Journal
CURRENT OPINION IN HIV AND AIDS
Volume 12, Issue 3, Pages 250-256Publisher
LIPPINCOTT WILLIAMS & WILKINS
DOI: 10.1097/COH.0000000000000364
Keywords
10E8; 2F5; 4E10; Gp41; membrane proximal external region
Categories
Funding
- European EAVI program
- European EHVA program
- platforms of the Grenoble Instruct Center (ISBG
- UMS CNRS-CEA-UJF-EMBL) - French Infrastructure for Integrated Structural Biology Initiative FRISBI [3518, ANR-10-INSB-05-02]
- GRAL within the Grenoble Partnership for Structural Biology (PSB) [ANR-10-LABX-49-01]
Ask authors/readers for more resources
Purpose of review We summarize the latest research on the progress to understand the neutralizing epitopes present within the membrane proximal external region (MPER) of the HIV-1 fusion protein subunit gp41. Recent findings The HIV-1 fusion protein subunit gp41 contains a highly conserved sequence that is essential for membrane fusion and targeted by broadly neutralizing antibodies such as 2F5, 4E10, Z13e1, and 10E8. These antibodies recognize a linear gp41 epitope with high affinity, but require additional hydrophobic sequences present in their heavy chain CDR3 for neutralization. Recent structural studies on mAbs 4E10 and 10E8 provide molecular details for specific interactions with lipids and implicate part of the transmembrane region as the relevant 10E8 epitope. Although many different approaches have been applied to engineer gp41 immunogens that can induce broadly neutralizing antibodies directed toward MPER, only modest success has yet been reported. Summary The new structural details on the complex gp41-lipidic epitope will spur new approaches to design gp41MPER immunogens that might induce broadly neutralizing antibody responses.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available