Elsevier

Virology

Volume 332, Issue 2, 20 February 2005, Pages 511-518
Virology

Heparin binding sites on Ross River virus revealed by electron cryo-microscopy

https://doi.org/10.1016/j.virol.2004.11.043Get rights and content
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Abstract

Cell surface glycosaminoglycans play important roles in cell adhesion and viral entry. Laboratory strains of two alphaviruses, Sindbis and Semliki Forest virus, have been shown to utilize heparan sulfate as an attachment receptor, whereas Ross River virus (RRV) does not significantly interact with it. However, a single amino acid substitution at residue 218 in the RRV E2 glycoprotein adapts the virus to heparan sulfate binding and expands the host range of the virus into chicken embryo fibroblasts. Structures of the RRV mutant, E2 N218R, and its complex with heparin were determined through the use of electron cryo-microscopy and image reconstruction methods. Heparin was found to bind at the distal end of the RRV spikes, in a region of the E2 glycoprotein that has been previously implicated in cell-receptor recognition and antibody binding.

Keywords

Alphavirus
Ross River virus
Heparan sulfate
Heparin
Electron cryo-microscopy
GAG
Three-dimensional reconstruction

Cited by (0)

1

Present address: Department of Microbiology, The University of Alabama at Birmingham, Birmingham, AL 35294-2170, USA.

2

Present address: Department of Chemistry and Biochemistry, University of California at San Diego, 9500 Gilman Drive #0378, La Jolla, CA 92093-0378, USA.