Evidence map›Paper›PMID 22829770›Full record

ArticlePLoS pathogens2012

Mgat1-dependent N-glycosylation of membrane components primes Drosophila melanogaster blood cells for the cellular encapsulation response.

Nathan T Mortimer, Balint Z Kacsoh, Erin S Keebaugh, Todd A Schlenke

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

32 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Complex anionic and zwitterionic N-glycans in Drosophila melanogaster.Biochimica et biophysica acta. General subjects · 2026
    Article
  4. Article
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  8. ThebioRxiv : the preprint server for biology · 2025
    Article
  9. Venom vesicles from the parasitoidbioRxiv : the preprint server for biology · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Extracellular matrix protein N-glycosylation mediates immune self-tolerance inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. The S1A protease family membersmicroPublication biology · 2021
    Article
  17. Article
  18. Review
  19. Article
  20. 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 2 institutions in 1 country.

Nathan T MortimerDepartment of Biology, Emory University, Atlanta, Georgia, United States of America. nmortim@emory.edu
Balint Z Kacsoh
Erin S Keebaugh
Todd A Schlenke
Emory University · USStanford University · US

Funding

A Model System For Host-Pathogen Interactions: Drosophila And Its Parasitic WaspsR01AI081879 · NIAID · UNIVERSITY OF ARIZONA · PI SCHLENKE, TODD ALEXANDER · 2009 to 2017
$2.8M
NIAID NIH HHS AI081879NIAID NIH HHS R01 AI081879
6 · The paper itself

Abstract

In nature, larvae of the fruitfly Drosophila melanogaster are commonly infected by parasitoid wasps, and so have evolved a robust immune response to counter wasp infection. In this response, fly immune cells form a multilayered capsule surrounding the wasp egg, leading to death of the parasite. Many of the molecular mechanisms underlying this encapsulation response are conserved with human immune responses. Our findings suggest that protein N-glycosylation, a common protein post-translational modification of human immune proteins, may be one such conserved mechanism. We found that membrane proteins on Drosophila immune cells are N-glycosylated in a temporally specific manner following wasp infection. Furthermore we have identified mutations in eight genes encoding enzymes of the N-glycosylation pathway that decrease fly resistance to wasp infection. More specifically, loss of protein N-glycosylation in immune cells following wasp infection led to the formation of defective capsules, which disintegrated over time and were thereby unsuccessful at preventing wasp development. Interestingly, we also found that one species of Drosophila parasitoid wasp, Leptopilina victoriae, targets protein N-glycosylation as part of its virulence mechanism, and that overexpression of an N-glycosylation enzyme could confer resistance against this wasp species to otherwise susceptible flies. Taken together, these findings demonstrate that protein N-glycosylation is a key player in Drosophila cellular encapsulation and suggest that this response may provide a novel model to study conserved roles of protein glycosylation in immunity.

Indexed as

AnimalsCell MembraneDrosophila melanogasterDrosophila ProteinsErythrocytesFemaleGlycosylationHost-Parasite InteractionsLarvaMembrane ProteinsN-AcetylglucosaminyltransferasesOvumWaspsDrosophila ProteinsMembrane ProteinsN-Acetylglucosaminyltransferases

Identifiers

PMID22829770
PMCPMC3400557
OpenAlexW1971371165

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.