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The membrane proximal external region (MPER) of gp41 is extremely conserved among diverse HIV-1 variants, implying its important
role in viral infection. Interestingly, two of the most broadly neutralizing antibodies, 2F5 and 4E10, specifically recognize
this region. Our previous study demonstrated that the antigenicity and immunogenicity of 4E10 epitope are affected by remodeling
gp41 fusion core, suggesting that the MPER may be associated with gp41 core and involved in gp41-mediated membrane fusion.
Here we measured the binding activity of 4E10 epitope peptide (D4E10P) with various gp41 core-derived peptides and found that
the N-trimer region in a construct designated N-trimer-6HB interacted significantly with D4E10P. Using N-trimer-6HB to screen
a phage library, we identified a motif (WF) located in 4E10 epitope that may play a certain role in the interaction of gp41
MPER with the N-trimer in gp41 fusion core and, we thus speculated upon the potential involvement of MPER in the fusion process
between viral envelope and target cell membrane.
Supported by National Key Basic Research and Development Program of China (Grant No. 2007CB914402) 相似文献