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Structure, interactions and membrane topology of HIV gp41 ectodomain sequences.
Aisenbrey, Christopher; Bechinger, Burkhard.
  • Aisenbrey C; Université de Strasbourg/CNRS, UMR7177, Institut de Chimie, 4, Rue Blaise Pascal, 67070 Strasbourg, France.
  • Bechinger B; Université de Strasbourg/CNRS, UMR7177, Institut de Chimie, 4, Rue Blaise Pascal, 67070 Strasbourg, France; Institut Universitaire de France, France. Electronic address: bechinge@unistra.fr.
Biochim Biophys Acta Biomembr ; 1862(7): 183274, 2020 07 01.
Article in English | MEDLINE | ID: covidwho-820155
ABSTRACT
The gp41 type I membrane protein is part of the trimeric Env complex forming the spikes at the HIV surface. By interacting with cellular receptors, the Env protein complex initiates the infectious cycle of HIV. After the first contact has been established Env disassembles by shedding gp120 while the remaining gp41 undergoes a number of conformational changes which drive fusion of the cellular and the viral membranes. Here we investigated the membrane interactions and oligomerization of the two gp41 heptad repeat domains NHR and CHR. While these are thought to form a six-helix bundle in the post-fusion state little is known about their structure and role during prior fusion events. When investigated in aqueous buffer by CD and fluorescence quenching techniques the formation of NHR/CHR hetero-oligomers is detected. An equilibrium of monomers and hetero-oligomers is also observed in membrane environments. Furthermore, the partitioning to POPC or POPC/POPG 3/1 vesicles of the two domains alone or in combination has been studied. The membrane interactions were further characterized by 15N solid-state NMR spectroscopy of uniaxially oriented samples which shows that the polypeptide helices are oriented parallel to the bilayer surface. The 31P solid-state NMR spectra of the same samples are indicative of considerable disordering of the membrane packing. The data support models where NHR and CHR insert in the viral and cellular membranes, respectively, where they exhibit an active role in the membrane fusion events.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: HIV Envelope Protein gp41 / HIV Infections / HIV-1 / Membrane Fusion Limits: Humans Language: English Journal: Biochim Biophys Acta Biomembr Year: 2020 Document Type: Article Affiliation country: J.bbamem.2020.183274

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Full text: Available Collection: International databases Database: MEDLINE Main subject: HIV Envelope Protein gp41 / HIV Infections / HIV-1 / Membrane Fusion Limits: Humans Language: English Journal: Biochim Biophys Acta Biomembr Year: 2020 Document Type: Article Affiliation country: J.bbamem.2020.183274