Otro
Structural and functional characterization of two novel peptide toxins isolated from the venom of the social wasp Polybia paulista
Registro en:
Peptides. New York: Elsevier B.V., v. 26, n. 11, p. 2157-2164, 2005.
0196-9781
10.1016/j.peptides.2005.04.026
WOS:000233373100016
Autor
Souza, B. M.
Mendes, M. A.
Santos, L. D.
Marques, M. R.
Cesar, LMM
Almeida, RNA
Pagnocca, F. C.
Konno, K.
Palma, Mario Sergio
Resumen
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. Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)