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Basic Characteristics of Mutations
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Mutation Site
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96_120del |
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Mutation Site Sentence
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Electron microscopy of one deletion mutant (MADelta96-120) showed that its particles were tethered to the surface of cells by membranous stalks. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Deletion |
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Gene/Protein/Region
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Gag |
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Standardized Encoding Gene
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Gag
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Genotype/Subtype
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HIV-1 |
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Viral Reference
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-
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Functional Impact and Mechanisms
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Disease
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Cell line
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Immune
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- |
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Target Gene
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-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
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- |
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Location
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- |
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Literature Information
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PMID
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25217711
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Title
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Deletions in the fifth alpha helix of HIV-1 matrix block virus release
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Author
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Sanford B,Li Y,Maly CJ,Madson CJ,Chen H,Zhou Y,Belshan M
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Journal
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Virology
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Journal Info
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2014 Nov;468-470:293-302
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Abstract
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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 alpha-helices (alpha1-alpha5). Deletions in the N-terminus of alpha5 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 alpha5 of MA inhibits virus release.
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Sequence Data
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-
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