BINDING OF BOVINE PARVOVIRUS TO ERYTHROCYTE-MEMBRANE SIALYLGLYCOPROTEINS

Bovine parvovirus (BPV), an autonomous parvovirus, haemagglutinates hu man type O erythrocytes and infects certain bovine cells in culture. L ittle is known about the receptor to which it attaches, either on nucl eated host cells or on erythrocytes, Haemagglutination assays and radi olabelled virus-binding tests measuring the effects of trypsin, chymot rypsin, neuraminidase, phospholipase C and sodium periodate on attachm ent of BPV to receptors indicated that BPV interacted with N-acetyl-ne uraminic acid-containing (sialyl) glycoproteins, SDS-polyacrylamide ge l separation of erythrocyte ghost proteins and virus overlay protein-b inding revealed BPV binding to glycophorin A. Confirmation testing sho wed BPV binding to purified glycophorin A on dot blots and on gels con taining membrane glycophorin A and purified glycophorin A. Further, in competition assays, purified glycophorin A completely inhibited the B PV haemagglutination reaction. The results of this study indicate that BPV binds to sialated membrane glycoproteins, one of which is the maj or erythrocyte membrane glycoprotein, glycophorin A.