Articles with "hiv gp41" as a keyword



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Changes in lipid bilayer structure caused by the helix-to-sheet transition of an HIV-1 gp41 fusion peptide derivative.

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Published in 2017 at "Chemistry and physics of lipids"

DOI: 10.1016/j.chemphyslip.2017.01.004

Abstract: HIV-1, like other enveloped viruses, undergoes fusion with the cell membrane to infect it. Viral coat proteins are thought to bind the virus to the membrane and actively fuse the viral and cellular membranes together.… read more here.

Keywords: transition; hiv gp41; lipid bilayer; bilayer ... See more keywords
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Conformational plasticity of the HIV-1 gp41 immunodominant region is recognized by multiple non-neutralizing antibodies.

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Published in 2022 at "Communications biology"

DOI: 10.1038/s42003-022-03235-w

Abstract: The early humoral immune response to acute HIV-1 infection is largely non-neutralizing. The principal target of these antibodies is the primary immunodominant region (PID) on the gp41 fusion protein. The PID is a highly conserved… read more here.

Keywords: non neutralizing; immunodominant region; hiv gp41; hiv ... See more keywords
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Proteoliposomal formulations of an HIV-1 gp41-based miniprotein elicit a lipid-dependent immunodominant response overlapping the 2F5 binding motif

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Published in 2017 at "Scientific Reports"

DOI: 10.1038/srep40800

Abstract: The HIV-1 gp41 Membrane Proximal External Region (MPER) is recognized by broadly neutralizing antibodies and represents a promising vaccine target. However, MPER immunogenicity and antibody activity are influenced by membrane lipids. To evaluate lipid modulation… read more here.

Keywords: response; hiv gp41; gp41; mper ... See more keywords