Arch Virol (2005) 150: 1477–1484
Attachment of bovine parvovirus to O-linked alpha
2,3 neuraminic acid on glycophorin A
S. D. Blackburn, S. E. Cline, J. P. Hemming, and F. B. Johnson
Department of Microbiology and Molecular Biology,
Brigham Young University, Provo, Utah, U.S.A.
Received October 27, 2004; accepted January 9, 2005
Published online March 8, 2005
Summary. 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 α2,3,-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 α2,3 glycosidic bonds eliminated
BPV binding and, following this treatment, virus binding to GPA was restored
by reconstitution of α2,3-linked neuraminic acids. These results indicated the
O-linked α2,3 neuraminic acids of GPA bind BPV.
Bovine parvovirus (BPV) is a common pathogen of cattle which causes primarily
gastroenteritis when infecting the alimentary canal . BPV was originally iso-
lated from the gastrointestinal tract of infected calves and serosurveys showed a
high incidence of infection in some herds [1, 8]. BPV is a member of the family
Parvoviridae, genus Parvovirus. This genus consists of small, autonomously
replicating, non-enveloped, single stranded DNA, icosahedral viruses. The BPV
genome encodes ﬁve gene products: three structural proteins  and two nonstruc-
tural proteins. Previous work has shown that the BPV capsid interacts with the
human erythrocyte transmembrane glycoprotein glycophorin A (GPA) to mediate
the hemagglutination reaction . GPA carries the MN blood group activities.
It exists naturally as a homodimer with a molecular mass of 78,500 daltons.
Each monomer is composed of 131 amino acids which span three domains: a
carboxy-terminal hydrophilic cytosolic domain, a hydrophobic transmembrane