Comparative proteomic analysis of two wasps venom, Vespa tropica and Vespa affinis.

Vespid venom is composed of many bioactive compounds. The venom of the banded tiger wasp (Vespa affinis, or VA) and the great banded wasp (Vespa tropica, or VT)-which are locally found in the northeastern part of Thailand and are well known for their life-threatening venom potency-were comparatively studied in terms of potency, composition and biological activity. Clinical studies that included word-of-mouth information shared by traditional healers in local areas noted that the venom of VT is more potent than that of VA. Our previous study showed that the venom of VA is lower in potency (PD50 = 12.5 µg/g body weight) than that of VT (PD50 = 3 µg/g body weight). Analysis with the PAGE technique showed that these two venoms showed similar patterns of active proteins. Most protein spots were basic proteins at an isoelectric point (pI) ranging from 5 to 10, with molecular weights between 27 and 50 kDa. These spots were identified as hyaluronidase, phospholipase, antigen 5, dipeptidyl peptidase and albumin-like protein. The proportion of hyaluronidase was 2.5 times higher in VT than in VA. VT also showed higher hyaluronidase, phospholipase and dipeptidyl peptidase activities, suggesting that these components made VT venom more potent than VA venom.

Extensive inter- and intraspecific venom variation in closely related parasites targeting the same host: the case of Leptopilina parasitoids of Drosophila.

The arms race between immune suppressive parasites that produce virulence factors and hosts that evolve resistance to these factors is suggested to be a key driver for the diversification of both partners. However, little is known regarding the diversity of virulence factors in closely related parasites or the mechanisms underlying the variation of virulence. One of the best-described model to address this issue is the interaction between Leptopilina parasitic wasps and their Drosophila hosts, in which variation of virulence is well documented. Thanks to a combined transcriptomic and proteomic approach, we have identified the main secreted proteins in the venom of Leptopilina heterotoma (Gotheron strain, 66 proteins) and of two well-characterized strains of Leptopilina boulardi, ISm and ISy (65 and 49 proteins, respectively). Results revealed significant quantitative differences in venom components between the L. boulardi strains, in agreement with their different virulence properties. Strikingly, the two related Leptopilina species did not share any abundant venom protein. The main identified proteins in L. boulardi were RhoGAPs and serpins while an aspartylglucosaminidase (AGA) was found abundant in L. heterotoma. The extensive quantitative variation observed between these species may be related with their use of different virulence strategies and/or to differences in their host range (specialist versus generalist). Altogether, our data suggests that parasitoid venom can quickly evolve, mainly through rapid changes in regulation of gene expression. It also evidences venom evolutionary processes largely described in other venomous animals i.e. the convergent recruitment of venom proteins between phylogenetically unrelated organisms, and the role of duplications in the emergence of multigenic families of virulence factors.

Protein kinase C activation generates superoxide and contributes to impairment of cerebrovasodilation induced by G protein activation after brain injury.

Previous studies have observed that activation of protein kinase C (PKC) contributes to generation of superoxide anion (O(-)(2)) after fluid percussion brain injury (FPI). This study was designed to characterize the effects of FPI on the vascular activity of two activators of a pertussis toxin sensitive G protein, mastoparan and mastoparan-7, and the role of PKC dependent O(-)(2) generation in such effects in newborn pigs equipped with a closed cranial window. Mastoparan (10(-8), 10(-6) M) elicited pial artery dilation that was blunted by FPI and partially restored by the PKC inhibitor chelerythrine (10(-7) M) or the O(-)(2) free radical scavengers polyethylene glycol superoxide dismutase and catalase (SODCAT) (9+/-1 and 16+/-1, sham control; 3+/-1 and 5+/-1, FPI; and 7+/-1 and 11+/-1%, FPI SODCAT pretreated). Similar results were observed for mastoparan-7 but the inactive analogue mastoparan-17 had no effect on pial artery diameter. Exposure of the cerebral cortex to a xanthine oxidase O(-)(2) generating system blunted mastoparan induced pial artery dilation similar to FPI (10+/-1 and 17+/-1 vs. 2+/-1 and 3+/-1%). Pertussis toxin (1 microg/ml) exposure blocked mastoparan and mastoparan-7 vasodilation. These data show that pertussis toxin sensitive G protein activation elicits cerebrovasodilation that is blunted following FPI in a PKC dependent manner. These data also show that O(-)(2) generation similarly blunts G protein mediated cerebrovasodilation. These data suggest that PKC dependent O(-)(2) generation contributes to impaired G protein mediated cerebrovasodilation after FPI.