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TitlePrion-like low complexity regions enable avid virus-host interactions during HIV-1 infection.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 5879, Year 2022
Publish dateOct 6, 2022
AuthorsGuochao Wei / Naseer Iqbal / Valentine V Courouble / Ashwanth C Francis / Parmit K Singh / Arpa Hudait / Arun S Annamalai / Stephanie Bester / Szu-Wei Huang / Nikoloz Shkriabai / Lorenzo Briganti / Reed Haney / Vineet N KewalRamani / Gregory A Voth / Alan N Engelman / Gregory B Melikyan / Patrick R Griffin / Francisco Asturias / Mamuka Kvaratskhelia /
PubMed AbstractCellular proteins CPSF6, NUP153 and SEC24C play crucial roles in HIV-1 infection. While weak interactions of short phenylalanine-glycine (FG) containing peptides with isolated capsid hexamers have ...Cellular proteins CPSF6, NUP153 and SEC24C play crucial roles in HIV-1 infection. While weak interactions of short phenylalanine-glycine (FG) containing peptides with isolated capsid hexamers have been characterized, how these cellular factors functionally engage with biologically relevant mature HIV-1 capsid lattices is unknown. Here we show that prion-like low complexity regions (LCRs) enable avid CPSF6, NUP153 and SEC24C binding to capsid lattices. Structural studies revealed that multivalent CPSF6 assembly is mediated by LCR-LCR interactions, which are templated by binding of CPSF6 FG peptides to a subset of hydrophobic capsid pockets positioned along adjoining hexamers. In infected cells, avid CPSF6 LCR-mediated binding to HIV-1 cores is essential for functional virus-host interactions. The investigational drug lenacapavir accesses unoccupied hydrophobic pockets in the complex to potently impair HIV-1 inside the nucleus without displacing the tightly bound cellular cofactor from virus cores. These results establish previously undescribed mechanisms of virus-host interactions and antiviral action.
External linksNat Commun / PubMed:36202818 / PubMed Central
MethodsEM (helical sym.) / X-ray diffraction
Resolution2.81 - 7.85 Å
Structure data

EMDB-27617: Helical reconstruction of A92E HIV capsid in complex with CPSF6 construct (filtered by local resolution)
Method: EM (helical sym.) / Resolution: 7.85 Å

EMDB-27619: Helical reconstruction of A92E HIV capsid in complex with CPSF6 construct (filtered by local resolution)
Method: EM (helical sym.) / Resolution: 7.4 Å

EMDB-27625: Helical reconstruction of A92E HIV capsid in presence of FG mutant CPSF6 construct (filtered by local resolution)
Method: EM (helical sym.) / Resolution: 7.0 Å

PDB-7snq:
Hexamer HIV-1 CA in complex with CPSF6 peptide and IP6 ligand
Method: X-RAY DIFFRACTION / Resolution: 2.81 Å

Chemicals

ChemComp-IHP:
INOSITOL HEXAKISPHOSPHATE / Phytic acid

ChemComp-CL:
Unknown entry / Chloride

ChemComp-HOH:
WATER / Water

Source
  • human immunodeficiency virus 1
  • human immunodeficiency virus type 1 group m subtype b (isolate bh10)
KeywordsVIRAL PROTEIN

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