The first Kunitz peptide was discovered by Moses Kunitz from

The first Kunitz peptide was discovered by Moses Kunitz from bovine pancreas and since then Kunitz peptides have been identified as a diverse protein family, affecting different serine proteases with distinct binding affinities. There are several tick salivary Kunitz peptides described in the literature as potent protease inhibitors with unique and stringent target specificity. For instance, the tick anticoagulant peptide from Ornithodoros moubata is a potent inhibitor of factor Xa, but has no effect on factor VIIa, kallikrein, trypsin, chymotrypsin, thrombin, urokinase, plasmin, tissue plasminogen activator and elastase. Another example is the tick-derived protease inhibitor from the hard tick Rhipicephalus appendiculatus that is a potent b-tryptase inhibitor, but not for urokinase, thrombin, factor Xa, factor XIIa, elastases, kallikreins, cathepsin G, granzyme B, chymase and chymotrypsins. Hard tick feeding lasts up to a week as opposed to their distant relative, the soft ticks, whose feeding cycle is much faster. Astragalus Polysacharin distributor Because of the extended hard tick feeding cycle, a complex of host defense responses takes place at the injury site that is counteracted by the pharmacological properties of tick saliva. Tick salivary protease inhibitors play a role in regulating host proteolytic events and the transmission of tick-borne diseases, such as Lyme disease, while other tick salivary proteins facilitate the transmission of rickettsioses and tick-borne encephalitis. Because of the known pharmacological properties of tick saliva, two salivary gland transcriptome and proteome projects �C also called sialome projects �C revealed secreted salivary proteins expressed from the hard tick, Ixodes scapularis. Annotating these sialome projects amounted to hundreds of tick salivary sequences that remain uncharacterized. These projects revealed many protein sequences classified as having the conserved Kunitz domain and 60 sequences are annotated as monolaris �C sequences that have six cysteine residues forming three disulfide KS176 bridges and a single Kunitz head. These 60 monolaris sequences can be further divided into subgroups categorized by variations in their Cys motif. The remaining Kunitz sequences from I. scapularis are defined as bilaris and p