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Sulphoevernan, a polyanionic polysaccharide, and the narcissus lectin potently inhibit human immunodeficiency virus infection by binding to viral envelope protein.

Abstract
Sulphoevernan is a sulphated alpha-1----3, 1----4 polyglucan (Mr 20,000) with a helical structure. This compound effectively inhibits both human immunodeficiency virus type 1 (HIV-1) and type 2 infection of cells in vitro at concentrations around 0.5 micrograms/ml. Moreover, the compound completely inhibits HIV-1-induced syncytium formation at a concentration of 1 microgram/ml. Competition experiments with 35S-labelled sulphoevernan revealed that the mannose-specific lectin from Narcissus pseudonarcissus prevented binding of sulphoevernan to HIV-1, whereas the antibody OKT4A did not reduce the amount of sulphoevernan bound to MT-2 cells. These data indicate that the non-cytotoxic polymer sulphoevernan binds to the virus rather than to the host cell. In vivo studies, using Rauscher leukaemia virus in NMRI mice, revealed that, at a daily dose of 20 mg/kg, the animals were protected against virus-induced increases in spleen weight. From these in vitro and in vivo data we conclude that sulphoevernan has potential in the treatment of acquired immunodeficiency syndrome.
AuthorsB E Weiler, H C Schröder, V Stefanovich, D Stewart, J M Forrest, L B Allen, B J Bowden, M H Kreuter, R Voth, W E Müller
JournalThe Journal of general virology (J Gen Virol) Vol. 71 ( Pt 9) Pg. 1957-63 (Sep 1990) ISSN: 0022-1317 [Print] England
PMID2212988 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Antiviral Agents
  • Glucans
  • Lectins
  • Plant Lectins
  • Polysaccharides
  • Viral Envelope Proteins
  • narcissus lectin
  • Zidovudine
  • sulfoevernan
Topics
  • Antiviral Agents (pharmacology)
  • Cell Division (drug effects)
  • Cell Line
  • Glucans
  • HIV-1 (drug effects, physiology)
  • HIV-2 (drug effects, physiology)
  • Humans
  • Lectins (metabolism, pharmacology)
  • Plant Lectins
  • Polysaccharides (metabolism, pharmacology)
  • Protein Binding
  • Viral Envelope Proteins (metabolism)
  • Zidovudine (pharmacology)

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