Abstract
A recombinant envelope glycoprotein derived from visna virus, a natural lentivirus pathogen of sheep, induced antibodies that neutralized cell-free virus and blocked virus-mediated cell-to-cell fusion. The visna virus envelope gene was subcloned into a baculovirus expression vector and was expressed in insect cells. A pair of guinea pigs were immunized with the recombinant glycoprotein, and postimmunization sera neutralized cell-free visna virus infectivity and also blocked virus-mediated syncytium formation when infected and uninfected cells were cocultured together. Thus, the recombinant visna surface envelope glycoprotein is capable of inducing both neutralizing and fusion-blocking antibodies. In addition to its relevance for vaccine development, the recombinant glycoprotein will be a useful tool to study differences between antibody-mediated enhancement versus neutralization during virus-host interactions in lentivirus infections in vivo.
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