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J. Biol. Chem., Vol. 276, Issue 3, 2200-2211, January 19, 2001
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From the Departments of Many serotype 3 reoviruses bind to two different
host cell molecules, sialic acid and an unidentified protein, using
discrete receptor-binding domains in viral attachment protein,
Utilization of Sialic Acid as a Coreceptor Enhances Reovirus
Attachment by Multistep Adhesion Strengthening*
§,§,§,§¶
Microbiology and Immunology
and ¶ Pediatrics and the § Elizabeth B. Lamb Center for
Pediatric Research, Vanderbilt University School of Medicine,
Nashville, Tennessee 37232-2581
1. To
determine mechanisms by which these receptor-binding events cooperate
to mediate cell attachment, we generated isogenic reovirus strains that
differ in the capacity to bind sialic acid. Strain SA+, but not SA
,
bound specifically to sialic acid on a biosensor chip with nanomolar
avidity. SA+ displayed 5-fold higher avidity for HeLa cells when
compared with SA, although both strains recognized the same
proteinaceous receptor. Increased avidity of SA+ binding was mediated
by increased kon. Neuraminidase treatment to
remove cell-surface sialic acid decreased the
kon of SA+ to that of SA. Increased
kon of SA+ enhanced an infectious attachment
process, since SA+ was 50-100-fold more efficient than SA at
infecting HeLa cells in a kinetic fluorescent focus assay. Sialic acid
binding was operant early during SA+ attachment, since the capacity of soluble sialyllactose to inhibit infection decreased rapidly during the
first 20 min of adsorption. These results indicate that reovirus binding to sialic acid enhances virus infection through adhesion of
virus to the cell surface where access to a proteinaceous receptor is
thermodynamically favored.
*
This work was supported by Public Health Service award
AI38296 from the NIAID, National Institutes of Health (NIH) and the National Science Foundation (to E. S. B.), the Vanderbilt University Research Council (to E. S. B. and J. C. F.), and the Elizabeth B. Lamb Center for Pediatric Research. Additional support was provided by
Public Health Service awards CA68485 (to the Vanderbilt Cancer Center),
DK20593 (to the Vanderbilt Diabetes Research and Training Center), and
NCI, NIH, Grant T32 CA09385 (to J. C. F).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Lamb Center for
Pediatric Research, D7235 MCN, Vanderbilt University School of Medicine, Nashville, TN 37232. Tel.: 615-343-9943; Fax: 615-343-9723; E-mail: terry.dermody@mcmail.vanderbilt.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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