Evidence map›Paper›PMID 20940421›Full record

ArticleBlood2011

A tick salivary protein targets cathepsin G and chymase and inhibits host inflammation and platelet aggregation.

Jindrich Chmelar, Carlo J Oliveira, Pavlina Rezacova, Ivo M B Francischetti, Zuzana Kovarova, Gunnar Pejler, Peter Kopacek, José M C Ribeiro, Michael Mares, Jan Kopecky and 1 more

Abstract read
In one paragraph

Article in Blood, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

97 citing papers in PubMed, 149 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Serpins in the Spotlight: Novel Bioinformatic Insights IntoBiochemistry research international · 2025
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Conformational transition of the Ixodes ricinus salivary serpin Iripin-4.Acta crystallographica. Section D, Structural biology · 2023
    Article
  11. Review
  12. Frontiers in cellular and infection microbiology · 2023
    Article
  13. Guianensin, aFrontiers in immunology · 2023
    Article
  14. Article
  15. Mast Cell and Basophil Granule Proteases -Frontiers in immunology · 2022
    Review
  16. Review
  17. Serpins in Tick Physiology and Tick-Host Interaction.Frontiers in cellular and infection microbiology · 2022
    Review
  18. Article
  19. Article
  20. Article

37 more citing papers are in PubMed but not listed here.

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

11 authors at 7 institutions in 4 countries.

Jindrich ChmelarInstitute of Parasitology, Biology Centre of the Academy of Sciences of Czech Republic, Ceske Budejovice, Czech Republic.
Carlo J Oliveira
Pavlina Rezacova
Ivo M B Francischetti
Zuzana Kovarova
Gunnar Pejler
Peter Kopacek
José M C Ribeiro
Michael Mares
Jan Kopecky
Michail Kotsyfakis
Czech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZInstitute of Parasitology · CZNational Institute of Allergy and Infectious Diseases · USCzech Academy of Sciences, Biology Centre · CZSwedish University of Agricultural Sciences · SEUniversidade de São Paulo · BRUniversity of South Bohemia in České Budějovice · CZ

Funding

Vector-Borne Diseases: Biology Of Vector Host RelationshipZIAAI000810 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI RIBEIRO, JOSE · 2009 to 2025
$20.8M
Vector-Borne Diseases: Biology Of Vector Host RelationshipZ01AI000810 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI RIBEIRO, JOSE M · 1997 to 2008
$3.5M
Intramural NIH HHS Z01 AI000810
6 · The paper itself

Abstract

Platelet aggregation and acute inflammation are key processes in vertebrate defense to a skin injury. Recent studies uncovered the mediation of 2 serine proteases, cathepsin G and chymase, in both mechanisms. Working with a mouse model of acute inflammation, we revealed that an exogenous salivary protein of Ixodes ricinus, the vector of Lyme disease pathogens in Europe, extensively inhibits edema formation and influx of neutrophils in the inflamed tissue. We named this tick salivary gland secreted effector as I ricinus serpin-2 (IRS-2), and we show that it primarily inhibits cathepsin G and chymase, while in higher molar excess, it affects thrombin activity as well. The inhibitory specificity was explained using the crystal structure, determined at a resolution of 1.8 Å. Moreover, we disclosed the ability of IRS-2 to inhibit cathepsin G-induced and thrombin-induced platelet aggregation. For the first time, an ectoparasite protein is shown to exhibit such pharmacological effects and target specificity. The stringent specificity and biological activities of IRS-2 combined with the knowledge of its structure can be the basis for the development of future pharmaceutical applications.

Indexed as

Amino Acid SequenceAnimalsCathepsin GChymasesCrystallizationDisease Models, AnimalFemaleGene ExpressionHumansInflammationInsect ProteinsIxodesMiceMice, Inbred C57BLMolecular Sequence DataPlatelet AggregationCathepsin GChymasesInsect ProteinsSalivary Proteins and Peptidesserpin-2Serpins

Identifiers

PMID20940421
PMCPMC3031492
OpenAlexW2043568569

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.