Structural and functional characterization of two novel peptide toxins isolated from the venom of the social wasp Polybia paulista
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Data
2005-11-01
Autores
Souza, B. M.
Mendes, M. A.
Santos, L. D.
Marques, M. R.
Cesar, LMM
Almeida, RNA
Pagnocca, F. C.
Konno, K.
Palma, Mario Sergio [UNESP]
Título da Revista
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Editor
Elsevier B.V.
Resumo
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-NH2 (1654.09 Da),Polybia-CP: I L G T I L G L L K S L-NH2 (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. (c) 2005 Elsevier B.V. All rights reserved.
Descrição
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Polybia paulista, hymenoptera insect, polycationic peptide, wasp venom, mastoparans, chemotactic peptides
Como citar
Peptides. New York: Elsevier B.V., v. 26, n. 11, p. 2157-2164, 2005.