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Differential Host-dependent Expression of -galactosyl Epitopes on Viral Glycoproteins: A Study of Eastern Equine Encephalitis Virus as a Model

Department of Microbiology and Immunology, Medical College of Pennsylvania, Philadelphia, Pennsylvania 19129, U.S.A.

The carbohydrate epitope Gal1-3Gal1-4GlcNAc-R (-galactosyl) is abundantly expressed on cells of non-primate mammals, prosimians and New World monkeys, where it is synthesized by the enzyme 1,3-galactosyltransferase (1,3GT). Old World monkeys, apes and humans lack 1,3GT and hence do not synthesize -galactosyl epitopes. Instead, these species produce a natural antibody, anti-Gal, which interacts specifically with -galactosyl epitopes and which constitutes up to 1% of circulating immunoglobulins in humans. We have used eastern equine encephalitis (EEE) virus as a model to examine the differential expression of -galactosyl epitopes on the glycoproteins of virus propagated in cells that either produce or lack 1,3GT. As predicted, virus propagated in Vero cells (derived from the African green monkey, an Old World monkey) did not express -galactosyl epitopes. In contrast, virus propagated in mouse 3T3 cells (EEE_3T3) expressed approximately 80 -galactosyl epitopes per virion on both the E1 and the E2 envelope glycoproteins. Thus, expression of the -galactosyl epitope on virions paralleled that on host cells. The binding of anti-Gal antibody to these epitopes on EEE_3T3 virions partially neutralized virus infectivity, raising the possibility that anti-Gal production in hosts may influence the initial infectious stage of viruses expressing -galactosyl epitopes.

Received 26 August 1993; accepted 10 December 1993.

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