Evidence map›Paper›PMID 28190135›Full record

ArticleVirus genes2017

Identification and characterization of Orf virus 050 protein proteolysis.

Han Wang, Junyi Jiang, Rui Ding, Xiaoping Wang, Meiying Liao, Jing Shao, Xiaohong Luo, Shuhong Luo, Chaohui Duan

Abstract read
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In one paragraph

Article in Virus genes, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.3field-weighted citation impact, top 49% 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

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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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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

9 authors at 4 institutions in 1 country.

Han WangDepartment of Laboratory Medicine, The Sun Yat-Sen Memorial Hospital, Sun Yat-Sen University, Guangzhou, 510120, Guangdong, People's Republic of China.
Junyi JiangDepartment of Laboratory Medicine, The Sun Yat-Sen Memorial Hospital, Sun Yat-Sen University, Guangzhou, 510120, Guangdong, People's Republic of China.
Rui DingDepartment of Laboratory Medicine, The Sun Yat-Sen Memorial Hospital, Sun Yat-Sen University, Guangzhou, 510120, Guangdong, People's Republic of China.
Xiaoping WangInstitute of Antibody Engineering, School of Biotechnology, Southern Medical University, Guangzhou, 510515, Guangdong, People's Republic of China.
Meiying LiaoDepartment of Laboratory Medicine, The Sun Yat-Sen Memorial Hospital, Sun Yat-Sen University, Guangzhou, 510120, Guangdong, People's Republic of China.
Jing ShaoGuangdong Provincial Key Laboratory of Malignant Tumor Epigenetics and Gene Regulation, The Sun Yat-Sen Memorial Hospital, Sun Yat-Sen University, Guangzhou, 510120, Guangdong, People's Republic of China.
Xiaohong LuoDepartment of Laboratory Medicine, The Sun Yat-Sen Memorial Hospital, Sun Yat-Sen University, Guangzhou, 510120, Guangdong, People's Republic of China.
Shuhong LuoDepartment of Laboratory Medicine, School of Stomatology and Medicine, Foshan University, 5 Hebin Road, Foshan, 528000, Guangdong, People's Republic of China. sluo815@gmail.com.
Chaohui DuanDepartment of Laboratory Medicine, The Sun Yat-Sen Memorial Hospital, Sun Yat-Sen University, Guangzhou, 510120, Guangdong, People's Republic of China. 1725012289@qq.com.
Sun Yat-sen Memorial Hospital · CNSun Yat-sen University · CNFoshan University · CNSouthern Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Orf virus 050 (ORFV050) gene is located in the core region of the ORFV genome. It is similar to Vaccinia virus (VV) Copenhagen L4R, and encodes the DNA-binding virion core protein VP8, which has structures similar to the VV P25K core protein and may undergo similar proteolytic processing during virus assembly. Three conserved Ala-Gly-X motifs at putative cleavage sites were identified in ORFV050. To investigate the proteolysis of ORFV050 and its participation in viral assembly, full-length and site-directed mutant ORFV050 recombinant proteins were constructed and expressed. Two distinct protein bands of 28.5 and 25 kDa were detected in the infected cells using anti-ORFV050 polyclonal antiserum. A potential cleavage site was identified at amino acids 30-32 of ORFV050. Mutation of AG/A to (R) in ORFV050 abolished the process of proteolysis. ORFV050 is a late gene synthesized during viral replication in the host cytoplasm. According to these results, we conclude that ORFV050 undergoes proteolysis and plays an important role in viral assembly.

Indexed as

ProteolysisAmino Acid SequenceAnimalsAntibodies, ViralCell LineCytoplasmDipeptidesDNA-Binding ProteinsEcthyma, ContagiousGene Expression Regulation, ViralGenes, ViralMolecular WeightMutationOrf virusRecombinant Fusion ProteinsRifampinalanylglycineAntibodies, ViralDipeptidesDNA-Binding ProteinsRecombinant Fusion ProteinsRifampinvaccinia virus protein VP8Viral Core ProteinsViral ProteinsViral Structural ProteinsCleavage siteORFV050Orf virusPolyclonal antiserumProteolysis

Identifiers

PMID28190135
OpenAlexW2586596572

What OpenQuestion holds

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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.