A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein

被引:162
作者
Jiang, S
Lin, K
Lu, M
机构
[1] New York Blood Ctr, Lindsley F Kimball Res Inst, New York, NY 10021 USA
[2] Cornell Univ, Joan & Sanford I Weill Med Coll, Dept Biochem, New York, NY 10021 USA
关键词
D O I
10.1128/JVI.72.12.10213-10217.1998
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
引用
收藏
页码:10213 / 10217
页数:5
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