{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yamamoto M"],"funding":["MEXT | Japan Society for the Promotion of Science","Japan Agency for Medical Research and Development","Ministry of Education, Culture, Sports, Science and Technology"],"pagination":["5677-5687"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6462516"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["294(14)"],"pubmed_abstract":["Membrane fusion is the first essential step in HIV-1 replication. The gp41 subunit of HIV-1 envelope protein (Env), a class I fusion protein, achieves membrane fusion by forming a structure called a six-helix bundle composed of N- and C-terminal heptad repeats. We have recently shown that the distal portion of the α9 helix in the C-terminal heptad repeat of X4-tropic HXB2 Env plays a critical role in the late-stage membrane fusion and viral infection. Here, we used R5-tropic JRFL Env and constructed six alanine insertion mutants, 641+A to 646+A, in the further distal portion of α9 where several glutamine residues are conserved (the number corresponds to the position of the inserted alanine in JRFL Env). 644+A showed the most severe defect in syncytia formation. Decreased fusion pore format"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Cell-cell and virus-cell fusion assay-based analyses of alanine insertion mutants in the distal α9 portion of the JRFL gp41 subunit from HIV-1."],"pmcid":["PMC6462516"],"funding_grant_id":["18K15235","Core-to-Core Program A: Advanced Research Networks","16H06575","JP18fm0108006"],"pubmed_authors":["Du Q","Tanaka Y","Yamamoto M","Inoue JI","Wang H","Watanabe A","Kawaguchi Y","Song J","Matsuda Z"],"additional_accession":[]},"is_claimable":false,"name":"Cell-cell and virus-cell fusion assay-based analyses of alanine insertion mutants in the distal α9 portion of the JRFL gp41 subunit from HIV-1.","description":"Membrane fusion is the first essential step in HIV-1 replication. The gp41 subunit of HIV-1 envelope protein (Env), a class I fusion protein, achieves membrane fusion by forming a structure called a six-helix bundle composed of N- and C-terminal heptad repeats. We have recently shown that the distal portion of the α9 helix in the C-terminal heptad repeat of X4-tropic HXB2 Env plays a critical role in the late-stage membrane fusion and viral infection. Here, we used R5-tropic JRFL Env and constructed six alanine insertion mutants, 641+A to 646+A, in the further distal portion of α9 where several glutamine residues are conserved (the number corresponds to the position of the inserted alanine in JRFL Env). 644+A showed the most severe defect in syncytia formation. Decreased fusion pore format","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Apr","modification":"2026-04-28T21:53:44.07Z","creation":"2020-10-04T07:07:01Z"},"accession":"S-EPMC6462516","cross_references":{"pubmed":["30737278"],"doi":["10.1074/jbc.RA118.004579","10.1074/jbc.ra118.004579"]}}