Profiling the proteome of the venom from the social wasp Polybia paulista: a clue to understand the envenoming mechanism.
The study reported here is a classical bottom-up proteomic approach where proteins from wasp venom were extracted and separated by 2-DE; the individual protein spots were proteolytically digested and subsequently identified by using tandem mass spectrometry and database query with the protein search engine MASCOT. Eighty-four venom proteins belonging to 12 different molecular functions were identified. These proteins were classified into three groups; the first is constituted of typical venom proteins: antigens-5, hyaluronidases, phospholipases, heat shock proteins, metalloproteinases, metalloproteinase-desintegrin like proteins, serine proteinases, proteinase inhibitors, vascular endothelial growth factor-related protein, arginine kinases, Sol i-II and -II like proteins, alpha-glucosidase, and superoxide dismutases. The second contained proteins structurally related to the muscles that involves the venom reservoir. The third group, associated with the housekeeping of cells from venom glands, was composed of enzymes, membrane proteins of different types, and transcriptional factors. The composition of P. paulista venom permits us to hypothesize about a general envenoming mechanism based on five actions: (i) diffusion of venom through the tissues and to the blood, (ii) tissue, (iii) hemolysis, (iv) inflammation, and (v) allergy-played by antigen-5, PLA1, hyaluronidase, HSP 60, HSP 90, and arginine kinases.
dos Santos
Lucilene Delazari
LD
Institute of Biosciences of Rio Claro, Department of Biology, Center of the Study of Social Insects, University of Sao Paulo State (UNESP), Rio Claro, SP, Brazil.
Santos
Keity Souza
KS
Pinto
José Roberto Aparecido
JR
Dias
Nathalia Baptista
NB
de Souza
Bibiana Monson
BM
dos Santos
Marise Fonseca
MF
Perales
Jonas
J
Domont
Gilberto Barbosa
GB
Castro
Fabio Morato
FM
Kalil
Jorge Elias
JE
Palma
Mario Sergio
MS
D000818:Animals; D001938:Brazil; D019295:Computational Biology; D015180:Electrophoresis, Gel, Two-Dimensional; D006031:Glycosylation; D007091:Image Processing, Computer-Assisted; D015151:Immunoblotting; D007299:Insect Bites and Stings / Q000235:genetics / Q000378:metabolism / Q000503:physiopathology*; D019476:Insect Proteins / Q000302:isolation & purification* / Q000378:metabolism; D040901:Proteomics / Q000379:methods*; D053719:Tandem Mass Spectrometry; D014862:Wasp Venoms / Q000737:chemistry* / Q000378:metabolism; D014863:Wasps / Q000737:chemistry* / Q000378:metabolism
D019476:Insect Proteins; D014862:Wasp Venoms