Swapping N-terminal regions among tick evasins reveals cooperative interactions influencing chemokine binding and selectivity.

ABSTRACT: Class A tick evasins are natural chemokine-binding proteins that block the signaling of multiple chemokines from the CC subfamily through their cognate receptors, thus suppressing leukocyte recruitment and inflammation. Development of tick evasins as chemokine-targeted anti-inflammatory therapeutics requires an understanding of the factors controlling their chemokine recognition and selectivity. To investigate the role of the evasin N-terminal region for chemokine recognition, we prepared chimeric evasins by interchanging the N-terminal regions of four class A evasins, including a newly identified evasin, EVA-RPU02. We show through chemokine binding analysis of the parental and chimeric evasins that the N-terminal region is critical for chemokine binding affinity and selectivity. Notably,

SUBMITTER: Aryal P 

PROVIDER: S-EPMC9478924 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature