Deletions in the fifth alpha helix of HIV-1 matrix block virus release

Bridget Sanford, Yan Li, Connor J. Maly, Christian J. Madson, Han Chen, You Zhou, Michael Belshan

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

The matrix (MA) protein of HIV-1 is the N-terminal component of the Gag structural protein and is critical for the early and late stages of viral replication. MA contains five α-helices (α1-α5). Deletions in the N-terminus of α5 as small as three amino acids impaired virus release. Electron microscopy of one deletion mutant (MAΔ96-120) showed that its particles were tethered to the surface of cells by membranous stalks. Immunoblots indicated all mutants were processed completely, but mutants with large deletions had alternative processing intermediates. Consistent with the EM data, MAΔ96-120 retained membrane association and multimerization capability. Co-expression of this mutant inhibited wild type particle release. Alanine scanning mutation in this region did not affect virus release, although the progeny virions were poorly infectious. Combined, these data demonstrate that structural ablation of the α5 of MA inhibits virus release.

Original languageEnglish (US)
Pages (from-to)293-302
Number of pages10
JournalVirology
Volume468
DOIs
StatePublished - Nov 1 2014

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Keywords

  • Deletion mutagenesis
  • HIV-1 assembly
  • HIV-1 budding
  • Matrix
  • NEDD4L

ASJC Scopus subject areas

  • Virology

Cite this

Sanford, B., Li, Y., Maly, C. J., Madson, C. J., Chen, H., Zhou, Y., & Belshan, M. (2014). Deletions in the fifth alpha helix of HIV-1 matrix block virus release. Virology, 468, 293-302. https://doi.org/10.1016/j.virol.2014.08.017