Summary auto-generated
This study identified the cellular receptors for bovine parvovirus (BPV), a small DNA virus that causes diarrhea in cattle. Using haemagglutination assays with human type O red blood cells and enzymatic treatments, researchers demonstrated that BPV attaches to sialylglycoproteins—specifically glycoproteins containing sialic acid. Treatment of erythrocytes with neuraminidase, which removes sialic acid, or with sodium periodate, which destroys carbohydrates, blocked viral binding. Further characterization revealed that BPV specifically binds to glycophorin A, the major glycoprotein on red blood cell membranes. This was confirmed through multiple complementary methods including gel electrophoresis with virus overlay protein-binding assays, dot blots using purified glycophorin A, and competition experiments. Pure glycophorin A completely inhibited BPV-mediated red cell agglutination in a dose-dependent manner, indicating it competes for virus attachment sites. These findings establish that BPV receptor recognition depends on sialic acid-containing membrane glycoproteins, paralleling attachment mechanisms of related parvoviruses like feline panleukopenia virus and canine parvovirus.
Key findings
- BPV binds to sialic acid-containing glycoproteins on erythrocyte membranes, as demonstrated by neuraminidase and periodate sensitivity
- The major erythrocyte membrane glycoprotein glycophorin A serves as the primary receptor for BPV attachment
- Purified glycophorin A completely blocks BPV-mediated hemagglutination in a concentration-dependent manner, indicating it is the sole erythrocyte receptor type
- Viral binding requires both protein and carbohydrate components, as proteolytic and oxidative treatments abolished attachment
- BPV interaction with sialylglycoproteins likely extends to nucleated host cells and may initiate the viral replication cycle
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Abstract
Bovine parvovirus (BPV), an autonomous parvovirus, haemagglutinates human type O erythrocytes and infects certain bovine cells in culture. Little is known about the receptor to which it attaches, either on nucleated host cells or on erythrocytes. Haemagglutination assays and radiolabelled virus-binding tests measuring the effects of trypsin, chymotrypsin, neuraminidase, phospholipase C and sodium periodate on attachment of BPV to receptors indicated that BPV interacted with N- acetylneuraminic acid-containing (sialyl) glycoproteins. SDS- polyacrylamide gel separation of erythrocyte ghost proteins and virus overlay protein-binding revealed BPV binding to glycophorin A. Confirmation testing showed BPV binding to purified glycophorin A on dot blots and on gels containing membrane glycophorin A and purified glycophorin A. Further, in competition assays, purified glycophorin A completely inhibited the BPV haemagglutination reaction. The results of this study indicate that BPV binds to sialated membrane glycoproteins, one of which is the major erythrocyte membrane glycoprotein, glycophorin A.