Evidence map›Paper›PMID 24227839›Full record

ArticleJournal of virology2014

Retrovirus-specific differences in matrix and nucleocapsid protein-nucleic acid interactions: implications for genomic RNA packaging.

Meng Sun, Iwen F Grigsby, Robert J Gorelick, Louis M Mansky, Karin Musier-Forsyth

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Journal of virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 20% of its field
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

25 citing papers in PubMed, 1 synthesis or guideline pooled it, 29 citations in OpenAlex.

  1. HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016
    Pooled it
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  8. Molecular Biology and Diversification of Human Retroviruses.Frontiers in virology (Lausanne, Switzerland) · 2022
    Article
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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

5 authors at 3 institutions in 1 country.

Meng SunDepartment of Chemistry and Biochemistry, Center for Retroviral Research, and Center for RNA Biology, The Ohio State University, Columbus, Ohio, USA.
Iwen F Grigsby
Robert J Gorelick
Louis M Mansky
Karin Musier-Forsyth
The Ohio State University · USUniversity of Minnesota · USLeidos (United States) · US

Funding

RNA Binding and Packaging By Retroviral Gag ProteinsR01GM065056 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI MUSIER-FORSYTH, KARIN M · 2002 to 2018
$4.9M
Dicentric chromosome formation and stability in humansR01GM098500 · NIGMS · DUKE UNIVERSITY · PI SULLIVAN, BETH A · 2012 to 2015
$1.3M
CCR NIH HHS HHSN261200800001CIntramural NIH HHSNCI NIH HHS HHSN261200800001ENIGMS NIH HHS GM065056NIGMS NIH HHS GM098500NIGMS NIH HHS R01 GM065056NIGMS NIH HHS R01 GM098500
6 · The paper itself

Abstract

Retroviral RNA encapsidation involves a recognition event between genomic RNA (gRNA) and one or more domains in Gag. In HIV-1, the nucleocapsid (NC) domain is involved in gRNA packaging and displays robust nucleic acid (NA) binding and chaperone functions. In comparison, NC of human T-cell leukemia virus type 1 (HTLV-1), a deltaretrovirus, displays weaker NA binding and chaperone activity. Mutation of conserved charged residues in the deltaretrovirus bovine leukemia virus (BLV) matrix (MA) and NC domains affects virus replication and gRNA packaging efficiency. Based on these observations, we hypothesized that the MA domain may generally contribute to NA binding and genome encapsidation in deltaretroviruses. Here, we examined the interaction between HTLV-2 and HIV-1 MA proteins and various NAs in vitro. HTLV-2 MA displays higher NA binding affinity and better chaperone activity than HIV-1 MA. HTLV-2 MA also binds NAs with higher affinity than HTLV-2 NC and displays more robust chaperone function. Mutation of two basic residues in HTLV-2 MA α-helix II, previously implicated in BLV gRNA packaging, reduces NA binding affinity. HTLV-2 MA binds with high affinity and specificity to RNA derived from the putative packaging signal of HTLV-2 relative to nonspecific NA. Furthermore, an HIV-1 MA triple mutant designed to mimic the basic character of HTLV-2 MA α-helix II dramatically improves binding affinity and chaperone activity of HIV-1 MA in vitro and restores RNA packaging to a ΔNC HIV-1 variant in cell-based assays. Taken together, these results are consistent with a role for deltaretrovirus MA proteins in viral RNA packaging.

Indexed as

Virus AssemblyAmino Acid MotifsAmino Acid SequenceAnimalsCattlegag Gene Products, Human Immunodeficiency VirusHIV-1HIV AntigensHIV InfectionsHTLV-II InfectionsHumansHuman T-lymphotropic virus 2Nucleocapsid ProteinsProtein BindingProtein Structure, SecondaryRNA, Viralgag Gene Products, Human Immunodeficiency VirusHIV AntigensNucleocapsid Proteinsp17 protein, Human Immunodeficiency Virus Type 1RNA, Viral

Identifiers

PMID24227839
PMCPMC3911680
OpenAlexW2107758050

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.