title: Reduced glycosylation of human cell lines increases susceptibility to CD4-independent infection by human immunodeficiency virus type 2 (LAV-2/B).
abstract: The human immunodeficiency virus type 2 (HIV-2) strain LAV-2/B is able to infect a variety of human cell lines via a CD4-independent pathway. We have used the glycosylation inhibitors tunicamycin, swainsonine, and deoxymannojirimycin to further characterize this putative alternative receptor for HIV-2 (LAV-2/B). These antibiotics resulted in an increase (5- to 30-fold) in the susceptibility of a variety of CD4- human cell lines to infection by LAV-2/B (RD, HeLa, HT29, Rsb, Heb7a, Hos, and Daudi). Several nonprimate cell lines (mink Mv-1-lu, rabbit SIRC, hamster a23, mouse NIH 3T3, cat CCC, and rat HSN) remained resistant to infection by LAV-2/B after treatment with glycosylation inhibitors, suggesting that they do not express the HIV-2 CD4-independent receptor. Two of these nonprimate cell lines are readily infected by HIV-2 when they express CD4 (Mv-1-lu and CCC). Treatment of human cells with neuraminidase had no effect on subsequent infection by LAV-2/B, suggesting that the increase in susceptibility to infection of deglycosylated cells is not due to a change in the electrostatic charge of the cell surface. Treatment of RD CD4- cells and HeLa CD4+ cells with a variety of proteases resulted in a 75 to 90% decrease in infection by LAV-2/B when compared with untreated cells. Taken together, all these data suggest that HIV-2 can utilize a membrane glycoprotein other than CD4 to attach and fuse with a variety of human cells.
authors.affiliation: Chester Beatty Laboratories, Institute for Cancer Research, London, United Kingdom.
authors.forename: S J
authors.initials: SJ
authors.lastname: Talbot
authors.forename: R A
authors.initials: RA
authors.lastname: Weiss
authors.forename: T F
authors.initials: TF
authors.lastname: Schulz
mesh_terms: D000818:Animals; D015704:CD4 Antigens / Q000502:physiology*; D002460:Cell Line; D010450:Endopeptidases / Q000378:metabolism; D006031:Glycosylation / Q000187:drug effects; D015498:HIV-2 / Q000472:pathogenicity / Q000502:physiology*; D006801:Humans; D008561:Membrane Fusion; D008562:Membrane Glycoproteins / Q000378:metabolism; D019158:N-Acetylneuraminic Acid; D011991:Receptors, Virus / Q000502:physiology; D012794:Sialic Acids / Q000378:metabolism; D014415:Tunicamycin / Q000494:pharmacology
chemical_list: D015704:CD4 Antigens; D008562:Membrane Glycoproteins; D011991:Receptors, Virus; D012794:Sialic Acids; D014415:Tunicamycin; D010450:Endopeptidases; D019158:N-Acetylneuraminic Acid