Evidence map›Paper›PMID 25217711›Full record

ArticleVirology2014

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

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed.

  1. Research progress on the mechanism of exosome-mediated virus infection.Frontiers in cellular and infection microbiology · 2024
    Review
  2. Article
  3. Article
  4. Article
  5. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Bridget SanfordDepartment of Medical Microbiology and Immunology, Creighton University, 2500 California Plaza, Omaha, NE 68178, USA.
Yan LiDepartment of Medical Microbiology and Immunology, Creighton University, 2500 California Plaza, Omaha, NE 68178, USA.
Connor J MalyDepartment of Medical Microbiology and Immunology, Creighton University, 2500 California Plaza, Omaha, NE 68178, USA.
Christian J MadsonDepartment of Medical Microbiology and Immunology, Creighton University, 2500 California Plaza, Omaha, NE 68178, USA.
Han ChenCenter for Biotechnology, University of Nebraska-Lincoln, Lincoln, NE, USA.
You ZhouCenter for Biotechnology, University of Nebraska-Lincoln, Lincoln, NE, USA; Nebraska Center for Virology, Lincoln, NE, USA.
Michael BelshanDepartment of Medical Microbiology and Immunology, Creighton University, 2500 California Plaza, Omaha, NE 68178, USA; Nebraska Center for Virology, Lincoln, NE, USA. Electronic address: michaelbelshan@creighton.edu.

Funding

Nebraska Center for VirologyP30GM103509 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI WOOD, CHARLES · 2012 to 2014
$3.3M
A Proteomic and Biochemical Study of HIV-1 Nucleoprotein ComplexesR01AI080348 · NIAID · CREIGHTON UNIVERSITY · PI BELSHAN, MICHAEL A · 2010 to 2014
$1.8M
NIAID NIH HHS AI080348NIAID NIH HHS R01 AI080348NIGMS NIH HHS GM103509NIGMS NIH HHS P30 GM103509
6 · The paper itself

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 (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.

Indexed as

Gene DeletionAmino Acid SequenceCell LineCell MembraneHIV-1HumansMicroscopy, Electron, TransmissionProtein ConformationProtein Structure, TertiaryViral Matrix ProteinsVirus ReleaseViral Matrix ProteinsDeletion mutagenesisHIV-1 assemblyHIV-1 buddingMatrixNEDD4L

Identifiers

PMID25217711
PMCPMC4253686

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.