Evidence map›Paper›PMID 26317500›Full record

ArticlePLoS pathogens2015

The Activation of Phytophthora Effector Avr3b by Plant Cyclophilin is Required for the Nudix Hydrolase Activity of Avr3b.

Guanghui Kong, Yao Zhao, Maofeng Jing, Jie Huang, Jin Yang, Yeqiang Xia, Liang Kong, Wenwu Ye, Qin Xiong, Yongli Qiao and 3 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 72 citations in OpenAlex.

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  11. Molecular mechanisms ofFrontiers in microbiology · 2022
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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

13 authors at 2 institutions in 2 countries.

Guanghui KongCollege of Plant Protection, Nanjing Agricultural University, Nanjing, China.
Yao ZhaoCollege of Plant Protection, Nanjing Agricultural University, Nanjing, China.
Maofeng JingCollege of Plant Protection, Nanjing Agricultural University, Nanjing, China.
Jie HuangCollege of Plant Protection, Nanjing Agricultural University, Nanjing, China.
Jin YangCollege of Plant Protection, Nanjing Agricultural University, Nanjing, China.
Yeqiang XiaCollege of Plant Protection, Nanjing Agricultural University, Nanjing, China.
Liang KongCollege of Plant Protection, Nanjing Agricultural University, Nanjing, China.
Wenwu YeCollege of Plant Protection, Nanjing Agricultural University, Nanjing, China.
Qin XiongCollege of Plant Protection, Nanjing Agricultural University, Nanjing, China.
Yongli QiaoDepartment of Plant Pathology and Microbiology, University of California, Riverside, Riverside, California, United States of America; National Key Facility for Crop Gene Resources and Genetic Improvement, Institute of Crop Science, Chinese Academy of Agricultural Sciences, Beijing, China.
Suomeng DongCollege of Plant Protection, Nanjing Agricultural University, Nanjing, China.
Wenbo MaDepartment of Plant Pathology and Microbiology, University of California, Riverside, Riverside, California, United States of America.
Yuanchao WangCollege of Plant Protection, Nanjing Agricultural University, Nanjing, China.
Nanjing Agricultural University · CNUniversity of California, Riverside · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant pathogens secrete an arsenal of effector proteins to impair host immunity. Some effectors possess enzymatic activities that can modify their host targets. Previously, we demonstrated that a Phytophthora sojae RXLR effector Avr3b acts as a Nudix hydrolase when expressed in planta; and this enzymatic activity is required for full virulence of P. sojae strain P6497 in soybean (Glycine max). Interestingly, recombinant Avr3b produced by E. coli does not have the hydrolase activity unless it was incubated with plant protein extracts. Here, we report the activation of Avr3b by a prolyl-peptidyl isomerase (PPIase), cyclophilin, in plant cells. Avr3b directly interacts with soybean cyclophilin GmCYP1, which activates the hydrolase activity of Avr3b in a PPIase activity-dependent manner. Avr3b contains a putative Glycine-Proline (GP) motif; which is known to confer cyclophilin-binding in other protein substrates. Substitution of the Proline (P132) in the putative GP motif impaired the interaction of Avr3b with GmCYP1; as a result, the mutant Avr3bP132A can no longer be activated by GmCYP1, and is also unable to promote Phytophthora infection. Avr3b elicits hypersensitive response (HR) in soybean cultivars producing the resistance protein Rps3b, but Avr3bP132A lost its ability to trigger HR. Furthermore, silencing of GmCYP1 rendered reduced cell death triggered by Avr3b, suggesting that GmCYP1-mediated Avr3b maturation is also required for Rps3b recognition. Finally, cyclophilins of Nicotiana benthamiana can also interact with Avr3b and activate its enzymatic activity. Overall, our results demonstrate that cyclophilin is a "helper" that activates the enzymatic activity of Avr3b after it is delivered into plant cells; as such, cyclophilin is required for the avirulence and virulence functions of Avr3b.

Indexed as

Amino Acid SequenceBlotting, WesternCyclophilinsGlycine maxHost-Parasite InteractionsImmunoprecipitationMolecular Sequence DataNudix HydrolasesPhytophthoraPlant DiseasesPlant ImmunityPlant ProteinsPyrophosphatasesTwo-Hybrid System TechniquesVirulenceCyclophilinsNudix HydrolasesPlant ProteinsPyrophosphatases

Identifiers

PMID26317500
PMCPMC4552650
OpenAlexW1924856383

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.