Ticks are hematophagous arachnids that parasitize humans, livestock and both domestic and wild animals and often transmit viral or bacterial pathogens to their hosts. As survival strategies, ticks secrete numerous salivary factors that enhance host blood flow or suppress the host inflammatory response, enabling longer residence times. These include proteins called Evasins, which help ticks to evade the host innate immune response by blocking the activity of host chemokine proteins, important modulators of leukocyte recruitment in inflammation. We have used bioinformatics methods to identify more than 250 putative Evasins and we have validated representative Evasins as chemokine-binding and inhibitory proteins. Sequence alignments enabled classification of the Evasins according to distinct patterns of cysteine residues and identification of conserved features contributing to structural integrity and chemokine class-selectivity. Mutational analysis is starting to define the requirements for selective recognition of particular chemokines. Recent sequence database mining suggests that the Evasin family may be more widespread and diverse than previously recognised. The Evasins are a valuable pool of anti-inflammatory proteins that could be repurposed or engineered as therapeutic anti-inflammatory agents.