Shankar Raj Devkota

Abstract The primate-specific chemokine CCL18 is a potent chemoattractant for T cells and is expressed at elevated levels in several inflammatory diseases. However, the cognate receptor for CCL18 remains unconfirmed. Here, we describe attempts to validate a previous report that the chemokine receptor CCR8 is the human CCL18 receptor (Islam et al. J Exp Med. 2013, 210:1889-98).

1 INTRODUCTION Inflammation is characterized by the accumulation of leukocytes in damaged or injured tissues. Chemokines mediate leukocyte recruitment by interacting with chemokine receptors located on leukocyte cell membranes (Griffith et al., 2014; Stone et al., 2017). Chemokines and their receptors play essential roles in development and homeostasis, while their dysregulation results in the progression of various autoimmune and inflammatory diseases (Chen et al., 2018).

Abstract Chemokines are key regulators of leukocyte trafficking and attractive targets for anti-inflammatory therapy. Evasins are chemokine-binding proteins from tick saliva, whose application as anti-inflammatory therapeutics will require manipulation of their chemokine target selectivity. Here we describe subclass A3 evasins, which are unique to the tick genus Amblyomma and distinguished from “classical” class A1 evasins by an additional disulfide bond near the chemokine recognition interface.