title: [New anti-HIV drug which binds the oligosaccharides of HIV envelope glycoprotein].
abstract: The virion surface of the human immunodeficiency virus (HIV-1) is covered with an envelope glycoprotein gp120. Study of the oligosaccharide structures of gp120 suggests that the high mannose type of oligosaccharides are essential for HIV-1 infection. Pradimicin A, an antifungal antibiotic isolated from Actinomadura hibisca, and the derivative BMY-28864 have the ability to inhibit HIV-1 infection in vitro. The inhibitory effect was suppressed by addition of high mannose type oligosaccharides of gp120. BMY-28864 bound directly to gp120, mannose-BSA, and neoglycolipids containing high mannose type oligosaccharides but not to natural mammalian glycoproteins. The binding was Ca2+ dependent and was inhibited by mannose. BMY-28864 is a unique carbohydrate-binding antibiotic which has never been reported. It is possible to block HIV-1 infection by targeting oligosaccharide chains of the envelope glycoprotein.
mesh_terms: D000163:Acquired Immunodeficiency Syndrome; D000818:Animals; D018943:Anthracyclines; D000903:Antibiotics, Antineoplastic / Q000378:metabolism*; D000935:Antifungal Agents / Q000378:metabolism*; D002118:Calcium / Q000502:physiology; D002240:Carbohydrate Sequence; D015195:Drug Design; D015699:HIV Envelope Protein gp120 / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D011485:Protein Binding
chemical_list: D018943:Anthracyclines; D000903:Antibiotics, Antineoplastic; D000935:Antifungal Agents; D015699:HIV Envelope Protein gp120; C067714:N,N-dimethylpradimicin FA-2; D002118:Calcium