It is believed that the fusion process is similar to that of HIV-1 [28]; for example, when S1 binds to the receptor on the cell membrane, the fusion peptide at the N terminus of S2 inserts into the cell membrane, then three HR1s attach to each other in parallel as a trimer, followed by binding of three HR2s separately onto the outside of the trimer to form a 6-helix bundle, thus bringing virus and cell membranes close to each other to trigger fusion.
Shibo Jiang
b Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA
e Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences, Fudan University, Shanghai, China
** Corresponding author. School of Basic Medical Sciences, Fudan University, 131 Dong An Road, Fuxing Building, Xuhui District, Shanghai 200032, China
The comparison of the pre- and post-fusion structures revealed the large conformational changes in gp41 during the antiparallel packing of the N- and C-terminal heptad repeats (NHRs and CHRs) in membrane fusion. Several mutagenesis studies of gp41 performed in the past were interpreted based on 6HB, the only available structure at that time.
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