Deletions in the fifth alpha helix of HIV-1 Matrix block virus release
| Autor: | You Zhou, Christian J. Madson, Yan Li, Bridget Sanford, Han Chen, Michael Belshan, Connor J. Maly |
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| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Protein Conformation
NEDD4L viruses Mutant Mutagenesis (molecular biology technique) HIV-1 budding Biology Article Cell Line Viral Matrix Proteins Protein structure Microscopy Electron Transmission Virology Humans Amino Acid Sequence HIV-1 assembly Virus Release Viral matrix protein Matrix Cell Membrane Wild type Deletion mutagenesis Alanine scanning Molecular biology Protein Structure Tertiary Viral replication HIV-1 Gene Deletion |
| Popis: | 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 (MA∆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∆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 α5 of MA inhibits virus release. |
| Databáze: | OpenAIRE |
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