Evidence map›Paper›PMID 30548752›Full record

ArticleMolecular plant pathology2019

Role of lysine residues of the Magnaporthe oryzae effector AvrPiz-t in effector- and PAMP-triggered immunity.

Pengfei Bai, Chan-Ho Park, Gautam Shirsekar, Pattavipha Songkumarn, Maria Bellizzi, Guo-Liang Wang

Open access · hybridAbstract read
In one paragraph

Article in Molecular plant pathology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
15.2field-weighted citation impact, top 1% 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

15 citing papers in PubMed, 37 citations in OpenAlex.

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  13. The Flower-Infecting FungusFrontiers in plant science · 2021
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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 2 institutions in 2 countries.

Pengfei BaiDepartment of Plant Pathology, Ohio State University, Columbus, OH, 43210.
Chan-Ho ParkDepartment of Plant Pathology, Ohio State University, Columbus, OH, 43210.
Gautam ShirsekarDepartment of Plant Pathology, Ohio State University, Columbus, OH, 43210.
Pattavipha SongkumarnDepartment of Plant Pathology, Ohio State University, Columbus, OH, 43210.
Maria BellizziDepartment of Plant Pathology, Ohio State University, Columbus, OH, 43210.
Guo-Liang WangDepartment of Plant Pathology, Ohio State University, Columbus, OH, 43210.ORCID 0000-0001-8877-3064
The Ohio State University · USInstitute of Plant Protection · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Magnaporthe oryzae is an important fungal pathogen of both rice and wheat. However, how M. oryzae effectors modulate plant immunity is not fully understood. Previous studies have shown that the M. oryzae effector AvrPiz-t targets the host ubiquitin-proteasome system to manipulate plant defence. In return, two rice ubiquitin E3 ligases, APIP6 and APIP10, ubiquitinate AvrPiz-t for degradation. To determine how lysine residues contribute to the stability and function of AvrPiz-t, we generated double (K1,2R-AvrPiz-t), triple (K1,2,3R-AvrPiz-t) and lysine-free (LF-AvrPiz-t) mutants by mutating lysines into arginines in AvrPiz-t. LF-AvrPiz-t showed the highest protein accumulation when transiently expressed in rice protoplasts. When co-expressed with APIP10 in Nicotiana benthamiana, LF-AvrPiz-t was more stable than AvrPiz-t and was less able to degrade APIP10. The avirulence of LF-AvrPiz-t on Piz-t:HA plants was less than that of AvrPiz-t, which led to resistance reduction and lower accumulation of the Piz-t:HA protein after inoculation with the LF-AvrPiz-t-carrying isolate. Chitin- and flg22-induced production of reactive oxygen species (ROS) was higher in LF-AvrPiz-t than in AvrPiz-t transgenic plants. In addition, LF-AvrPiz-t transgenic plants were less susceptible than AvrPiz-t transgenic plants to a virulent isolate. Furthermore, both AvrPiz-t and LF-AvrPiz-t interacted with OsRac1, but the suppression of OsRac1-mediated ROS generation by LF-AvrPiz-t was significantly lower than that by AvrPiz-t. Together, these results suggest that the lysine residues of AvrPiz-t are required for its avirulence and virulence functions in rice.

Indexed as

Disease ResistanceFungal ProteinsLysineMagnaportheOryzaPlant DiseasesPlant ImmunityPlant ProteinsFungal ProteinsLysinePlant Proteinseffectorlysine residueprotein stabilityreactive oxygen speciesrice immunity

Identifiers

PMID30548752
PMCPMC6637882
OpenAlexW2904356167

What OpenQuestion holds

Textmetadata
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.