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Evidence for the multimeric nature and cell binding ability of avian reovirus 3 protein

¹ Section de virologie, Faculté de médecine vétérinaire, Université de Montréal, C.P. 5000, St-Hyacinthe, Québec, J2S 7C6
and² Centre de recherche en virologie, Institut Armand-Frappier, C.P. 100, Laval, Québec, H7N 4Z3, Canada

It has been suggested that avian reovirus 3 protein is analogous to 1 trimer, the mammalian reovirus attachment protein. We have investigated the multimeric nature and cell binding ability of 3 protein. The data presented here demonstrate that 3 protein is a multimer in its undisrupted form as determined by SDS-PAGE in non-dissociating conditions. However, virion-associated 3 protein and COS-7 cell-expressed protein behaved differently in SDS-PAGE, suggesting a need for virus-associated factor(s) to control the multimerization of the protein. The data also show that Escherichia coli expressed 3 fusion protein (3-MBP) in its multimeric form is capable of attaching to Vero cells. The binding was found to be specific and receptor mediated by the fact that it was inhibited by a monoclonal antibody specific for 3 protein and by competition with avian reovirus particles. As determined by a reverse experiment, 3-MBP was also able to reduce the virus p.f.u. in monolayer cell cultures, indicating the important role of 3 protein in the initiation of virus infection.

^* Author for correspondence. Fax +1 514 778 8113. e-mail silima@ere.umontreal.ca

Received 20 November 1995; accepted 30 January 1996.

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