ABSTRACT
Snake venoms contain two types of C-type lectins based on the structural features and functional properties: snake C-type lectin-like proteins (CLPs) and sugar binding snake lectins. There is some degree of sequence homology between the two proteins. Most snake lectins are 26-28 kDa homodimers that agglutinate erythrocytes only via binding to carbohydrates. On the other hand, CLPs are composed of homologous heterodimers existing as monomeric or oligomeric forms (αβ)x and contribute to the disruption of hemostasis in envenomed prey by targeting a wide range of plasma components or blood cell types (especially platelets), either activating or inhibiting these. Snake CLPs, with a relatively conservative and homologous structure (primary, secondary, and tertiary), are unique in their diverse biological targets and have become useful tools in studies of protein structural and functional relationships. The thorough characterization of convulxin, a snake-derived CLP, has contributed greatly to the cloning and identication of glycoprotein (GP) VI and helped to open the eld of platelet signaling transduction pathways via GPVI. Botrocetin, a von Willebrand Factor (VWF) modulator, has been broadly applied in clinical diagnostics. In this work, we will report recent ndings on snake venom-derived CLPs and sugar binding lectins, as well as their targets and interacting mechanisms.
