Evidence map›Paper›PMID 27928637›Full record

ReviewPlanta2017

Molecular functions of Xanthomonas type III effector AvrBsT and its plant interactors in cell death and defense signaling.

Sang Wook Han, Byung Kook Hwang

Abstract readReview
PubMed Publisher
In one paragraph

Review in Planta, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. Pathogens (Basel, Switzerland) · 2026
    Review
  2. A protein elicitor PeVn1 fromFrontiers in plant science · 2024
    Article
  3. Cytoplasmic CaFrontiers in plant science · 2024
    Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. AFrontiers in plant science · 2021
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
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

2 authors at 2 institutions in 1 country.

Sang Wook HanDepartment of Integrative Plant Science, Chung-Ang University, Anseong, 17546, Republic of Korea.
Byung Kook HwangLaboratory of Molecular Plant Pathology, College of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-ku, Seoul, 02841, Republic of Korea. bkhwang@korea.ac.kr.ORCID http://orcid.org/0000-0003-1782-8990
Chung-Ang University · KRKorea University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MAIN

conclusionXanthomonas effector AvrBsT interacts with plant defense proteins and triggers cell death and defense response. This review highlights our current understanding of the molecular functions of AvrBsT and its host interactor proteins. The AvrBsT protein is a member of a growing family of effector proteins in both plant and animal pathogens. Xanthomonas type III effector AvrBsT, a member of the YopJ/AvrRxv family, suppresses plant defense responses in susceptible hosts, but triggers cell death signaling leading to hypersensitive response (HR) and defense responses in resistant plants. AvrBsT interacts with host defense-related proteins to trigger the HR cell death and defense responses in plants. Here, we review and discuss recent progress in understanding the molecular functions of AvrBsT and its host interactor proteins in pepper (Capsicum annuum). Pepper arginine decarboxylase1 (CaADC1), pepper aldehyde dehydrogenase1 (CaALDH1), pepper heat shock protein 70a (CaHSP70a), pepper suppressor of the G2 allele of skp1 (CaSGT1), pepper SNF1-related kinase1 (SnRK1), and Arabidopsis acetylated interacting protein1 (ACIP1) have been identified as AvrBsT interactors in pepper and Arabidopsis. Gene expression profiling, virus-induced gene silencing, and transient transgenic overexpression approaches have advanced the functional characterization of AvrBsT-interacting proteins in plants. AvrBsT is localized in the cytoplasm and forms protein-protein complexes with host interactors. All identified AvrBsT interactors regulate HR cell death and defense responses in plants. Notably, CaSGT1 physically binds to both AvrBsT and pepper receptor-like cytoplasmic kinase1 (CaPIK1) in the cytoplasm. During infection with Xanthomonas campestris pv. vesicatoria strain Ds1 (avrBsT), AvrBsT is phosphorylated by CaPIK1 and forms the active AvrBsT-CaSGT1-CaPIK1 complex, which ultimately triggers HR cell death and defense responses. Collectively, the AvrBsT interactor proteins are involved in plant cell death and immunity signaling.

Indexed as

Host-Pathogen InteractionsAldehyde DehydrogenaseBacterial ProteinsCapsicumCarboxy-LyasesCell DeathHSP70 Heat-Shock ProteinsPlant CellsPlant ProteinsSignal TransductionXanthomonas campestrisAldehyde Dehydrogenasearginine decarboxylaseBacterial ProteinsCarboxy-LyasesHSP70 Heat-Shock ProteinsPlant ProteinsAvrBsT interactorsCell deathDefense-related genesHypersensitive responsePlant defenseXanthomonas type III effector AvrBsT

Identifiers

PMID27928637
OpenAlexW2559965163

What OpenQuestion 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 OpenQuestion graph.