Iyengar S, Hildreth J E, Schwartz D H
Department of Pharmacology and Molecular Sciences, School of Medicine, The Johns Hopkins University, Baltimore, Maryland 21205, USA.
J Virol. 1998 Jun;72(6):5251-5. doi: 10.1128/JVI.72.6.5251-5255.1998.
Human immunodeficiency virus (HIV) envelope binds CD4 and a chemokine receptor in sequence, releasing hydrophobic viral gp41 residues into the target membrane. HIV entry required actin-dependent concentration of coreceptors, which could be disrupted by cytochalasin D (CytoD) without an effect on cell viability or mitosis. Pretreatment of peripheral blood mononuclear cells, but not virus, inhibited entry and infection. Immunofluorescent confocal microscopy of activated cells revealed CD4 and CXCR4 in nonoverlapping patterns. Addition of gp120 caused polarized cocapping of both molecules with subsequent pseudopod formation, while CytoD pretreatment blocked these membrane changes completely.
人类免疫缺陷病毒(HIV)包膜依次结合CD4和趋化因子受体,将疏水性病毒糖蛋白41(gp41)残基释放到靶细胞膜中。HIV进入需要肌动蛋白依赖性的共受体聚集,细胞松弛素D(CytoD)可破坏这种聚集,且对细胞活力或有丝分裂无影响。对外周血单核细胞而非病毒进行预处理可抑制病毒进入和感染。对活化细胞进行免疫荧光共聚焦显微镜检查显示,CD4和CXCR4呈非重叠模式。添加gp120会导致这两种分子发生极化共帽化,随后形成伪足,而CytoD预处理则完全阻断了这些膜变化。