期刊
JOURNAL OF PROTEOME RESEARCH
卷 9, 期 8, 页码 3867-3877出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr1000829
关键词
social wasp venom; Polybia paulista; Hymenoptera; allergy; immunoreactivity; 2-D electrophoresis; mass spectrometry; envenoming mechanism
资金
- FAPESP [05/00982-1]
- BIOprospecTA/FAPESP [06/57122-7]
- INCT/CNPq-Instituto de Investigacoes em Imunologia (iii)
- CNPq
- CAPES
- National Research Council of Brazil-CNPq
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [05/00982-1] Funding Source: FAPESP
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.
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