HIV-1 matrix domain removal ameliorates virus assembly and processing defects incurred by positive nucleocapsid charge elimination.

Li-Jung Ko, Fu-Hsien Yu, Kuo-Jung Huang, Chin-Tien Wang

Abstract read

In one paragraph

Article in FEBS open bio, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it

0cells of the map it votes in

2citing 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

2 citing papers in PubMed.

In vitro protease cleavage and computer simulations reveal the HIV-1 capsid maturation pathway.Nature communications · 2016
Article
Glutamic Acid Residues in HIV-1 p6 Regulate Virus Budding and Membrane Association of Gag.Viruses · 2016
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

4 authors.

Li-Jung KoDepartment of Medical Research, Taipei Veterans General Hospital, Taipei, Taiwan ; Institute of Public Health, National Yang-Ming University School of Medicine, Taipei, Taiwan.

Fu-Hsien YuInstitute of Clinical Medicine, National Yang-Ming University School of Medicine, Taipei, Taiwan.

Kuo-Jung HuangDepartment of Medical Research, Taipei Veterans General Hospital, Taipei, Taiwan.

Chin-Tien WangDepartment of Medical Research, Taipei Veterans General Hospital, Taipei, Taiwan ; Institute of Clinical Medicine, National Yang-Ming University School of Medicine, Taipei, Taiwan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human immunodeficiency virus type 1 nucleocapsid (NC) basic residues presumably contribute to virus assembly via RNA, which serves as a scaffold for Gag-Gag interaction during particle assembly. To determine whether NC basic residues play a role in Gag cleavage (thereby impacting virus assembly), Gag processing efficiency and virus particle production were analyzed for an HIV-1 mutant NC15A, with alanine serving as a substitute for all NC basic residues. Results indicate that NC15A significantly impaired virus maturation in addition to significantly affecting Gag membrane binding and assembly. Interestingly, removal of the matrix (MA) central globular domain ameliorated the NC15A assembly and processing defects, likely through enhancement of Gag multimerization and membrane binding capacities.

Indexed as

CA, capsidGag cleavageHIV-1MA, matrixMatrixMembrane associationNC, nucleocapsidNucleocapsidPR, viral proteaseVirus assemblyVLP, virus-like particle

Identifiers

PMID25905033

DOI10.1016/j.fob.2015.04.003

PMCPMC4402288

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LicenceCC BY-NC-ND

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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.