Attachment of bovine parvovirus to O-linked alpha 2,3 neuraminic acid on glycophorin A.
The bovine parvovirus (BPV) hemagglutinates human erythrocytes by binding to glycophorin A (GPA). The purpose of this study was to determine which carbohydrate on GPA binds BPV. Treatment of GPA with alpha2,3,-6,-8 neuraminidase eliminated binding of BPV to GPA. Beta-elimination of O-linked sialic acids on GPA eliminated binding, while removal of N-linked carbohydrates using the N-glycosidase PNGase F failed to eliminate binding. Treatment of GPA with a neuraminidase which specifically cleaved alpha2,3 glycosidic bonds eliminated BPV binding and, following this treatment, virus binding to GPA was restored by reconstitution of alpha2,3-linked neuraminic acids. These results indicated the O-linked alpha2,3 neuraminic acids of GPA bind BPV.
Blackburn
S D
SD
Department of Microbiology and Molecular Biology, Brigham Young University, Provo, Utah 84602, USA.
Cline
S E
SE
Hemming
J P
JP
Johnson
F B
FB
D000818:Animals; D002417:Cattle / Q000821:virology*; D002462:Cell Membrane / Q000821:virology*; D006021:Glycophorins / Q000378:metabolism* / Q000502:physiology; D006384:Hemagglutination; D019158:N-Acetylneuraminic Acid / Q000378:metabolism*; D009975:Orthomyxoviridae / Q000502:physiology; D017992:Parvovirus / Q000378:metabolism*; D011991:Receptors, Virus / Q000502:physiology
D006021:Glycophorins; D011991:Receptors, Virus; D019158:N-Acetylneuraminic Acid