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.
Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Department of Biochemistry, Faculty of Science, Khon Kaen University, Khon Kaen 40002, Thailand.
Prapenpuksiri
P
Rungsa
Department of Chemistry, Faculty of Engineering, Rajamangala University of Technology Isan, Khon Kaen Campus, Khon Kaen 40000, Thailand.
Paroonkorn
P
Incamnoi
Chulabhorn International College of Medicine, Thammasat University, Rangsit Campus, Pathumthani 12120, Thailand.
Sophida
S
Sukprasert
Division of Chemistry, Faculty of Science, Nakhon Phanom University, Nakhon Phanom 48000, Thailand.
Nunthawun
N
Uawonggul
Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Department of Biochemistry, Faculty of Science, Khon Kaen University, Khon Kaen 40002, Thailand.
Sompong
S
Klaynongsruang
Department of Clinical Chemistry, Faculty of Associated Medical Sciences, Khon Kaen University, Khon Kaen 40002, Thailand.
Jureerut
J
Daduang
Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Department of Biochemistry, Faculty of Science, Khon Kaen University, Khon Kaen 40002, Thailand.
Rina
R
Patramanon
Genome Institute, National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency (NSTDA), Pathumthani, Thailand.
Sittiruk
S
Roytrakul
Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Department of Biochemistry, Faculty of Science, Khon Kaen University, Khon Kaen 40002, Thailand; Division of Pharmacognosy and Toxicology, Faculty of Pharmaceutical Sciences, Khon Kaen University, Khon Kaen 40002, Thailand. Electronic address: sakdad@kku.ac.th.
Sakda
S
Daduang
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D013058:Mass Spectrometry; D040901:Proteomics; D014862:Wasp Venoms / Q000737:chemistry* / Q000145:classification
D014862:Wasp Venoms
Antigen 5; Dipeptidyl peptidase; Hornet; Hyaluronidase; Phospholipase; Proteomics; Venom; Vespa affinis; Vespa tropica; Wasp