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.
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Similar content being viewed by others Explore related subjectsDiscover the latest articles and news from researchers in related subjects, suggested using machine learning. Author information Authors and AffiliationsDepartment of Microbiology and Molecular Biology, Brigham Young University, Provo, Utah, U.S.A.
S. D. Blackburn, S. E. Cline, J. P. Hemming & F. B. Johnson
Blackburn, S., Cline, S., Hemming, J. et al. Attachment of bovine parvovirus to O-linked alpha 2,3 neuraminic acid on glycophorin A. Arch Virol 150, 1477–1484 (2005). https://doi.org/10.1007/s00705-005-0496-y
Received: 27 October 2004
Accepted: 09 January 2005
Published: 08 March 2005
Issue Date: July 2005
DOI: https://doi.org/10.1007/s00705-005-0496-y
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