Evidence map›Paper›PMID 26813519›Full record

ArticleThe Journal of general virology2016

Morbillivirus and henipavirus attachment protein cytoplasmic domains differently affect protein expression, fusion support and particle assembly.

Bevan Sawatsky, Dennis A Bente, Markus Czub, Veronika von Messling

Open access · greenAbstract read
In one paragraph

Article in The Journal of general virology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Functional and antigenic constraints on the Nipah virus fusion protein.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Functional and antigenic constraints on the Nipah virus fusion protein.bioRxiv : the preprint server for biology · 2026
    Article
  3. Human Riboviruses: A Comprehensive Study.Journal of molecular evolution · 2025
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Emergence and adaptive evolution of Nipah virus.Transboundary and emerging diseases · 2020
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. 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

4 authors at 3 institutions in 3 countries.

Bevan SawatskyGalveston National Laboratory, University of Texas Medical Branch, Galveston, Texas, USA.
Dennis A BenteDepartment of Microbiology & Immunology, University of Texas Medical Branch, Galveston, Texas, USA.
Markus CzubFaculty of Veterinary Medicine, University of Calgary, Calgary, Alberta, Canada.
Veronika von MesslingINRS-Institut Armand-Frappier, University of Quebec, Laval, Quebec, Canada.
Institut National de la Recherche Scientifique · CAThe University of Texas Medical Branch at Galveston · USUniversity of Calgary · CA

Funding

Health, Safety and Training ServicesUC7AI070083 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI LEMON, STANLEY M. · 2006 to 2010
$49.5M
CIHR 66989NIAID NIH HHS UC7 AI070083
6 · The paper itself

Abstract

The amino-terminal cytoplasmic domains of paramyxovirus attachment glycoproteins include trafficking signals that influence protein processing and cell surface expression. To characterize the role of the cytoplasmic domain in protein expression, fusion support and particle assembly in more detail, we constructed chimeric Nipah virus (NiV) glycoprotein (G) and canine distemper virus (CDV) haemagglutinin (H) proteins carrying the respective heterologous cytoplasmic domain, as well as a series of mutants with progressive deletions in this domain. CDV H retained fusion function and was normally expressed on the cell surface with a heterologous cytoplasmic domain, while the expression and fusion support of NiV G was dramatically decreased when its cytoplasmic domain was replaced with that of CDV H. The cell surface expression and fusion support functions of CDV H were relatively insensitive to cytoplasmic domain deletions, while short deletions in the corresponding region of NiV G dramatically decreased both. In addition, the first 10 residues of the CDV H cytoplasmic domain strongly influence its incorporation into virus-like particles formed by the CDV matrix (M) protein, while the co-expression of NiV M with NiV G had no significant effect on incorporation of G into particles. The cytoplasmic domains of both the CDV H and NiV G proteins thus contribute differently to the virus life cycle.

Indexed as

Virus InternalizationAmino Acid SequenceGene Expression Regulation, ViralHenipavirusMorbillivirusViral Envelope ProteinsVirus AssemblyViral Envelope Proteins

Identifiers

PMID26813519
PMCPMC7482510
OpenAlexW2270213832

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.