A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein
A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein
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DOI：
10.1128/jvi.72.12.10213-10217.1998
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发表时间：
1998-12-01
影响因子：
5.4
通讯作者：
Lu, M
中科院分区：
文献类型：
--
作者：
Jiang, S;Lin, K;Lu, M
人类免疫缺陷病毒1型（HIV-1）包膜糖蛋白的gp 41亚基在病毒感染的膜融合步骤中起主要作用。gp 41的胞外域含有六螺旋结构域，其可能代表分子的融合活性构象的核心。从用模型多肽N36（L 6）C34免疫的小鼠产生并克隆单克隆抗体（MAb），命名为NC-1，所述模型多肽N36（L 6）C34折叠成稳定的六螺旋束。NC-1特异性地结合到ru-螺旋核心结构域和gp 41的寡聚体形式。这种构象依赖的反应性被gp 41的N-末端卷曲螺旋区域内的点突变显著降低，这阻碍了gp 41核心的形成。NC-1仅在可溶性CD 4存在下才与HIV-1感染细胞的表面结合。这些结果表明，NC-1是能够与融合活性的gp 41在构象特异性的方式进行反应，并可用作一个有价值的生物试剂，用于研究受体诱导的膜融合和HIV-1感染所需的gp 41的构象变化。
The gp41 subunit of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein plays a major role in the membrane fusion step of viral infection. The ectodomain of gp41 contains a six-helix structural domain that likely represents the core of the fusion-active conformation of the molecule. A monoclonal antibody (MAb), designated NC-I, was generated and cloned from a mouse immunized with the model polypeptide N36 (L6)C34, which folds into a stable six-helix bundle. NC-1 binds specifically to both the ru-helical core domain and the oligomeric forms of gp41. This conformation-dependent reactivity is dramatically reduced by point mutations within the N-terminal coiled-coil region of gp41 which impede formation of the gp41 core. NC-1 binds to the surfaces of HIV-l-infected cells only in the presence of soluble CD4. These results indicate that NC-1 is capable of reacting with fusion-active gp41 in a conformation-specific manner and can be used as a valuable biological reagent for studying the receptor-induced conformational changes in gp41 required for membrane fusion and HIV-1 infection.