Journal
CELL
Volume 185, Issue 4, Pages 641-+Publisher
CELL PRESS
DOI: 10.1016/j.cell.2022.01.013
Keywords
-
Categories
Funding
- National Institutes of Health [S10OD032290]
- NIH NIGMS
- NIH NIAID [R01GM099989, R01AI140868, T32GM008268, R01AI143563]
- James B. Pendleton Charitable Trust
- University of Washington's Proteomics Resource [UWPR95794]
- Bill & Melinda Gates Foundation [OPP1126258]
- Bill and Melinda Gates Foundation [OPP1126258] Funding Source: Bill and Melinda Gates Foundation
Ask authors/readers for more resources
This study used cryo-electron tomography to analyze Env in HIV-1 particles and revealed distinct positioning of Env in immature particles relative to the underlying Gag lattice. Additionally, unexpected structural features of virion-bound Env, such as a variable central core and heterogeneous glycosylation, were discovered. These findings provide a comprehensive understanding of HIV assembly and structural variation in Env antigen presentation.
HIV-1 Env mediates viral entry into host cells and is the sole target for neutralizing antibodies. However, Env structure and organization in its native virion context has eluded detailed characterization. Here, we used cryo-electron tomography to analyze Env in mature and immature HIV-1 particles. Immature particles showed distinct Env positioning relative to the underlying Gag lattice, providing insights into long-standing questions about Env incorporation. A 9.1-A sub-tomogram-averaged reconstruction of virion-bound Env in conjunction with structural mass spectrometry revealed unexpected features, including a variable central core of the gp41 subunit, heterogeneous glycosylation between protomers, and a flexible stalk that allows Env tilting and variable exposure of neutralizing epitopes. Together, our results provide an integrative understanding of HIV assembly and structural variation in Env antigen presentation.
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