Results 11 to 20 of about 24,285 (259)

Structure of HIV-1 gp41 with its membrane anchors targeted by neutralizing antibodies [PDF]

open access: yesbioRxiv, 2020
The HIV-1 gp120/gp41 trimer undergoes a series of conformational changes in order to catalyze gp41-induced fusion of viral and cellular membranes. Here, we present the crystal structure of gp41 locked in a fusion intermediate state by an MPER-specific ...
C. Caillat   +8 more
semanticscholar   +2 more sources

Asymmetric deactivation of HIV-1 gp41 following fusion inhibitor binding. [PDF]

open access: yesPLoS Pathogens, 2009
Both equilibrium and nonequilibrium factors influence the efficacy of pharmaceutical agents that target intermediate states of biochemical reactions. We explored the intermediate state inhibition of gp41, part of the HIV-1 envelope glycoprotein complex ...
Kristen M Kahle   +2 more
doaj   +4 more sources

Model for the structure of the HIV gp41 ectodomain: insight into the intermolecular interactions of the gp41 loop

open access: yesBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 2001
In human immunodeficiency virus (HIV) the viral envelope proteins gp41 and gp120 form a non-covalent complex, which is a potential target for AIDS therapies. In addition gp41 plays a possible role in HIV infection of B cells via the complement system.
Caffrey, Michael
openaire   +3 more sources

Evolution of the HIV-1 envelope glycoproteins with a disulfide bond between gp120 and gp41 [PDF]

open access: yesRetrovirology, 2004
Background We previously described the construction of an HIV-1 envelope glycoprotein complex (Env) that is stabilized by an engineered intermolecular disulfide bond (SOS) between gp120 and gp41.
Caffrey Michael   +5 more
doaj   +2 more sources

A Fusion Intermediate gp41 Immunogen Elicits Neutralizing Antibodies to HIV-1* [PDF]

open access: yesJournal of Biological Chemistry, 2014
Background: HIV-1 gp41 MPER is a target for inducing broadly neutralizing antibodies. Results: Gp41int folds into a compact elongated structure that induces neutralizing antibodies upon immunization.
R. Lai   +17 more
semanticscholar   +3 more sources

Investigating the role of a conserved hydrophobic pocket of gp41 in the anti-HIV activity of fusion inhibitors. [PDF]

open access: yesProtein Sci
Abstract Membrane fusion between HIV and host cells requires interaction between the N‐terminal and C‐terminal repeat regions (NHR and CHR) of the gp41 envelope subunit. A deep hydrophobic pocket (HP) on the surface of NHR is considered crucial in this interaction.
Polo-Megías D   +9 more
europepmc   +2 more sources

HIV DNA-Adenovirus Multiclade Envelope Vaccine Induces gp41 Antibody Immunodominance in Rhesus Macaques

open access: yesJournal of Virology, 2017
Dominant antibody responses in vaccinees who received the HIV-1 multiclade (A, B, and C) envelope (Env) DNA/recombinant adenovirus virus type 5 (rAd5) vaccine studied in HIV-1 Vaccine Trials Network (HVTN) efficacy trial 505 (HVTN 505) targeted Env gp41 ...
Qifeng Han   +25 more
semanticscholar   +2 more sources

Impact of stabilizing mutations on the antigenic profile and glycosylation of membrane-expressed HIV-1 envelope glycoprotein.

open access: yesPLoS Pathogens, 2023
Recent HIV-1 vaccine development has centered on "near native" soluble envelope glycoprotein (Env) trimers that are artificially stabilized laterally (between protomers) and apically (between gp120 and gp41).
Tommy Tong   +7 more
doaj   +1 more source

Cholesterol Interaction with the Trimeric HIV Fusion Protein gp41 in Lipid Bilayers Investigated by Solid-State NMR Spectroscopy and Molecular Dynamics Simulations

open access: yesJournal of Molecular Biology, 2020
HIV-1 entry into cells is mediated by the fusion protein gp41. Cholesterol plays an important role in this virus-cell fusion, but molecular structural information about cholesterol-gp41 interaction is so far absent.
B. Kwon   +5 more
semanticscholar   +1 more source

Concerted interactions between multiple gp41 trimers and the target cell lipidome may be required for HIV-1 entry

open access: yesbioRxiv, 2020
The HIV-1 envelope glycoprotein gp41 mediates the fusion between viral and host cell membranes leading to virus entry and target cell infection. Despite years of research, important aspects of this process such as the number of gp41 trimers involved and ...
Biswajit Gorai   +4 more
semanticscholar   +1 more source

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