首页> 美国卫生研究院文献>Virology Journal >Sequence similarity between the erythrocyte binding domain of the Plasmodium vivax Duffy binding protein and the V3 loop of HIV-1 strain MN reveals a functional heparin binding motif involved in binding to the Duffy antigen receptor for chemokines
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Sequence similarity between the erythrocyte binding domain of the Plasmodium vivax Duffy binding protein and the V3 loop of HIV-1 strain MN reveals a functional heparin binding motif involved in binding to the Duffy antigen receptor for chemokines

机译:间日疟原虫达菲结合蛋白的红细胞结合结构域与HIV-1株MN的V3环之间的序列相似性揭示了功能肝素结合基序该基团与达菲抗原受体的趋化因子结合

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摘要

BackgroundThe HIV surface glycoprotein gp120 (SU, gp120) and the Plasmodium vivax Duffy binding protein (PvDBP) bind to chemokine receptors during infection and have a site of amino acid sequence similarity in their binding domains that often includes a heparin binding motif (HBM). Infection by either pathogen has been found to be inhibited by polyanions.
机译:背景技术HIV表面糖蛋白gp120(SU,gp120)和间日疟原虫达菲结合蛋白(PvDBP)在感染过程中与趋化因子受体结合,并在其结合域中具有氨基酸序列相似性位点,该位点通常包含肝素结合基序(HBM)。现已发现,任何一种病原体的感染都可被聚阴离子抑制。

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