Glycophorin is the reovirus receptor on human erythrocytes.

Abstract:

:Purified glycophorin (predominantly type A) from human erythrocytes was found to effectively inhibit reovirus hemagglutination (HA) in contrast to other glycoproteins such as fetuin or ovalbumin. Glycophorin was also a potent inhibitor of reovirus and protein sigma 1 binding to mouse L fibroblasts. Glycophorin pretreated with neuraminidase lost these inhibitory properties. Using a solid phase binding assay, it was demonstrated that reovirus as well as protein sigma 1 could specifically bind to glycophorin immobilized on polystyrene plates. This binding was inhibited by wheat germ agglutinin (WGA) but not by other lectins such as peanut agglutinin (PA), Maclura pomifera agglutinin (MPA), Bauhinia purpurea agglutinin (BPA), or concanavalin A (Con A). Binding of reovirus to glycophorin was also partially inhibited by a monoclonal antibody (10F7) (W. L. Bigbee, R. G. Langlois, M. Vanderlaan, and R. H. Jensen, 1984, J. Immunol. 133, 3149-3155), which recognizes a determinant common to the M and N forms of glycophorin, but not by N-specific monoclonal antibodies NN4 and NN5 or an M-specific monoclonal antibody, 6A7. Taken together, these results clearly indicate that the M, N blood group antigen, glycophorin, is the erythrocyte receptor for reovirus.

journal_name

Virology

journal_title

Virology

authors

Paul RW,Lee PW

doi

10.1016/0042-6822(87)90351-5

subject

Has Abstract

pub_date

1987-07-01 00:00:00

pages

94-101

issue

1

eissn

0042-6822

issn

1096-0341

journal_volume

159

pub_type

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