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Journal of Virology, October 2001, p. 9274-9281, Vol. 75, No. 19
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.19.9274-9281.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Evidence that Equine Rhinitis A Virus VP1 Is a Target of Neutralizing Antibodies and Participates Directly in Receptor Binding

Simone Warner,1 Carol A. Hartley,2 Rachel A. Stevenson,2 Nino Ficorilli,2 Annalisa Varrasso,2 Michael J. Studdert,2 and Brendan S. Crabb1,3,*

Department of Microbiology and Immunology and the Co-Operative Research Centre for Vaccine Technology1 and School of Veterinary Science,2 The University of Melbourne, Melbourne, Victoria 3010, and The Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria 3050,3 Australia

Received 20 February 2001/Accepted 21 June 2001

Equine rhinitis A virus (ERAV) is a respiratory pathogen of horses and is classified as an Aphthovirus, the only non-Foot-and-mouth disease virus (FMDV) member of this genus. In FMDV, virion protein 1 (VP1) is a major target of protective antibodies and is responsible for viral attachment to permissive cells via an RGD motif located in a distal surface loop. Although both viruses share considerable sequence identity, ERAV VP1 does not contain an RGD motif. To investigate antibody and receptor-binding properties of ERAV VP1, we have expressed full-length ERAV VP1 in Escherichia coli as a glutathione S-transferase (GST) fusion protein (GST-VP1). GST-VP1 reacted specifically with antibodies present in serum from a rabbit immunized with purified ERAV virions and also in convalescent-phase sera from horses experimentally infected with ERAV. An antiserum raised in rabbits to GST-VP1 reacted strongly with viral VP1 and effectively neutralized ERAV infection in vitro. Using a flow cytometry-based binding assay, we found that GST-VP1, but not other GST fusion proteins, bound to cell surface receptors. This binding was reduced in a dose-dependent manner by the addition of purified ERAV virions, demonstrating the specificity of this interaction. A separate cell-binding assay also implicated GST-VP1 in receptor binding. Importantly, anti-GST-VP1 antibodies inhibited the binding of ERAV virions to Vero cells, suggesting that these antibodies exert their neutralizing effect by blocking viral attachment. Thus ERAV VP1, like its counterpart in FMDV, appears to be both a target of protective antibodies and involved directly in receptor binding. This study reveals the potential of recombinant VP1 molecules to serve as vaccines and diagnostic reagents for the control of ERAV infections.

* Corresponding author. Mailing address: The Walter and Eliza Hall Institute of Medical Research, PO The Royal Melbourne Hospital, VIC 3050, Australia. Phone: 61 3 8345 2469. Fax: 61 3 9347 0852. E-mail: crabb{at}wehi.edu.au.

Journal of Virology, October 2001, p. 9274-9281, Vol. 75, No. 19
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.19.9274-9281.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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