Journal
NATURE COMMUNICATIONS
Volume 7, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms10714
Keywords
-
Categories
Funding
- National Institutes of Health NIGMS [R01GM085043, P50GM082251, P41GM104601, R01GM067887]
- National Science Foundation (NSF) [PHY-1430124]
- Israeli Science Foundation [1115/13]
- NSF [OCI-0725070, ACI-1238993, CHE0959496]
- Department of Energy [DE-AC05-00OR22725]
- NIGMS [P30GM110758]
- Direct For Mathematical & Physical Scien
- Division Of Physics [1430124] Funding Source: National Science Foundation
Ask authors/readers for more resources
The host cell factor cyclophilin A (CypA) interacts directly with the HIV-1 capsid and regulates viral infectivity. Although the crystal structure of CypA in complex with the N-terminal domain of the HIV-1 capsid protein (CA) has been known for nearly two decades, how CypA interacts with the viral capsid and modulates HIV-1 infectivity remains unclear. We determined the cryoEM structure of CypA in complex with the assembled HIV-1 capsid at 8-angstrom resolution. The structure exhibits a distinct CypA-binding pattern in which CypA selectively bridges the two CA hexamers along the direction of highest curvature. EM-guided all-atom molecular dynamics simulations and solid-state NMR further reveal that the CypA-binding pattern is achieved by single-CypA molecules simultaneously interacting with two CA subunits, in different hexamers, through a previously uncharacterized non-canonical interface. These results provide new insights into how CypA stabilizes the HIV-1 capsid and is recruited to facilitate HIV-1 infection.
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