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

被引:136
作者
Souza, BM
Mendes, MA
Santos, LD
Marques, MR
César, LMM
Almeida, RNA
Pagnocca, FC
Konno, K
Palma, MS [1 ]
机构
[1] UNESP, CEIS, Dept Biol,IBRC,CAT CEPID FAPESP, Inst Immunol Invest,Millennium Inst,MCT CNPq, BR-13506900 Rio Claro, SP, Brazil
[2] UNESP, IBRC, Dept Biochem & Microbiol, Rio Claro, SP, Brazil
[3] FAPESP, CAT, CEPID, Inst Butantan, Sao Paulo, Brazil
基金
巴西圣保罗研究基金会;
关键词
Polybia paulista; hymenoptera insect; polycationic peptide; wasp venom; mastoparans; chemotactic peptides;
D O I
10.1016/j.peptides.2005.04.026
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 Inc. All rights reserved.
引用
收藏
页码:2157 / 2164
页数:8
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