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

作者：Sanford Bridget; Li Yan; Maly Connor J; Madson Christian J; Chen Han; Zhou You; Belshan Michael^*

来源：Virology, 2014, 468: 293-302.

DOI：10.1016/j.virol.2014.08.017

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

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 a-helices (alpha 1-alpha 5). Deletions in the N-terminus of alpha 5 as small as three amino acids impaired virus release. Electron microscopy of one deletion mutant (MA Delta 96-120) 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, MA Delta 96-120 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 alpha 5 of MA inhibits virus release.

• 出版日期2014-11