Evidence map›Paper›PMID 15731243›Full record

ArticleJournal of virology2005

Receptor-induced conformational changes in the SU subunit of the avian sarcoma/leukosis virus A envelope protein: implications for fusion activation.

Sue E Delos, Jesse A Godby, Judith M White

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2005. 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
1.4field-weighted citation impact, top 18% 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, 19 citations in OpenAlex.

  1. Review
  2. Review
  3. Fusion of Enveloped Viruses in Endosomes.Traffic (Copenhagen, Denmark) · 2016
    Review
  4. 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
  5. Article
  6. Article
  7. Anterograde or retrograde transsynaptic labeling of CNS neurons with vesicular stomatitis virus vectors.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
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.

Sue E DelosDepartment of Cell Biology, UVA Health System, School of Medicine, P.O. Box 800732, Charlottesville, VA 22908-0732, USA. sed7a@virginia.edu
Jesse A Godby
Judith M White
University of Virginia · US

Funding

MOLECULAR MECHANISMS OF VIRAL MEMBRANE FUSION PROTEINSR01AI022470 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI WHITE, JUDITH M. · 1985 to 2009
$3.4M
NIAID NIH HHS AI22470NIAID NIH HHS R01 AI022470
6 · The paper itself

Abstract

The avian sarcoma/leukosis virus (ASLV) is activated for fusion by a two-step mechanism. For ASLV subgroup A (ASLV-A), association with its receptor (Tva) at neutral pH converts virions to a form that can bind target membranes and, in some assays, induce the lipid-mixing stage of fusion. Low pH is necessary to complete the fusion reaction. ASLV-A env (EnvA) exists on the viral surface as a trimer of heterodimers consisting of receptor binding (SU-A) and fusion-mediating (TM-A) subunits. As the receptor binding and fusion-mediating functions reside in separate subunits, we hypothesize that SU-A and TM-A are conformationally coupled. To begin to understand the effect of the binding of a soluble 47-residue domain of the receptor (sTva) on this coupling and the subsequent function of low pH, we prepared recombinant proteins representing full-length SU-A and a nested set of deletion mutant proteins. Full-length SU-A binds sTva with high affinity, but even small deletions at either the N or the C terminus severely impair sTva binding. We have purified the full-length SU-A subunit and characterized its interactions with sTva and the subsequent effect of low pH on the complex. sTva binds SU-A with an apparent KD of 3 pM. Complex formation occludes hydrophobic surfaces and tryptophan residues and leads to a partial loss of alpha-helical structure in SU-A. Low pH does not alter the off rate for the complex, further alter the secondary structure of SU-A, or induce measurable changes in tryptophan environment. The implications of these findings for fusion are discussed.

Indexed as

Protein ConformationAvian Leukosis VirusAvian ProteinsAvian Sarcoma VirusesCircular DichroismHydrogen-Ion ConcentrationMembrane FusionProtein BindingProtein Structure, TertiaryProtein SubunitsReceptors, VirusRecombinant ProteinsSequence DeletionSolubilitySpectrometry, FluorescenceSurface Plasmon ResonanceAvian Proteinsglycoprotein 85, avian leukosis virusProtein SubunitsReceptors, VirusRecombinant ProteinsTva receptorViral Envelope Proteins

Identifiers

PMID15731243
PMCPMC1075726
OpenAlexW2160730921

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.