       Document 0372
 DOCN  M9620372
 TI    [New anti-HIV drug which binds the oligosaccharides of HIV envelope
       glycoprotein]
 DT    9602
 AU    Mizuochi T; Nakata M; Department of Applied Chemistry, Tokai University.
 SO    Nippon Rinsho. 1995 Sep;53(9):2340-9. Unique Identifier : AIDSLINE
       MED/96008339
 AB    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.
 DE    *Acquired Immunodeficiency Syndrome  Animal  Antibiotics,
       Anthracycline/*METABOLISM  Antibiotics, Antifungal/*METABOLISM
       Calcium/PHYSIOLOGY  Carbohydrate Sequence  Drug Design  English Abstract
       Human  HIV Envelope Protein gp120/*METABOLISM  Molecular Sequence Data
       Protein Binding  JOURNAL ARTICLE  REVIEW  REVIEW, TUTORIAL

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

