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Peer-reviewed veterinary case report

Proteins in venoms of two wasps, Polistes comanchus navajoe and Vespa orientalis.

Journal:
Comparative biochemistry and physiology. C: Comparative pharmacology
Year:
1982
Authors:
Bernheimer, A W et al.

Plain-English summary

Researchers studied the venom from two types of wasps, Polistes comanchus navajoe and Vespa orientalis, and found that each had a different number of proteins—six in the first wasp and five in the second, all weighing more than 15,000. Some of these proteins were similar between the two wasps. They identified a key protein in the venom of Polistes comanchus that can break down red blood cells, which is different from similar components found in bee and ant venoms because it is larger and acts like an enzyme. This study helps us understand the unique properties of wasp venom compared to other insects.

Abstract

1. By means of gel electrophoresis the basic proteins in venoms of Polistes comanchus navajoe and Vespa orientalis were resolved into 6 and 5 proteins respectively, all of molecular weights greater than 15,000. 2. Several proteins appeared to be similar in both venoms. 3. The main component of P. comanchus venom responsible for hemolysis was isolated, and data concerning its thermolability, molecular weight (approximately 26,000) and amino acid composition show that unlike the cytolytic components of bee and ant venoms which are small peptides, the corresponding functional entity of P. comanchus venom (polistin) is a protein having the characteristics of an enzyme.

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Original publication: https://pubmed.ncbi.nlm.nih.gov/6122535/