Evidence map›Paper›PMID 16439527›Full record

ArticleJournal of virology2006

Function of small hydrophobic proteins of paramyxovirus.

Rebecca L Wilson, Sandra M Fuentes, Ping Wang, Erica C Taddeo, Alicia Klatt, Andrew J Henderson, Biao He

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
5.1field-weighted citation impact, top 5% 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

71 citing papers in PubMed, 127 citations in OpenAlex.

  1. Review
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  7. Small hydrophobic (SH) proteins ofJournal of virology · 2024
    Review
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11 more citing papers are in PubMed but not listed here.

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

7 authors at 1 institution in 2 countries.

Rebecca L WilsonCenter of Molecular Immunology and Infectious Disease, Department of Veterinary and Biomedical Sciences, Pennsylvania State University, 115 Henning Bldg., University Park, PA 16802, USA.
Sandra M Fuentes
Ping Wang
Erica C Taddeo
Alicia Klatt
Andrew J Henderson
Biao He
Intercollege · CY

Funding

Activation and Inhibition of Apoptotic Pathways by SV5R01AI051372 · NIAID · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI HE, BIAO · 2003 to 2007
$1.2M
NIAID NIH HHS AI 051372NIAID NIH HHS R01 AI051372
6 · The paper itself

Abstract

Mumps virus (MuV), a rubulavirus of the paramyxovirus family, causes acute infections in humans. MuV has seven genes including a small hydrophobic (SH) gene, which encodes a type I membrane protein of 57 amino acid residues. The function of the SH protein is not clear, although its expression is not necessary for growth of MuV in tissue culture cells. It is speculated that MuV SH plays a role in viral pathogenesis. Simian virus 5 (SV5), a closely related rubulavirus, encodes a 44-amino-acid-residue SH protein. Recombinant SV5 lacking the SH gene (rSV5DeltaSH) is viable and has no growth defect in tissue culture cells. However, rSV5DeltaSH induces apoptosis in tissue culture cells and is attenuated in vivo. Neutralizing antibodies against tumor necrosis factor alpha (TNF-alpha) and TNF-alpha receptor 1 block rSV5DeltaSH-induced apoptosis, suggesting that SV5 SH plays an essential role in blocking the TNF-alpha-mediated apoptosis pathway. Because MuV is closely related to SV5, we hypothesize that the SH protein of MuV has a function similar to that of SV5, even though there is no sequence homology between them. To test this hypothesis and to study the function of MuV SH, we have replaced the open reading frame (ORF) of SV5 SH with the ORF of MuV SH in a SV5 genome background. The recombinant SV5 (rSV5DeltaSH+MuV-SH) was analyzed in comparison with SV5. It was found that rSV5DeltaSH+MuV-SH was viable and behaved like wild-type SV5, suggesting that MuV SH has a function similar to that of SV5 SH. Furthermore, both ectopically expressed SV5 SH and MuV SH blocked activation of NF-kappaB by TNF-alpha in a reporter gene assay, suggesting that both SH proteins can inhibit TNF-alpha signaling.

Indexed as

AnimalsApoptosisCattleCell LineChlorocebus aethiopsCytopathogenic Effect, ViralHumansMiceModels, BiologicalMumps virusParainfluenza Virus 5Recombination, GeneticRetroviridae Proteins, OncogenicTumor Necrosis Factor-alphaViral Plaque AssayViral ProteinsRetroviridae Proteins, Oncogenicsmall hydrophobic protein, Mumps virussmall hydrophobic protein, virusTumor Necrosis Factor-alphaViral Proteins

Identifiers

PMID16439527
PMCPMC1367141
OpenAlexW2058143909

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.