Evidence map›Paper›PMID 26596626›Full record

ArticleScientific reports2015

M233I Mutation in the β-Tubulin of Botrytis cinerea Confers Resistance to Zoxamide.

Meng Cai, Dong Lin, Lei Chen, Yang Bi, Lu Xiao, Xi-li Liu

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
8.3field-weighted citation impact, top 3% 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

12 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Stepwise accumulation of mutations in CesA3 inEvolutionary applications · 2021
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Frontiers in microbiology · 2019
    Article
  11. Article
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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

6 authors at 3 institutions in 1 country.

Meng CaiDepartment of Plant Pathology, China Agricultural University, Beijing, 100193, P. R. China.
Dong LinDepartment of Plant Pathology, China Agricultural University, Beijing, 100193, P. R. China.
Lei ChenCollege of Forestry, Beijing Forestry University, Beijing, 100083, P.R. China.
Yang BiPlant Science and Technology College, Beijing University of Agriculture, Beijing, 102206, P.R. China.
Lu XiaoDepartment of Plant Pathology, China Agricultural University, Beijing, 100193, P. R. China.
Xi-li LiuDepartment of Plant Pathology, China Agricultural University, Beijing, 100193, P. R. China.
China Agricultural University · CNBeijing Forestry University · CNBeijing University of Agriculture · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Three phenotypes were detected in 161 Botrytis cinerea field isolates, including Zox(S)Car(S) (sensitive to zoxamide and carbendazim), Zox(S)Car(R) (sensitive to zoxamide and resistant to carbendazim), and Zox(R)Car(R) (resistant to zoxamide and carbendazim), but not Zox(R)Car(S) (resistant to zoxamide and sensitive to carbendazim). The baseline sensitivity to zoxamide was determined with a mean EC50 of 0.76 μg/ml. Two stable Zox(R)Car(S) isolates were obtained with a resistance factor of 13.28 and 20.43; there was a fitness penalty in mycelial growth rate, sporulation, virulence and sclerotium production. The results suggest that the resistance risk of B. cinerea to zoxamide is low where benzimidazoles have not been used. E198V, E198K and M233I, were detected in the β-tubulin of Zox(S)Car(R), Zox(R)Car(R), Zox(R)Car(S), respectively. Molecular docking indicated that position 198 in β-tubulin were targets for both zoxamide and carbendazim. The mutations at 198 prevented formation of hydrogen bonds between β-tubulin and carbendazim (E198V/K), and changed the conformation of the binding pocket of zoxamide (E198K). M233I had no effect on the binding of carbendazim but resulted in loss of a hydrogen bond between zoxamide and F200. M233 is suggested to be a unique target site for zoxamide and be very important in the function of β tubulin.

Indexed as

AmidesBenzimidazolesBinding SitesBotrytisCarbamatesDrug Resistance, FungalFungicides, IndustrialMicrobial Sensitivity TestsMolecular Docking SimulationMutation, MissenseMyceliumPlant DiseasesProtein BindingSpores, FungalTubulinVirulenceAmidesBenzimidazolesCarbamatescarbendazimFungicides, IndustrialTubulinzoxamide

Identifiers

PMID26596626
PMCPMC4657022
OpenAlexW2174722508

What OpenQuestion holds

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LicenceCC BY
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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.