Evidence map›Paper›PMID 33970306›Full record

ArticleCellular and molecular life sciences : CMLS2021

Venom chemistry underlying the painful stings of velvet ants (Hymenoptera: Mutillidae).

Timo Jensen, Andrew A Walker, Son H Nguyen, Ai-Hua Jin, Jennifer R Deuis, Irina Vetter, Glenn F King, Justin O Schmidt, Samuel D Robinson

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.8field-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

11 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Multiple mechanisms of action of an extremely painful venom.bioRxiv : the preprint server for biology · 2024
    Article
  5. Article
  6. Article
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  11. 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

9 authors at 1 institution in 1 country.

Timo JensenInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, 4072, Australia.
Andrew A WalkerInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, 4072, Australia.
Son H NguyenInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, 4072, Australia.
Ai-Hua JinInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, 4072, Australia.
Jennifer R DeuisInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, 4072, Australia.
Irina VetterInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, 4072, Australia.
Glenn F KingInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, 4072, Australia.
Justin O SchmidtSouthwest Biological Institute, Tucson, AZ, 85745, USA.
Samuel D RobinsonInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, 4072, Australia. sam.robinson@uq.edu.au.ORCID http://orcid.org/0000-0002-3518-0377
The University of Queensland · AU

Funding

Australian Research Council DP190103787National Geographic Society EC-58468R-19National Health and Medical Research Council APP1136889
6 · The paper itself

Abstract

Velvet ants (Hymenoptera: Mutillidae) are a family of solitary parasitoid wasps that are renowned for their painful stings. We explored the chemistry underlying the stings of mutillid wasps of the genus Dasymutilla Ashmead. Detailed analyses of the venom composition of five species revealed that they are composed primarily of peptides. We found that two kinds of mutillid venom peptide appear to be primarily responsible for the painful effects of envenomation. These same peptides also have defensive utility against invertebrates, since they were able to incapacitate and kill honeybees. Both act directly on cell membranes where they directly increase ion conductivity. The defensive venom peptides of Dasymutilla bear a striking similarity, in structure and mode of action, to those of the ant Myrmecia gulosa (Fabricius), suggesting either retention of ancestral toxins, or convergence driven by similar life histories and defensive selection pressures. Finally, we propose that other highly expressed Dasymutilla venom peptides may play a role in parasitisation, possible in delay or arrest of host development. This study represents the first detailed account of the composition and function of the venoms of the Mutillidae.

Indexed as

Amino Acid SequenceAnimalsArthropod VenomsBehavior, AnimalFemaleHymenopteraInsect Bites and StingsMaleMiceMice, Inbred C57BLPainPeptide FragmentsSequence HomologyArthropod VenomsPeptide FragmentsCow killerDasymutillaPainParasitoidWasp

Identifiers

PMID33970306
PMCPMC11072429
OpenAlexW3162064574

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.