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The N-terminal domain of a tick evasin is critical for chemokine binding and neutralization and confers specific binding activity to other evasins

Abstract:

Tick chemokine-binding proteins (evasins) are an emerging class of biologicals that target multiple chemokines and show anti-inflammatory activities in preclinical disease models. Using yeast surface display, we identified a CCL8-binding evasin, P672, from the tick Rhipicephalus pulchellus. We found that P672 binds CCL8 and eight other CC-class chemokines with a Kd < 10 nM and four other CC chemokines with a Kd between 10 and 100 nM and neutralizes CCL3, CCL3L1, and CCL8 with an IC50 < ...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1074/jbc.ra117.000487

Authors


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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
RDM; RDM Cardiovascular Medicine
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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
RDM; RDM Cardiovascular Medicine
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
RDM; RDM Cardiovascular Medicine
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Physical & Theoretical Chem
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Saudi Arabian Cultural Bureau More from this funder
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Grant:
Dorothy Hodgkin Fellowship
Publisher:
American Society for Biochemistry and Molecular Biology Publisher's website
Journal:
Journal of Biological Chemistry Journal website
Volume:
293
Issue:
16
Pages:
6134-6146
Publication date:
2018-02-27
Acceptance date:
2018-02-27
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Pubs id:
pubs:827104
URN:
uri:9bec8460-5b7e-42a3-810e-4b125e613bad
UUID:
uuid:9bec8460-5b7e-42a3-810e-4b125e613bad
Local pid:
pubs:827104

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