sciences Bldg., University of
Alberta, Edmonton, Alberta T6G 2H7, Canada. Phone: (780) 492-2303. Fax: (780) 492-7521. E-mail: glen.armstrong{at}ualberta.ca.
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