PRESENTATION OF NEUTRALIZING EPITOPES BY ENGINEERED ROTAVIRUS VP7S EXPRESSED BY RECOMBINANT VACCINIA VIRUSES

Previous studies showed that a calcium-dependent neutralization domain forms on the rotavirus glycoprotein VP7 during assembly into particle s. Here, we demonstrate that expressed, recombinant VP7 is capable of forming this neutralization domain in the absence of other rotavirus p roteins, but that the domain is unstable. High calcium environments, i ncorporation into particles, and binding of neutralizing antibodies st abilize the neutralization domain on expressed VP7. A chimeric, cell s urface-anchored molecule, VP7sc, has an enhanced ability to react with neutralizing antibodies. This may explain why immunization of mice wi th expressed native VP7 has had limited success white immunization wit h VP7sc efficiently induced neutralizing antibodies and passively prot ected pups from diarrhea. A model of VP7 folding consistent with these results is presented, (C) 1994 Academic Press, Inc.