Abstract
HIV-1 fusion of host-cell and viral membranes is induced by the transmembrane subunit gp41 of the envelope glycoprotein (Env). Antibodies targeting the C-terminal sequence of the Membrane-Proximal External Region (C-MPER) exert potent and broad neutralization of HIV-1 by blocking the fusogenic activity of gp41. Thus, recreating the structure that generates broadly neutralizing C-MPER antibodies during infection is a major goal in HIV vaccine development. Here, we have reconstituted peptides that contain the C-MPER epitope and the TMD residues required for the anchorage of the Env glycoprotein in lipid bilayers, and analyzed peptide structure, membrane perturbations and immunogenicity of the resulting Lipid-Peptide Formulations (LPFs).
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
