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Identification of the HIV‐1 gp41 core‐binding motif – HXXNPF
Author(s) -
Huang Jing-He,
Liu Zu-Qiang,
Liu Shuwen,
Jiang Shibo,
Chen Ying-Hua
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.07.067
Subject(s) - gp41 , epitope , glycoprotein , chemistry , monoclonal antibody , heptad repeat , peptide , binding site , peptide sequence , biology , microbiology and biotechnology , biochemistry , antigen , antibody , genetics , gene
The HIV‐1 gp41 core, a six‐helix bundle formed between the N‐ and C‐terminal heptad repeats, plays a critical role in fusion between the viral and target cell membranes. Using N36(L8)C34 as a model of the gp41 core to screen phage display peptide libraries, we identified a common motif, HXXNPF (X is any of the 20 natural amino acid residues). A selected positive phage clone L7.8 specifically bound to N36(L8)C34 and this binding could be blocked by a gp41 core‐specific monoclonal antibody (NC‐1). JCH‐4, a peptide containing HXXNPF motif, effectively inhibited HIV‐1 envelope glycoprotein‐mediated syncytium‐formation. The epitope of JCH‐4 was proven to be linear and might locate in the NHR regions of the gp41 core. These data suggest that HXXNPF motif may be a gp41 core‐binding sequence and HXXNPF motif‐containing molecules can be used as probes for studying the role of the HIV‐1 gp41 core in membrane fusion process.