Effect on platelet FXIII and partial characterization of Lonomin V, a proteolytic enzyme from Lonomia achelous caterpillars.

Contact with Lonomia achelous caterpillars venom induces a severe bleeding syndrome in humans. A constant finding in all reported cases is a marked decrease of blood coagulation factor XIII (FXIII), which has been attributed to the presence of a proteolytic enzyme, isolated and named Lonomin V, in the hemolymph and hair secretion. In this study, the effect of Lonomin V on transglutaminase activity from human plasma, rabbit plasma, and platelet FXIII was analyzed. The decrease of activity was more pronounced in platelet (A2) when compared with rabbit plasma (AB) and human plasma FXIII (A2B2). This finding might be explained by the differences in FXIII molecular structure. In addition, platelet FXIII molecule was degraded by Lonomin to several fragments of low molecular mass. Lonomin V was stable over a wide range of pH (6-8.5) and temperatures of -70 degrees C, -20 degrees C and between 4 to 24 degrees C, with a progressive decrease at 37 degrees C and total inactivation at 60 degrees C after 2 hours incubation. Diisopropyl fluoro-phosphate, phenylmethylsulfonyl fluoride, tosyl-l-lysine chloromethyl ketone, and iodoacetamide abolished the effect of Lonomin V on FXIII; in contrast dithiothreitol and EDTA-Na enhance the activity. We concluded that Lonomin V is a serine proteinase with a free Cys essential for the enzymatic activity. Due to its proteolytic activity on FXIII, with concomitant impairment of fibrin cross-linking, Lonomin V might be useful in association with thrombolytic drugs for preventing rethrombosis.