The nucleocapsid protein isolated from HIV-1 particles binds zinc and forms retroviral-type zinc fingers

Biochemistry. 1990 Aug 28;29(34):7786-9. doi: 10.1021/bi00486a002.

Abstract

The role of zinc in retroviral gag protein function has been addressed through the application of high-resolution nuclear magnetic resonance spectroscopy to samples of the nucleocapsid protein (NCP, p7) isolated directly from infectious HIV-1 particles. Unlike reports for the NCP from avian myeloblastosis virus (AMV) particles [Jentoft et al. (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 7094], we find that the HIV-1 NCP binds 2 equiv of zinc tightly and stoichiometrically. Two-dimensional NMR spectroscopic studies reveal that zinc binding induces formation of folded domains that are conformationally similar to (if not identical with) structures observed previously for relevant retroviral-type (RT) zinc finger peptides [formerly called zinc fingerlike peptides; Summers et al. (1990) Biochemistry 29, 329]. This finding is consistent with the hypothesis that the inability of mutant proteins (with substituted Cys and His residues) to package viral RNA results from deficient zinc-binding capability, which may have significant consequences in the development of vaccines for the prevention of AIDS.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Capsid / isolation & purification*
  • HIV-1 / analysis*
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Viral Core Proteins / isolation & purification*
  • Virion / analysis*
  • Zinc / metabolism*
  • Zinc Fingers*

Substances

  • Viral Core Proteins
  • Zinc