Distinctive Membrane Accommodation Traits Underpinning the Neutralization Activity of HIV-1 Antibody against MPER.

ABSTRACT: The membrane-proximal external region (MPER), located in the carboxy-terminal section of HIV's envelope glycoprotein (Env) ectodomain, which is essential for viral entry into host cells, has gained considerable attention as a target for HIV vaccine development due to the exceptional neutralization breadth of antibodies against MPER epitopes. A distinctive feature of broadly neutralizing antibodies (bnAbs) targeting MPER is their requirement to accommodate the viral membrane into the surface of the antigen-binding fragment, or Fab moiety, to optimize antigen recognition. In this study, we sought to elucidate the molecular mechanism behind this interaction and its relevance to the antiviral function of bnAb 10E8. We conducted all-atom molecular dynamics simulations of three systems: (i) Fab

SUBMITTER: Domene C 

PROVIDER: S-EPMC12056697 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature