Evidence map›Paper›PMID 26712000›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

A ribosome-inactivating protein in a Drosophila defensive symbiont.

Phineas T Hamilton, Fangni Peng, Martin J Boulanger, Steve J Perlman

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
11.0field-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

58 citing papers in PubMed, 120 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. A human-associatediScience · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Infection and immunity · 2025
    Review
  16. Review
  17. Article
  18. Potential effect ofFrontiers in microbiology · 2025
    Article
  19. Article
  20. The endosymbiontmBio · 2024
    Article
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

4 authors at 1 institution in 1 country.

Phineas T HamiltonDepartment of Biology, University of Victoria, Victoria, BC, Canada V8W 2Y2; phin.hamilton@gmail.com stevep@uvic.ca.
Fangni PengDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada V8P 5C2;
Martin J BoulangerDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada V8P 5C2;
Steve J PerlmanDepartment of Biology, University of Victoria, Victoria, BC, Canada V8W 2Y2; Integrated Microbial Biodiversity Program, Canadian Institute for Advanced Research, Toronto, ON, Canada M5G 1Z8 phin.hamilton@gmail.com stevep@uvic.ca.
University of Victoria · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vertically transmitted symbionts that protect their hosts against parasites and pathogens are well known from insects, yet the underlying mechanisms of symbiont-mediated defense are largely unclear. A striking example of an ecologically important defensive symbiosis involves the woodland fly Drosophila neotestacea, which is protected by the bacterial endosymbiont Spiroplasma when parasitized by the nematode Howardula aoronymphium. The benefit of this defense strategy has led to the rapid spread of Spiroplasma throughout the range of D. neotestacea, although the molecular basis for this protection has been unresolved. Here, we show that Spiroplasma encodes a ribosome-inactivating protein (RIP) related to Shiga-like toxins from enterohemorrhagic Escherichia coli and that Howardula ribosomal RNA (rRNA) is depurinated during Spiroplasma-mediated protection of D. neotestacea. First, we show that recombinant Spiroplasma RIP catalyzes depurination of 28S rRNAs in a cell-free assay, as well as Howardula rRNA in vitro at the canonical RIP target site within the α-sarcin/ricin loop (SRL) of 28S rRNA. We then show that Howardula parasites in Spiroplasma-infected flies show a strong signal of rRNA depurination consistent with RIP-dependent modification and large decreases in the proportion of 28S rRNA intact at the α-sarcin/ricin loop. Notably, host 28S rRNA is largely unaffected, suggesting targeted specificity. Collectively, our study identifies a novel RIP in an insect defensive symbiont and suggests an underlying RIP-dependent mechanism in Spiroplasma-mediated defense.

Indexed as

SymbiosisAnimalsDrosophilaEndoribonucleasesFungal ProteinsPolymerase Chain ReactionRabbitsRecombinant ProteinsRibosome Inactivating ProteinsRibosomesRicinRNA, Ribosomal, 28SSequence Analysis, RNASpiroplasmaalpha-sarcinEndoribonucleasesFungal ProteinsRecombinant ProteinsRibosome Inactivating ProteinsRicinRNA, Ribosomal, 28Smale-killingnematodeShiga toxinSpiroplasmasymbiosis

Identifiers

PMID26712000
PMCPMC4720295
OpenAlexW2212958389

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.