Alteration of glycosylation renders HIV sensitive to inactivation by normal human serum
Reed, D.J.; Lin, X.; Thomas, T.D.; Birks, C.W.; Tang, J.; Rother, R.P.
Journal of Immunology 159(9): 4356-4361
1997
ISSN/ISBN: 0022-1767 PMID: 9379032 Document Number: 471677
In this study, normal human serum (NHS) sensitivity of HIV was assessed following viral propagation in human cells that were manipulated to express the alpha -galactosyl epitope. HUT-78 cells were transduced with an exogenous alpha 1-3-galactosyl transferase gene, which codes for the terminal glycosyl transferase responsible for generation of the alpha -galactosyl epitope. The transduced HUT-78 cells expressed high levels of the alpha -galactosyl epitope on their membrane surface, rendering them sensitive to killing in NHS. Similarly, HIV passaged through these cells acquired the alpha -galactosyl epitope in association with the envelope glycoprotein gp120 and was also effectively inactivated in NHS. Viral inactivation was abolished by the addition of a synthetic disaccharide that contains the alpha -galactosyl epitope, indicating that virolysis is mediated by anti- alpha -galactosyl natural antibody. These results demonstrate that, like other retroviruses bearing the alpha -galactosyl epitope, HIV modified to express this epitope is inactivated in NHS. Furthermore, these data suggest that expression of the alpha -galactosyl epitope on the surface of viruses may have implications in the interspecies transmission of such viruses to humans.