Glicoproteomic analysis of venom from the social wasp Polybia paulista

Abstract

Polybia paulista is a clinically relevant social wasp involved in a high number of sting accidents in Southeast Brazil. As most social Hymenoptera, venom from P. paulista comprises a complex mixture of bioactive toxins ranging from low molecular weight compounds to peptides and proteins such as phospholipases A1 and A2, hyaluronidase, acid phosphatase and antigen 5. In our laboratory, this venom has been investigated by proteomics and peptidomics approaches, besides analysis of allergy studies, which have contributed significantly for the identification of venom compounds as well as get a better understanding about envenoming mechanism. However, many proteins were not identified yet. The results obtained with bottom-up proteomic analyses, previously performed in our laboratory, demonstrated that only the most abundant proteins were identified, whereas the less abundant proteins, and proteins with a low weight were not detected. It's probably not only because of the biochemical composition complexity of venom but also due to the technical limitations of the approach used during the period that the previously study was performed. Thus, we decided to analysis the P. paulista proteome trough shotgun proteomic approach. With this strategy, will be possible to increase the number of protein identifications in the venom, as well as use enrichment methods for proteins and peptides glycosylated affinity, allowing the analysis and identifications of molecules that present this type of pos-translational modification. The identification of new molecules, can enable the discovery of new drugs, with high biotechnology potential application; besides to contribute for the development of specific immunotherapy strategies against allergenic reactions caused by this wasp venom. (AU)