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TitleMolecular Determinants of PQBP1 Binding to the HIV-1 Capsid Lattice.
Journal, issue, pagesJ Mol Biol, Vol. 436, Issue 4, Page 168409, Year 2024
Publish dateFeb 15, 2024
AuthorsJuliana Piacentini / Dale S Allen / Barbie K Ganser-Pornillos / Sumit K Chanda / Sunnie M Yoh / Owen Pornillos /
PubMed AbstractHuman immunodeficiency virus type 1 (HIV-1) stimulates innate immune responses upon infection, including cyclic GMP-AMP synthase (cGAS) signaling that results in type I interferon production. HIV-1- ...Human immunodeficiency virus type 1 (HIV-1) stimulates innate immune responses upon infection, including cyclic GMP-AMP synthase (cGAS) signaling that results in type I interferon production. HIV-1-induced activation of cGAS requires the host cell factor polyglutamine binding protein 1 (PQBP1), an intrinsically disordered protein that bridges capsid recognition and cGAS recruitment. However, the molecular details of PQBP1 interactions with the HIV-1 capsid and their functional implications remain poorly understood. Here, we show that PQBP1 binds to HIV-1 capsids through charge complementing contacts between acidic residues in the N-terminal region of PQBP1 and an arginine ring in the central channel of the HIV-1 CA hexamer that makes up the viral capsid. These studies reveal the molecular details of PQBP1's primary interaction with the HIV-1 capsid and suggest that additional elements are likely to contribute to stable capsid binding.
External linksJ Mol Biol / PubMed:38128824 / PubMed Central
MethodsEM (single particle)
Resolution3.3 Å
Structure data

41711

8ty6

EMDB-41711, PDB-8ty6:
Disulfide-stabilized HIV-1 CA hexamer in complex with PQBP1 Nt
Method: EM (single particle) / Resolution: 3.3 Å

Source
  • human immunodeficiency virus 1
KeywordsVIRAL PROTEIN / capsid / innate immune sensor

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