Evidence map›Paper›PMID 23008466›Full record

ArticlePlant physiology2012

An amino acid substitution inhibits specialist herbivore production of an antagonist effector and recovers insect-induced plant defenses.

Eric A Schmelz, Alisa Huffaker, Mark J Carroll, Hans T Alborn, Jared G Ali, Peter E A Teal

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

22 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
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  11. Review
  12. A plant surface receptor for sensing insect herbivory.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. A receptor-like protein mediates plant immune responses to herbivore-associated molecular patterns.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Article
  15. Review
  16. Plant Perception and Short-Term Responses to Phytophagous Insects and Mites.International journal of molecular sciences · 2018
    Review
  17. Article
  18. Article
  19. Article
  20. 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

6 authors at 4 institutions in 1 country.

Eric A SchmelzChemistry Research Unit, Agricultural Research Service, Center of Medical, Agricultural, and Veterinary Entomology, United States Department of Agriculture, Gainesville, Florida 32608, USA. eric.schmelz@ars.usda.gov
Alisa Huffaker
Mark J Carroll
Hans T Alborn
Jared G Ali
Peter E A Teal
Agricultural Research Service · USCenter for Medical, Agricultural and Veterinary Entomology · USCornell University · USUnited States Department of Agriculture · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants respond to insect herbivory through the production of biochemicals that function as either direct defenses or indirect defenses via the attraction of natural enemies. While attack by closely related insect pests can result in distinctive levels of induced plant defenses, precise biochemical mechanisms responsible for differing responses remain largely unknown. Cowpea (Vigna unguiculata) responds to Fall armyworm (Spodoptera frugiperda) herbivory through the detection of fragments of chloroplastic ATP synthase γ-subunit proteins, termed inceptin-related peptides, present in larval oral secretions (OS). In contrast to generalists like Fall armyworm, OS of the legume-specializing velvetbean caterpillar (VBC; Anticarsia gemmatalis) do not elicit ethylene production and demonstrate significantly lower induced volatile emission in direct herbivory comparisons. Unlike all other Lepidoptera OS examined, which preferentially contain inceptin (Vu-In; +ICDINGVCVDA-), VBC OS contain predominantly a C-terminal truncated peptide, Vu-In(-A) (+ICDINGVCVD-). Vu-In(-A) is both inactive and functions as a potent naturally occurring antagonist of Vu-In-induced responses. To block antagonist production, amino acid substitutions at the C terminus were screened for differences in VBC gut proteolysis. A valine-substituted peptide (Vu-In(ΔV); +ICDINGVCVDV-) retaining full elicitor activity was found to accumulate in VBC OS. Compared with the native polypeptide, VBC that previously ingested 500 pmol of the valine-modified chloroplastic ATP synthase γ-subunit precursor elicited significantly stronger plant responses in herbivory assays. We demonstrate that a specialist herbivore minimizes the activation of defenses by converting an elicitor into an antagonist effector and identify an amino acid substitution that recovers these induced plant defenses to a level observed with generalist herbivores.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsChloroplast Proton-Translocating ATPasesFabaceaeHerbivoryLarvaModels, BiologicalMolecular Sequence DataMothsPeptidesSpodopteraChloroplast Proton-Translocating ATPasesPeptides

Identifiers

PMID23008466
PMCPMC3490598
OpenAlexW2051024770

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.