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J Gen Virol 71 (1990), 1957-1963; DOI 10.1099/0022-1317-71-9-1957
© 1990 Society for General Microbiology

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

Barbara E. Weiler1, Heinz C. Schröder1, Vladimir Stefanovich1, Derek Stewart3, John M. S. Forrest3, Lois B. Allen4, Bonnie J. Bowden4, Matthias H. Kreuter1, Rita Voth2 and Werner E. G. Müller1

1 Institut für Physiologische Chemie, Abteilung Angewandte Molekularbiologie, Universität, Duesbergweg 6, 6500 Mainz
2 Institut für Medizinische Mikrobiologie, Abteilung Experimentelle Virologie, Obere Zahlbacher Strasse 67, 6500 Mainz, F.R.G.
3 Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, U.K.
and4 Southern Research Institute, Virology Division, 2000 Ninth Avenue South, Birmingham, Alabama 35255-5305, U.S.A.

Sulphoevernan is a sulphated {alpha}-1 -> 3, 1 -> 4 polyglucan (Mr 20000) 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 µg/ml. Moreover, the compound completely inhibits HIV-1-induced syncytium formation at a concentration of 1 µg/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.

Received 27 November 1989; accepted 24 May 1990.


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Marked Depletion of Glycosylation Sites in HIV-1 gp120 under Selection Pressure by the Mannose-Specific Plant Lectins of Hippeastrum Hybrid and Galanthus nivalis
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[Abstract] [Full Text] [PDF]




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