Evidence map›Paper›PMID 16258019›Full record

ArticlePlant physiology2005

Arabidopsis vegetative storage protein is an anti-insect acid phosphatase.

Yilin Liu, Ji-Eun Ahn, Sumana Datta, Ron A Salzman, Jaewoong Moon, Beatrice Huyghues-Despointes, Barry Pittendrigh, Larry L Murdock, Hisashi Koiwa, Keyan Zhu-Salzman

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
10.7field-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

72 citing papers in PubMed, 194 citations in OpenAlex.

  1. Review
  2. Article
  3. Expression analysis of phosphatase III-B subfamily in common bean reveals two storage proteins highly expressed during seed formation and germination.Physiology and molecular biology of plants : an international journal of functional plant biology · 2026
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  4. A natural variant of anProceedings of the National Academy of Sciences of the United States of America · 2025
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  9. Proteomic Analysis of Proteins Related to Defense Responses inInternational journal of molecular sciences · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Fine mapping of a thrips resistance QTL in Capsicum and the role of diterpene glycosides in the underlying mechanism.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2021
    Article
  17. Article
  18. Article
  19. Review
  20. Proteomic Changes in the Sound Vibration-TreatedThe plant pathology journal · 2019
    Article

12 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Yilin LiuDepartment of Entomology, Texas A&M University, College Station, TX 77843, USA.
Ji-Eun Ahn
Sumana Datta
Ron A Salzman
Jaewoong Moon
Beatrice Huyghues-Despointes
Barry Pittendrigh
Larry L Murdock
Hisashi Koiwa
Keyan Zhu-Salzman
Purdue University West Lafayette · USTexas A&M University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Indirect evidence previously suggested that Arabidopsis (Arabidopsis thaliana) vegetative storage protein (VSP) could play a role in defense against herbivorous insects. To test this hypothesis, other AtVSP-like sequences in Arabidopsis were identified through a Basic Local Alignment Search Tool search, and their transcriptional profiles were investigated. In response to methyl jasmonate application or phosphate starvation, AtVSP and AtVSP-like genes exhibited differential expression patterns, suggesting distinct roles played by each member. Arabidopsis VSP2 (AtVSP2), a gene induced by wounding, methyl jasmonate, insect feeding, and phosphate deprivation, was selected for bacterial expression and functional characterization. The recombinant protein exhibited a divalent cation-dependent phosphatase activity in the acid pH range. When incorporated into the diets of three coleopteran and dipteran insects that have acidic gut lumen, recombinant AtVSP2 significantly delayed development of the insects and increased their mortality. To further determine the biochemical basis of the anti-insect activity of the protein, the nucleophilic aspartic acid-119 residue at the conserved DXDXT signature motif was substituted by glutamic acid via site-directed mutagenesis. This single-amino acid alteration did not compromise the protein's secondary or tertiary structure, but resulted in complete loss of its acid phosphatase activity as well as its anti-insect activity. Collectively, we conclude that AtVSP2 is an anti-insect protein and that its defense function is correlated with its acid phosphatase activity.

Indexed as

AcetatesAcid PhosphataseAmino Acid SequenceAnimalsArabidopsisArabidopsis ProteinsCyclopentanesDrosophilaGene Expression Regulation, PlantInsectaInsect ControlMolecular Sequence DataMutationOxylipinsPhosphatesProtein ConformationAcetatesAcid PhosphataseArabidopsis ProteinsCyclopentanesmethyl jasmonateOxylipinsPhosphatesRNA, MessengerVSP2 protein, Arabidopsis

Identifiers

PMID16258019
PMCPMC1283788
OpenAlexW2114182170

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.