Evidence map›Paper›PMID 16014938›Full record

ArticleJournal of virology2005

A virus essential for insect host-parasite interactions encodes cystatins.

E Espagne, V Douris, G Lalmanach, B Provost, L Cattolico, J Lesobre, S Kurata, K Iatrou, J-M Drezen, E Huguet

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Microbial inhibitors of cysteine proteases.Medical microbiology and immunology · 2016
    Review
  5. Article
  6. Article
  7. Article
  8. When parasitic wasps hijacked viruses: genomic and functional evolution of polydnaviruses.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013
    Review
  9. Article
  10. Article
  11. Paleozoic origin of insect large dsDNA viruses.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  12. Article
  13. Article
  14. Parasitism of an insect Manduca sexta L. alters feeding behaviour and nutrient utilization to influence developmental success of a parasitoid.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2008
    Article
  15. Blurring borders: innate immunity with adaptive features.Clinical & developmental immunology · 2007
    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

10 authors at 5 institutions in 3 countries.

E EspagneInstitut de Recherche sur la Biologie de l'Insecte, UMR CNRS 6035, Faculté des Sciences et Techniques, Parc de Grandmont, Tours.
V Douris
G Lalmanach
B Provost
L Cattolico
J Lesobre
S Kurata
K Iatrou
J-M Drezen
E Huguet
Centre National de la Recherche Scientifique · FRNational Centre of Scientific Research "Demokritos" · GRGenoscope · FRTohoku University · JPUniversité de Tours · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cotesia congregata is a parasitoid wasp that injects its eggs in the host caterpillar Manduca sexta. In this host-parasite interaction, successful parasitism is ensured by a third partner: a bracovirus. The relationship between parasitic wasps and bracoviruses constitutes one of the few known mutualisms between viruses and eukaryotes. The C. congregata bracovirus (CcBV) is injected at the same time as the wasp eggs in the host hemolymph. Expression of viral genes alters the caterpillar's immune defense responses and developmental program, resulting in the creation of a favorable environment for the survival and emergence of adult parasitoid wasps. Here, we describe the characterization of a CcBV multigene family which is highly expressed during parasitism and which encodes three proteins with homology to members of the cystatin superfamily. Cystatins are tightly binding, reversible inhibitors of cysteine proteases. Other cysteine protease inhibitors have been described for lepidopteran viruses; however, this is the first description of the presence of cystatins in a viral genome. The expression and purification of a recombinant form of one of the CcBV cystatins, cystatin 1, revealed that this viral cystatin is functional having potent inhibitory activity towards the cysteine proteases papain, human cathepsins L and B and Sarcophaga cathepsin B in assays in vitro. CcBV cystatins are, therefore, likely to play a role in host caterpillar physiological deregulation by inhibiting host target proteases in the course of the host-parasite interaction.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCathepsinsCystatinsDipteraGenes, ViralHost-Parasite InteractionsHumansManducaMolecular Sequence DataMultigene FamilyOvumPapainPolydnaviridaeSequence AlignmentCathepsinsCystatinsPapain

Identifiers

PMID16014938
PMCPMC1181612
OpenAlexW2126997026

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.