The catalytic activity of protein disulfide isomerase is involved in human immunodeficiency virus envelope- mediated membrane fusion after CD4 cell binding

被引:96
作者
Fenouillet, E [1 ]
Barbouche, R [1 ]
Courageot, J [1 ]
Miquelis, R [1 ]
机构
[1] Fac Med Nord, CNRS, F-13015 Marseille, France
关键词
D O I
10.1086/318823
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Protein disulfide isomerase (PDI) is a multifunctional protein with thiol-disulfide redox-isomerase activities. It catalyzes thiol-disulfide interchange reactions on the cell surface that may cause structural modifications of exofacial proteins. PDI inhibitors alter human immunodeficiency virus (HIV) spread, and it has been suggested that PDI may be necessary to trigger HIV entry. This study examined this hypothesis by using cell-to-cell fusion assays, in which the HIV envelope (Env) expressed on the cell surface interacts with CD4(+) lymphocytes. PDI is clustered at the lymphocyte surface in the vicinity of CD4-enriched regions, but both antigens essentially do not colocalize. Anti-PDI antibodies and 2 inhibitors of its catalytic function altered Env-mediated membrane fusion at a post-CD4 cell binding step. The fact that the PDI catalytic activity present on lymphocytes is required for fusion supports the hypothesis that catalysts assist post-CD4 cell binding conformational changes within Env.
引用
收藏
页码:744 / 752
页数:9
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