It has been suggested that avian reovirus σ3 protein is analogous to σ1 trimer, the mammalian reovirus attachment protein. We have investigated the multimeric nature and cell binding ability of σ3 protein. The data presented here demonstrate that σ3 protein is a multimer in its undisrupted form as determined by SDS-PAGE in non-dissociating conditions. However, virion-associated σ3 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 expressed σ3 fusion protein (σ3-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 σ3 protein and by competition with avian reovirus particles. As determined by a reverse experiment, σ3-MBP was also able to reduce the virus p.f.u. in monolayer cell cultures, indicating the important role of σ3 protein in the initiation of virus infection.


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