Binding of Sindbis virus to cell surface heparan sulfate

Andrew P. Byrnes, Diane Griffin

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)7349-7356
Number of pages8
JournalJournal of Virology
Volume72
Issue number9
StatePublished - Sep 1998

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Sindbis virus
Sindbis Virus
Heparitin Sulfate
Alphavirus
heparin
cells
Heparin
Ross River virus
Arboviruses
Virus Attachment
Tropism
tissue tropism
Cell Surface Receptors
arboviruses
receptors
Neutralizing Antibodies
Glycosaminoglycans
glycosaminoglycans
Glycoproteins
neutralizing antibodies

ASJC Scopus subject areas

  • Immunology

Cite this

Binding of Sindbis virus to cell surface heparan sulfate. / Byrnes, Andrew P.; Griffin, Diane.

In: Journal of Virology, Vol. 72, No. 9, 09.1998, p. 7349-7356.

Research output: Contribution to journalArticle

Byrnes, Andrew P. ; Griffin, Diane. / Binding of Sindbis virus to cell surface heparan sulfate. In: Journal of Virology. 1998 ; Vol. 72, No. 9. pp. 7349-7356.
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