Evidence map›Paper›PMID 24109216›Full record

ArticleJournal of virology2013

Effect of multimerization on membrane association of Rous sarcoma virus and HIV-1 matrix domain proteins.

Robert A Dick, Elena Kamynina, Volker M Vogt

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

32 citing papers in PubMed, 37 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Robert A DickDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, New York, USA.
Elena Kamynina
Volker M Vogt
Cornell University · US

Funding

AVIAN RETROVIRUS STRUCTURE AND ASSEMBLYR01CA020081 · NCI · CORNELL UNIVERSITY ITHACA · PI VOGT, VOLKER M. · 1985 to 2011
$3.9M
Structure and Assembly of RetrovirusesR01GM107013 · NIGMS · CORNELL UNIVERSITY · PI VOGT, VOLKER M. · 2013 to 2018
$1.5M
AVIAN RETROVIRUS STRUCTURE AND ASSEMBLYR37CA020081 · NCI · CORNELL UNIVERSITY ITHACA · PI VOGT, VOLKER M. · 1988 to 1995
–
NCI NIH HHS CA20081-34NCI NIH HHS R01 CA020081NIGMS NIH HHS GM107013-35NIGMS NIH HHS R01 GM107013
6 · The paper itself

Abstract

In most retroviruses, plasma membrane (PM) association of the Gag structural protein is a critical step in viral assembly, relying in part on interaction between the highly basic Gag MA domain and the negatively charged inner leaflet of the PM. Assembly is thought to begin with Gag dimerization followed by multimerization, resulting in a hexameric lattice. To directly address the role of multimerization in membrane binding, we fused the MA domains of Rous sarcoma virus (RSV) and HIV-1 to the chemically inducible dimerization domain FK506-binding protein (FKBP) or to the hexameric protein CcmK4 from cyanobacteria. The cellular localization of the resulting green fluorescent protein (GFP)-tagged chimeric proteins was examined by fluorescence imaging, and the association of the proteins with liposomes was quantified by flotation in sucrose gradients, following synthesis in a reticulocyte extract or as purified proteins. Four lipid compositions were tested, representative of liposomes commonly reported in flotation experiments. By themselves, GFP-tagged RSV and HIV-1 MA proteins were largely cytoplasmic, but both hexamerized proteins were highly concentrated at the PM. Dimerization led to partial PM localization for HIV-1 MA. These in vivo effects of multimerization were reproduced in vitro. In flotation analyses, the intact RSV and HIV-1 Gag proteins were more similar to multimerized MA than to monomeric MA. RNA is reported to compete with acidic liposomes for HIV-1 Gag binding, and thus we also examined the effects of RNase treatment or tRNA addition on flotation. tRNA competed with liposomes in the case of some but not all lipid compositions and ionic strengths. Taken together, our results further underpin the model that multimerization is critical for PM association of retroviral Gag proteins. In addition, they suggest that the modulation of membrane binding by RNA, as previously reported for HIV-1, may not hold for RSV.

Indexed as

AnimalsCell LineCell MembraneCytoplasmgag Gene Products, Human Immunodeficiency VirusGene Products, gagHIV-1HIV InfectionsHumansProtein MultimerizationProtein Structure, TertiaryQuailRous sarcoma virusSarcoma, Aviangag Gene Products, Human Immunodeficiency VirusGene Products, gag

Identifiers

PMID24109216
PMCPMC3838224
OpenAlexW2105093369

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.