Inhibition of anti-V3 domain antibody binding to human immunodeficiency virus type-1-infected cells by sulfated polysaccharides.
Inhibition of anti-V3 domain antibody binding to human immunodeficiency virus type-1-infected cells by sulfated polysaccharides.
复制标题
硫酸化多糖抑制抗 V3 结构域抗体与人类免疫缺陷病毒 1 型感染细胞的结合。
DOI：
10.1006/bbrc.1995.1577
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发表时间：
1995
影响因子：
3.1
通讯作者：
Gurney,ME
中科院分区：
文献类型：
--
作者：
Okada,T;Patterson,BK;Gurney,ME
The third variable domain (V3 domain) of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein gp120 is an immunodominant region. Anti-V3 domain antibodies neutralize both HTV-1 infection and syncytium formation. The V3 domain has a high density of positive charge which is a potential binding site for anti-HTV-1 sulfated polysaccharides. To investigate the inhibitory effect of sulfated polysaccharides on the binding of anti-V3 domain anibody, fluorescence-activating cell sorting analysis was performed using two kinds of antibodies, NEA9284 (purified, 0.25 μg/ml) and 0.5β (ascite, 2.0 mg/ml), and HN-1-infected CEM cells. When the binding assay with a 1:100 dilution of each antibody was performed in the presence of dextran sulfate, heparin, and inositol hexasulfate at concentrations which are antiviral, the compounds did not inhibit the binding of either antibodiy. As the antibody concentration was decreased with higher dilution, dextran sulfate was able to reduce antibody binding by 50-60%. Thus, antagonism of anti-V3 domain antibody binding by sulfated polysaccharides is not as extensive as reported previously by several groups.
