Abstract
The surface nature of the proteins of a bovine enterovirus were determined by using 125I and pyridoxal phosphate-sodium borohydride labeling techniques. As found previously, 125I labels only VP1 in intact capsid particles, whereas reaction with pyridoxal phosphate followed by reduction with tritiated sodium borohydride labels VP1, VP2 and VP3. Only VP4 had no surface tyrosine, histidine or lysine available for reaction. After neutralization with homologous antisera, VP4 becomes exposed and is then available for labeling with 125I. This must reflect a substantial conformational change in the virus particle after neutralization.