Evidence map›Paper›PMID 28863165›Full record

ArticlePloS one2017

Comprehensive analysis of amino acid sequence diversity at the F protein cleavage site of Newcastle disease virus in fusogenic activity.

Yanhong Wang, Wanqi Yu, Na Huo, Wenbin Wang, Yuanyuan Guo, Qiaolin Wei, Xinglong Wang, Shuxia Zhang, Zengqi Yang, Sa Xiao

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 1 pooled it
1.6field-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

28 citing papers in PubMed, 1 synthesis or guideline pooled it, 40 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

10 authors at 1 institution in 1 country.

Yanhong WangCollege of Veterinary Medicine, Northwest A&F University, Yangling, Shaanxi, P.R. China.
Wanqi YuCollege of Veterinary Medicine, Northwest A&F University, Yangling, Shaanxi, P.R. China.
Na HuoCollege of Veterinary Medicine, Northwest A&F University, Yangling, Shaanxi, P.R. China.
Wenbin WangCollege of Veterinary Medicine, Northwest A&F University, Yangling, Shaanxi, P.R. China.
Yuanyuan GuoCollege of Veterinary Medicine, Northwest A&F University, Yangling, Shaanxi, P.R. China.
Qiaolin WeiCollege of Veterinary Medicine, Northwest A&F University, Yangling, Shaanxi, P.R. China.
Xinglong WangCollege of Veterinary Medicine, Northwest A&F University, Yangling, Shaanxi, P.R. China.
Shuxia ZhangCollege of Veterinary Medicine, Northwest A&F University, Yangling, Shaanxi, P.R. China.
Zengqi YangCollege of Veterinary Medicine, Northwest A&F University, Yangling, Shaanxi, P.R. China.
Sa XiaoCollege of Veterinary Medicine, Northwest A&F University, Yangling, Shaanxi, P.R. China.ORCID http://orcid.org/0000-0003-3444-7241
Northwest A&F University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Newcastle disease virus (NDV) is a contagious agent of Newcastle disease in avian species and seriously affects the poultry industry. The cleavage site of the viral F protein (Fcs) is a key determinant of membrane fusion and viral virulence. In this study, we investigated the precise effect of variable amino acid sequences of the Fcs on fusogenic activity. Based on viral pathogenicity, the Fcs sequences of natural isolates (n = 1572) are classified into eight types of virulent Fcs (VFcs) with the motif "G/R/K-R-Q/R/K-R/K-R↓F" and ten types of the avirulent Fcs (AFcs) with the motif "G/R/E-R/K/Q-Q-G/E-R↓L". The VFcs is only found in the Class II cluster of viral classification and not in Class I. The AFcs exists in both Class I and II isolates. The VFc and AFc types present an evolutionary relationship with temporal distribution and host species. Using a fusion assay in vitro, VFcs-1 "RRQKR↓F" and VFcs-2 "RRQRR↓F" show the highest efficiency in triggering membrane fusion. The neutral residue Q at the P3 position of the VFcs plays an enhancing role compared to effect of the basic residues R and K. A single residue K at P3 or P5 is less efficient of the fusogenic activity in the VFcs with all basic residues. Moreover, the cleavage efficiencies of F0 proteins with different types of Fcs motifs do not appear to affect membrane fusion. Our findings offer insight into the effect of amino acid variation of the Fcs on the fusion triggered by NDV.

Indexed as

Amino AcidsCodonDNA Mutational AnalysisEvolution, MolecularGenome, ViralNewcastle disease virusNucleotidesPrincipal Component AnalysisRecombination, GeneticViral Fusion ProteinsVirulenceVirus ReplicationAmino AcidsCodonNucleotidesViral Fusion Proteins

Identifiers

PMID28863165
PMCPMC5580908
OpenAlexW2753325553

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.