Abstract

In this study, we describe the isolation and partial characterization of a Pixuna virus receptor, which is a component of a plasma membrane fraction of chicken embryo fibroblast (CEF). Polyclonal antiserum was prepared from rabbits immunized with the membrane fraction. Said polyclonal antiserum reacted in a similar way as monoclonal antibodies raised against the membrane fraction. Both antisera were able to prevent CEF and Vero cells from infection with Pixuna virus. Immunofluorescence studies suggested that the receptors found in the fibroblasts and in the Vero cells shared at least some epitopes. The Western blot analysis of the purified membrane fraction antigens, which reacted with the monoclonal and polyclonal antibodies, detected a double band with a molecular mass of approximately 60 kDa. Not only immunofluorescence staining but also electron and immunoelectron microscopy studies evidenced the receptor localization in the plasma membrane. In this manner, we reported the isolation and partial characterization of a new Pixuna virus receptor in the plasma membrane of chicken embryo fibroblasts in culture. The data obtained demonstrated the receptor significance for the penetration of Pixuna virus into fibroblasts and mammalian cell and the related importance of designing new antiviral drugs by blocking the mechanism of receptor penetration of the virus into the cells.

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