Evidence map›Paper›PMID 28655871›Full record

ArticleScientific reports2017

Yeast surface display identifies a family of evasins from ticks with novel polyvalent CC chemokine-binding activities.

Kamayani Singh, Graham Davies, Yara Alenazi, James R O Eaton, Akane Kawamura, Shoumo Bhattacharya

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

23 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Structural basis of chemokine recognition by the class A3 tick evasin EVA-ACA1001.Protein science : a publication of the Protein Society · 2024
    Article
  5. Article
  6. Structure-guided engineering of tick evasins for targeting chemokines in inflammatory diseases.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Immunomodulatory Proteins in Tick Saliva From a Structural Perspective.Frontiers in cellular and infection microbiology · 2021
    Review
  11. Article
  12. Article
  13. Semisynthesis of an evasin from tick saliva reveals a critical role of tyrosine sulfation for chemokine binding and inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
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  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Kamayani SinghRDM Division of Cardiovascular Medicine and Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, United Kingdom.
Graham DaviesRDM Division of Cardiovascular Medicine and Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, United Kingdom.
Yara AlenaziRDM Division of Cardiovascular Medicine and Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, United Kingdom.
James R O EatonRDM Division of Cardiovascular Medicine and Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, United Kingdom.
Akane KawamuraRDM Division of Cardiovascular Medicine and Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, United Kingdom.ORCID 0000-0003-1169-5082
Shoumo BhattacharyaRDM Division of Cardiovascular Medicine and Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, United Kingdom. sbhattac@well.ox.ac.uk.
Centre for Human Genetics · GB

Funding

British Heart Foundation CH/09/003British Heart Foundation PG/16/100/32632British Heart Foundation RG/10/17/28553Wellcome Trust
6 · The paper itself

Abstract

Chemokines function via G-protein coupled receptors in a robust network to recruit immune cells to sites of inflammation. Due to the complexity of this network, targeting single chemokines or receptors has not been successful in inflammatory disease. Dog tick saliva contains polyvalent CC-chemokine binding peptides termed evasins 1 and 4, that efficiently disrupt the chemokine network in models of inflammatory disease. Here we develop yeast surface display as a tool for functionally identifying evasins, and use it to identify 10 novel polyvalent CC-chemokine binding evasin-like peptides from salivary transcriptomes of eight tick species in Rhipicephalus and Amblyomma genera. These evasins have unique binding profiles compared to evasins 1 and 4, targeting CCL2 and CCL13 in addition to other CC-chemokines. Evasin binding leads to neutralisation of chemokine function including that of complex chemokine mixtures, suggesting therapeutic efficacy in inflammatory disease. We propose that yeast surface display is a powerful approach to mine potential therapeutics from inter-species protein interactions that have arisen during evolution of parasitism in ticks.

Indexed as

Amino Acid SequenceCell Surface Display TechniquesChemokines, CCFungal ProteinsPeptide LibraryProtein BindingReceptors, ChemokineSequence Analysis, ProteinYeastsChemokines, CCFungal ProteinsPeptide LibraryReceptors, Chemokine

Identifiers

PMID28655871
PMCPMC5487423
OpenAlexW2652010170

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.