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 K_d < 10 nm and four other CC chemokines with a K_d between 10 and 100 nm and neutralizes CCL3, CCL3L1, and CCL8 with an IC₅₀ < 10 nm The CC chemokine-binding profile was distinct from that of evasin 1 (EVA1), which does not bind CCL8. We also show that P672's binding activity can be markedly modulated by the location of a StrepII-His purification tag. Combining native MS and botto

SUBMITTER: Eaton JRO 

PROVIDER: S-EPMC5912465 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature