Evidence map›Paper›PMID 29588400›Full record

ArticlemBio2018

HIV-1 Uncoating and Reverse Transcription Require eEF1A Binding to Surface-Exposed Acidic Residues of the Reverse Transcriptase Thumb Domain.

Daniel J Rawle, Dongsheng Li, Joakim E Swedberg, Lu Wang, Dinesh C Soares, David Harrich

Open access · goldAbstract read
In one paragraph

Article in mBio, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

13 citing papers in PubMed, 22 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

6 authors at 3 institutions in 2 countries.

Daniel J RawleDepartment of Cell and Molecular Biology, QIMR Berghofer Medical Research Institute, Herston, Queensland, Australia.
Dongsheng LiDepartment of Cell and Molecular Biology, QIMR Berghofer Medical Research Institute, Herston, Queensland, Australia.
Joakim E SwedbergInstitute for Molecular Biosciences, University of Queensland, St. Lucia, Queensland, Australia.
Lu WangDepartment of Cell and Molecular Biology, QIMR Berghofer Medical Research Institute, Herston, Queensland, Australia.
Dinesh C SoaresMRC Institute of Genetics and Molecular Medicine, Western General Hospital, University of Edinburgh, Edinburgh, United Kingdom.
David HarrichDepartment of Cell and Molecular Biology, QIMR Berghofer Medical Research Institute, Herston, Queensland, Australia david.harrich@qimrberghofer.edu.au.
QIMR Berghofer Medical Research Institute · AUUniversity of Edinburgh · GBUniversity of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Once HIV-1 enters a cell, the viral core is uncoated by a poorly understood mechanism and the HIV-1 genomic RNA is reverse transcribed into DNA. Host cell factors are essential for these processes, although very few reverse transcription complex binding host cell factors have been convincingly shown to affect uncoating or reverse transcription. We previously reported that cellular eukaryotic translation elongation factor 1A (eEF1A) interacts tightly and directly with HIV-1 reverse transcriptase (RT) for more efficient reverse transcription. Here we report that the surface-exposed acidic residues in the HIV-1 RT thumb domain alpha-J helix and flanking regions are important for interaction with eEF1A. Mutation of surface-exposed acidic thumb domain residues D250, E297, E298, and E300 to arginine resulted in various levels of impairment of the interaction between RT and eEF1A. This indicates that this negatively charged region in the RT thumb domain is important for interaction with the positively charged eEF1A protein. The impairment of RT and eEF1A interaction by the RT mutations correlated with the efficiency of reverse transcription, uncoating, and infectivity. The best example of this is the strictly conserved E300 residue, where mutation significantly impaired the interaction of RT with eEF1A and virus replication in CD4

Indexed as

HEK293 CellsHeLa CellsHIV Reverse TranscriptaseHumansJurkat CellsMutagenesis, Site-DirectedMutationPeptide Elongation Factor 1Protein MultimerizationRibonuclease HVirus ReplicationEEF1A1 protein, humanHIV Reverse TranscriptasePeptide Elongation Factor 1reverse transcriptase, Human immunodeficiency virus 1Ribonuclease HeEF1Ahuman immunodeficiency virusreverse transcriptaseuncoatingvirus-host interactions

Identifiers

PMID29588400
PMCPMC5874916
OpenAlexW2791877860

What OpenQuestion holds

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LicenceCC BY
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.