Structural and biological characterization of three novel mastoparan peptides from the venom of the neotropical social wasp Protopolybia exigua (Saussure)

The venom of the Neotropical social wasp Protopolybia exigua(Saussure) was fractionated by RP-HPLC resulting in the elution of 20 fractions. The homogeneity of the preparations were checked out by using ESI-MS analysis and the fractions 15, 17 and 19 (eluted at the most hydrophobic conditions) were...

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Bibliographic Details
Published in:Toxicon (Oxford) 2005, Vol.45 (1), p.101-106
Main Authors: Mendes, Maria Anita, de Souza, Bibiana Monson, Palma, Mario Sergio
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animal poisons toxicology. Antivenoms
Animals
Antimicrobial peptide
Biological and medical sciences
Cell Degranulation - drug effects
Dose-Response Relationship, Drug
Erythrocytes - drug effects
G-protein receptor
Hemolysis
In Vitro Techniques
Insect Proteins - chemistry
Insect Proteins - pharmacology
Logistic Models
Mast Cells - drug effects
Mastoparan
Medical sciences
Molecular Structure
Protopolybia exigua
Rats
Social wasp
Toxicology
Wasp Venoms - chemistry
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Summary:The venom of the Neotropical social wasp Protopolybia exigua(Saussure) was fractionated by RP-HPLC resulting in the elution of 20 fractions. The homogeneity of the preparations were checked out by using ESI-MS analysis and the fractions 15, 17 and 19 (eluted at the most hydrophobic conditions) were enough pure to be sequenced by Edman degradation chemistry, resulting in the following sequences: Protopolybia MPI I-N-W-L-K-L-G-K-K-V-S-A-I-L-NH 2 Protopolybia-MP II I-N-W-K-A-I-I-E-A-A-K-Q-A-L-NH 2 Protopolybia-MP III I-N-W-L-K-L-G-K-A-V-I-D-A-L-NH 2 All the peptides were manually synthesized on-solid phase and functionally characterized. Protopolybia-MP I is a hemolytic mastoparan, probably acting on mast cells by assembling in plasma membrane, resulting in pore formation; meanwhile, the peptides Protopolybia-MP II and -MP III were characterized as a non-hemolytic mast cell degranulator toxins, which apparently act by virtue of their binding to G-protein receptor, activating the mast cell degranulation.
ISSN:0041-0101
1879-3150
DOI:10.1016/j.toxicon.2004.09.015