Two structural switches in HIV-1 capsid regulate capsid curvature and host factor binding.
HIV-1
capsid
cryo-electron microscopy
retrovirus structure
virus-host interactions
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
18 04 2023
18 04 2023
Historique:
medline:
13
4
2023
entrez:
11
4
2023
pubmed:
12
4
2023
Statut:
ppublish
Résumé
The mature HIV-1 capsid protects the viral genome and interacts with host proteins to travel from the cell periphery into the nucleus. To achieve this, the capsid protein, CA, constructs conical capsids from a lattice of hexamers and pentamers, and engages in and then relinquishes multiple interactions with cellular proteins in an orchestrated fashion. Cellular host factors including Nup153, CPSF6, and Sec24C engage the same pocket within CA hexamers. How CA assembles pentamers and hexamers of different curvatures, how CA oligomerization states or curvature might modulate host-protein interactions, and how binding of multiple cofactors to a single site is coordinated, all remain to be elucidated. Here, using single-particle cryoEM, we have determined the structure of the mature HIV-1 CA pentamer and hexamer from conical CA-IP
Identifiants
pubmed: 37040417
doi: 10.1073/pnas.2220557120
pmc: PMC10120081
doi:
Substances chimiques
Capsid Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2220557120Subventions
Organisme : NIAID NIH HHS
ID : R01 AI147890
Pays : United States
Organisme : NIAID NIH HHS
ID : U54 AI150472
Pays : United States
Organisme : NIAID NIH HHS
ID : U54 AI170855
Pays : United States
Organisme : Medical Research Council
ID : MC_UP_1201/16
Pays : United Kingdom
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