Evidence map›Paper›PMID 21304939›Full record

ArticlePLoS pathogens2011

Charge-surrounded pockets and electrostatic interactions with small ions modulate the activity of retroviral fusion proteins.

Daniel Lamb, Alexander W Schüttelkopf, Daan M F van Aalten, David W Brighty

Open access · goldAbstract readComparative Study
In one paragraph

Article in PLoS pathogens, 2011. 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
0.8field-weighted citation impact, top 33% 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, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Crystal structures of MBP fusion proteins.Protein science : a publication of the Protein Society · 2016
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Structural characterization of a fusion glycoprotein from a retrovirus that undergoes a hybrid 2-step entry mechanism.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    Article
  13. 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 at 2 institutions in 1 country.

Daniel LambThe Biomedical Research Institute, College of Medicine, Ninewells Hospital, The University of Dundee, Dundee, UK.
Alexander W Schüttelkopf
Daan M F van Aalten
David W Brighty
University of Dundee · GBNinewells Hospital · GB

Funding

Medical Research Council G0900138Medical Research Council G0900138(90614)Wellcome Trust 087590
6 · The paper itself

Abstract

Refolding of viral class-1 membrane fusion proteins from a native state to a trimer-of-hairpins structure promotes entry of viruses into cells. Here we present the structure of the bovine leukaemia virus transmembrane glycoprotein (TM) and identify a group of asparagine residues at the membrane-distal end of the trimer-of-hairpins that is strikingly conserved among divergent viruses. These asparagines are not essential for surface display of pre-fusogenic envelope. Instead, substitution of these residues dramatically disrupts membrane fusion. Our data indicate that, through electrostatic interactions with a chloride ion, the asparagine residues promote assembly and profoundly stabilize the fusion-active structures that are required for viral envelope-mediated membrane fusion. Moreover, the BLV TM structure also reveals a charge-surrounded hydrophobic pocket on the central coiled coil and interactions with basic residues that cluster around this pocket are critical to membrane fusion and form a target for peptide inhibitors of envelope function. Charge-surrounded pockets and electrostatic interactions with small ions are common among class-1 fusion proteins, suggesting that small molecules that specifically target such motifs should prevent assembly of the trimer-of-hairpins and be of value as therapeutic inhibitors of viral entry.

Indexed as

Protein FoldingStatic ElectricityAmino Acid SequenceAnimalsAnti-Retroviral AgentsCatalytic DomainCattleHumansHuman T-lymphotropic virus 1Hydrogen BondingIonsLeukemia Virus, BovineModels, MolecularMolecular Sequence DataProtein ConformationProtein Structure, TertiaryAnti-Retroviral AgentsIonsRecombinant Fusion ProteinsRetroviridae ProteinsViral Envelope Proteins

Identifiers

PMID21304939
PMCPMC3033372
OpenAlexW2052188940

What OpenQuestion holds

Textmetadata
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.