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Structural and functional characterization of two novel peptide toxins isolated from the venom of the social wasp Polybia paulista

Two novel inflammatory peptides were isolated from the venom of the social wasp Polybia paulista. They had their molecular masses determined by ESI-MS and their primary sequences were elucidated by Edman degradation chemistry as: • Polybia-MPI: I D W K K L L D A A K Q I L-NH 2 (1654.09 Da), • Polybi...

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Published in:Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2005-11, Vol.26 (11), p.2157-2164
Main Authors: Souza, Bibiana M., Mendes, Maria A., Santos, Lucilene D., Marques, Maurício R., César, Lilian M.M., Almeida, Roberta N.A., Pagnocca, Fernando C., Konno, Katsuhiro, Palma, Mario S.
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Language:English
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Summary:Two novel inflammatory peptides were isolated from the venom of the social wasp Polybia paulista. They had their molecular masses determined by ESI-MS and their primary sequences were elucidated by Edman degradation chemistry as: • Polybia-MPI: I D W K K L L D A A K Q I L-NH 2 (1654.09 Da), • Polybia-CP: I L G T I L G L L K S L-NH 2 (1239.73 Da). Both peptides were functionally characterized by using Wistar rat cells. Polybia-MPI is a mast cell lytic peptide, which causes no hemolysis to rat erythrocytes and presents chemotaxis for polymorphonucleated leukocytes (PMNL) and with potent antimicrobial action both against Gram-positive and Gram-negative bacteria. Polybia-CP was characterized as a chemotactic peptide for PMNL cells, presenting antimicrobial action against Gram-positive bacteria, but causing no hemolysis to rat erythrocytes and no mast cell degranulation activity at physiological concentrations.
ISSN:0196-9781
1873-5169
DOI:10.1016/j.peptides.2005.04.026