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Journal of Virology, September 1998, p. 7349-7356, Vol. 72, No. 9
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Binding of Sindbis Virus to Cell Surface
Heparan Sulfate
Andrew P.
Byrnes1 and
Diane E.
Griffin1,2,*
Departments of Molecular Microbiology and
Immunology1 and
Medicine and
Neurology,2 Johns Hopkins University School
of Hygiene and Public Health, Baltimore, Maryland 21205
Received 26 February 1998/Accepted 5 June 1998
Alphaviruses are arthropod-borne viruses with wide species ranges
and diverse tissue tropisms. The cell surface receptors which allow
infection of so many different species and cell types are still
incompletely characterized. We show here that the widely expressed
glycosaminoglycan heparan sulfate can participate in the binding of
Sindbis virus to cells. Enzymatic removal of heparan sulfate or the use
of heparan sulfate-deficient cells led to a large reduction in virus
binding. Sindbis virus bound to immobilized heparin, and this
interaction was blocked by neutralizing antibodies against the viral E2
glycoprotein. Further experiments showed that a high degree of
sulfation was critical for the ability of heparin to bind Sindbis
virus. However, Sindbis virus was still able to infect and replicate on
cells which were completely deficient in heparan sulfate, indicating
that additional receptors must be involved. Cell surface binding of
another alphavirus, Ross River virus, was found to be independent of
heparan sulfate.
*
Corresponding author. Mailing address: Department of
Molecular Microbiology and Immunology, Johns Hopkins University School of Hygiene and Public Health, 615 N. Wolfe St., Baltimore, MD 21205. Phone: (410) 955-3459. Fax: (410) 955-0105. E-mail:
dgriffin{at}welchlink.welch.jhu.edu.
Journal of Virology, September 1998, p. 7349-7356, Vol. 72, No. 9
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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