Evidence map›Paper›PMID 29115017›Full record

ArticleMolecular plant pathology2018

Truncation of a P1 leader proteinase facilitates potyvirus replication in a non-permissive host.

Hongying Shan, Fabio Pasin, Ioannis E Tzanetakis, Carmen Simón-Mateo, Juan Antonio García, Bernardo Rodamilans

Open access · bronzeAbstract read
In one paragraph

Article in Molecular plant pathology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
7.1field-weighted citation impact, top 4% 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

22 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. The Mechanism of Resistance of EUROPEAN Plum toPlants (Basel, Switzerland) · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. P1 ofJournal of virology · 2021
    Article
  16. The P1 Protein ofFrontiers in microbiology · 2021
    Article
  17. A Newly Identified Virus in the FamilyJournal of virology · 2020
    Article
  18. Article
  19. Review
  20. Article
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

6 authors at 2 institutions in 2 countries.

Hongying ShanDepartamento de Genética Molecular de Plantas, Centro Nacional de Biotecnología (CNB-CSIC), Campus Universidad Autónoma de Madrid, Darwin 3, Madrid 28049, Spain.
Fabio PasinDepartamento de Genética Molecular de Plantas, Centro Nacional de Biotecnología (CNB-CSIC), Campus Universidad Autónoma de Madrid, Darwin 3, Madrid 28049, Spain.ORCID 0000-0002-9620-4301
Ioannis E TzanetakisDepartment of Plant Pathology, Division of Agriculture, University of Arkansas System, Fayetteville, AR 72701, USA.
Carmen Simón-MateoDepartamento de Genética Molecular de Plantas, Centro Nacional de Biotecnología (CNB-CSIC), Campus Universidad Autónoma de Madrid, Darwin 3, Madrid 28049, Spain.
Juan Antonio GarcíaDepartamento de Genética Molecular de Plantas, Centro Nacional de Biotecnología (CNB-CSIC), Campus Universidad Autónoma de Madrid, Darwin 3, Madrid 28049, Spain.ORCID 0000-0002-4861-9609
Bernardo RodamilansDepartamento de Genética Molecular de Plantas, Centro Nacional de Biotecnología (CNB-CSIC), Campus Universidad Autónoma de Madrid, Darwin 3, Madrid 28049, Spain.ORCID 0000-0002-6541-2589
Centro Nacional de Biotecnología · ESUniversity of Arkansas System · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Potyviridae family is a major group of plant viruses that includes c. 200 species, most of which have narrow host ranges. The potyvirid P1 leader proteinase self-cleaves from the remainder of the viral polyprotein and shows large sequence variability linked to host adaptation. P1 proteins can be classified as Type A or Type B on the basis, amongst other things, of their dependence or not on a host factor to develop their protease activity. In this work, we studied Type A proteases from the Potyviridae family, characterizing their host factor requirements. Our in vitro cleavage analyses of potyvirid P1 proteases showed that the N-terminal domain is relevant for host factor interaction and suggested that the C-terminal domain is also involved. In the absence of plant factors, the N-terminal end of Plum pox virus P1 antagonizes protease self-processing. We performed extended deletion mutagenesis analysis to define the N-terminal antagonistic domain of P1. In viral infections, removal of the P1 protease antagonistic domain led to a gain-of-function phenotype, strongly increasing local infection in a non-permissive host. Altogether, our results shed new insights into the adaptation and evolution of potyvirids.

Indexed as

PotyvirusViral ProteinsVirus ReplicationViral Proteinshost adaptationhost factorP1 proteasespolyprotein processingPotyviridaeRNA silencing suppression

Identifiers

PMID29115017
PMCPMC6638051
OpenAlexW2767991121

What Socratic 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 Socratic graph.