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Re: Work Harder post# 19904

Thursday, 08/27/2020 8:57:22 AM

Thursday, August 27, 2020 8:57:22 AM

Post# of 27661
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

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7102556/

Ref 28

The conserved residue Arg46 in the N-terminal heptad repeat domain of HIV-1 gp41 is critical for viral fusion and entry

https://pubmed.ncbi.nlm.nih.gov/22970321/

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.

https://read.qxmd.com/read/29609648/six-helix-bundle-completion-in-the-distal-c-terminal-heptad-repeat-region-of-gp41-is-required-for-efficient-human-immunodeficiency-virus-type-1-infection

We attempted to stabilize native Env trimers by incorporation of mutations at the NHR-CHR interface that disrupt the postfusion 6-HB of gp41

https://read.qxmd.com/read/24920800/stabilizing-the-native-trimer-of-hiv-1-env-by-destabilizing-the-heterodimeric-interface-of-the-gp41-postfusion-six-helix-bundle


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