Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site
| Author(s) | Liu, Chuang | |
| Author(s) | Perilla, Juan R. | |
| Author(s) | Ning, Jiying | |
| Author(s) | Lu, Manman | |
| Author(s) | Hou, Guangjin | |
| Author(s) | Ramalho, Ruben | |
| Author(s) | Himes, Benjamin A. | |
| Author(s) | Zhao, Gongpu | |
| Author(s) | Bedwell, Gregory J. | |
| Author(s) | Byeon, In-Ja | |
| Author(s) | Ahn, Jinwoo | |
| Author(s) | Gronenborn, Angela M. | |
| Author(s) | Prevelige, Peter E. | |
| Author(s) | Rousso, Itay | |
| Author(s) | Aiken, Christopher | |
| Author(s) | Polenova, Tatyana | |
| Author(s) | Schulten, Klaus | |
| Author(s) | Zhang, Peijun | |
| Ordered Author | Chuang Liu, Juan R. Perilla, Jiying Ning, Manman Lu, Guangjin Hou, Ruben Ramalho, Benjamin A. Himes, Gongpu Zhao, Gregory J. Bedwell, In-Ja Byeon, Jinwoo Ahn, Angela M. Gronenborn, Peter E. Prevelige, Itay Rousso, Christopher Aiken, Tatyana Polenova, Klaus Schulten & Peijun Zhang | |
| UD Author | Lu, Manman | en_US |
| UD Author | Hou, Guangjin | en_US |
| UD Author | Polenova, Tatyana | en_US |
| Date Accessioned | 2016-11-04T15:57:01Z | |
| Date Available | 2016-11-04T15:57:01Z | |
| Copyright Date | Copyright © | en_US |
| Publication Date | 2016-03-04 | |
| Description | Publisher's PDF | en_US |
| Abstract | 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-Å 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. | en_US |
| Department | University of Delaware. Department of Chemistry and Biochemistry. | en_US |
| Citation | Liu, C. et al. Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site. Nat. Commun. 7:10714 doi: 10.1038/ncomms10714 (2016). | en_US |
| DOI | DOI: 10.1038/ncomms10714 | en_US |
| ISSN | 2041-1723 | en_US |
| URL | http://udspace.udel.edu/handle/19716/19829 | |
| Language | en_US | en_US |
| Publisher | Nature Publishing Group | en_US |
| dc.rights | CC BY 4.0 | en_US |
| dc.source | Nature Communications | en_US |
| dc.source.uri | http://www.nature.com/ncomms/ | en_US |
| Title | Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site | en_US |
| Type | Article | en_US |
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