Evidence map›Paper›PMID 34618145›Full record

ArticlePlant physiology2021

Cytotoxic function of xylanase VdXyn4 in the plant vascular wilt pathogen Verticillium dahliae.

Dan Wang, Jie-Yin Chen, Jian Song, Jun-Jiao Li, Steven J Klosterman, Ran Li, Zhi-Qiang Kong, Krishna V Subbarao, Xiao-Feng Dai, Dan-Dan Zhang

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
9.3field-weighted citation impact, top 2% 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

28 citing papers in PubMed, 55 citations in OpenAlex.

  1. International journal of molecular sciences · 2026
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  16. International journal of molecular sciences · 2023
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  18. Microbiology spectrum · 2023
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  19. Microbiology spectrum · 2023
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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

10 authors at 3 institutions in 2 countries.

Dan WangTeam of Crop Verticillium wilt, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.ORCID 0000-0003-2270-0254
Jie-Yin ChenTeam of Crop Verticillium wilt, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.ORCID 0000-0002-8040-099X
Jian SongTeam of Crop Verticillium wilt, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Jun-Jiao LiTeam of Crop Verticillium wilt, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Steven J KlostermanDepartment of Agriculture, Agricultural Research Service, Crop Improvement and Protection Research Unit, Salinas, California, USA.ORCID 0000-0002-0571-5051
Ran LiTeam of Crop Verticillium wilt, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Zhi-Qiang KongTeam of Crop Verticillium wilt, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Krishna V SubbaraoDepartment of Plant Pathology, University of California, Davis, c/o U.S. Agricultural Research Station, Salinas, California, USA.ORCID 0000-0002-2075-1835
Xiao-Feng DaiTeam of Crop Verticillium wilt, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Dan-Dan ZhangTeam of Crop Verticillium wilt, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.ORCID 0000-0003-2187-3487
Institute of Plant Protection · CNAgricultural Research Service · USUniversity of California, Davis · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phytopathogen xylanases play critical roles in pathogenesis, likely due to their ability to degrade plant structural barriers and manipulate host immunity. As an invader of plant xylem vessels, the fungus Verticillium dahliae is thought to deploy complex cell wall degrading enzymes. Comparative genomics analyses revealed that the V. dahliae genome encodes a family of six xylanases, each possessing a glycosyl hydrolase 11 domain, but the functions of these enzymes are undetermined. Characterizing gene deletion mutants revealed that only V. dahliae xylanase 4 (VdXyn4) degraded the plant cell wall and contributed to the virulence of V. dahliae. VdXyn4 displayed cytotoxic activity and induced a necrosis phenotype during the late stages of infection, leading to vein and petiole collapse that depended on the enzyme simultaneously localizing to nuclei and chloroplasts. The internalization of VdXyn4 was in conjunction with that of the plasma membrane complexLeucine-rich repeat (LRR)-receptor-like kinase suppressor of BIR1-1 (SOBIR1)/LRR-RLK BRI1-associated kinase-1 (BAK1), but we could not rule out the possibility that VdXyn4 may also act as an apoplastic effector. Immune signaling (in the SA-JA pathways) induced by VdXyn4 relative to that induced by known immunity effectors was substantially delayed. While cytotoxic activity could be partially suppressed by known effectors, they failed to impede necrosis in Nicotiana benthamiana. Thus, unlike typical effectors, cytotoxicity of VdXyn4 plays a crucial intracellular role at the late stages of V. dahliae infection and colonization, especially following pathogen entry into the xylem; this cytotoxic activity is likely conserved in the corresponding enzyme families in plant vascular pathogens.

Indexed as

AscomycotaEndo-1,4-beta XylanasesFungal ProteinsNicotianaPlant DiseasesVerticilliumEndo-1,4-beta XylanasesFungal Proteins

Identifiers

PMID34618145
PMCPMC8418393
OpenAlexW3167674030

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.