Peptide diversity in the venom of the social wasp Polybia paulista (Hymenoptera): A comparison of the intra- and inter-colony compositions

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Análise histoquímica comparativa das glândulas de veneno de abelhas Apis mellifera africanizada e das vespas Polistes versicolor, Agelaia palipes palipes e Polybia paulista

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Peptidome profiling of venom from the social wasp Polybia paulista

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Estudos da atividade geral, antinociceptiva/nociceptiva, anti-inflamatória/inflamatória da β-feniletilamina (FEA), uma substância isolada do veneno de vesta Polybia paulista

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Exometaboloma do tegumento da vespa social Polybia paulista por análises GC-MS: bases moleculares do reconhecimento de tipos parentais

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Otimização dos métodos de expressão e solubilização do alérgeno fosfolipase A1 do veneno de Polybia paulista

A vespa social Polybia paulista (Hymenoptera, Vespidae) é bastante abundante e endêmica nos Estados de São Paulo e sul de Minas Gerais. Os indivíduos da espécie causam um elevado número de acidentes de importância médica. Após a ferroada a vítima pode experimentar reações imunológicas locais e/ou sistêmicas, que em alguns casos podem conduzir a anafilaxia e morte. O diagnóstico e terapia de alergia à ferroada de P. paulista é baseado no uso de extrato de veneno bruto o que se associa à ocorrência de reatividade cruzada e reações imunológicas adversas durante a imunoterapia. O uso de alérgenos recombinantes (r) tem-se mostrado como uma alternativa interessante para reduzir o impacto destas desvantagens. Neste trabalho, foram avaliadas diferentes condições para otimizar a expressão recombinante e solubilização dos corpúsculos de inclusão da fosfolipase A1 (Poly p 1) (70kDa) do veneno de P. paulista previamente obtida mediante expressão heteróloga no sistema procariótico, Escherichia coli. Os resultados aqui obtidos contribuirão para aumentar as quantidades do r Poly p 1 necessárias para sua avaliação bioquímica e imunológica, e finalmente para melhorar os resultados do diagnóstico e imunoterapia específica de alergia ao veneno de P. paulista

Otimização dos métodos de expressão e solubilização do alérgeno fosfolipase A1 do veneno de Polybia paulista

A vespa social Polybia paulista (Hymenoptera, Vespidae) é bastante abundante e endêmica nos Estados de São Paulo e sul de Minas Gerais. Os indivíduos da espécie causam um elevado número de acidentes de importância médica. Após a ferroada a vítima pode experimentar reações imunológicas locais e/ou sistêmicas, que em alguns casos podem conduzir a anafilaxia e morte. O diagnóstico e terapia de alergia à ferroada de P. paulista é baseado no uso de extrato de veneno bruto o que se associa à ocorrência de reatividade cruzada e reações imunológicas adversas durante a imunoterapia. O uso de alérgenos recombinantes (r) tem-se mostrado como uma alternativa interessante para reduzir o impacto destas desvantagens. Neste trabalho, foram avaliadas diferentes condições para otimizar a expressão recombinante e solubilização dos corpúsculos de inclusão da fosfolipase A1 (Poly p 1) (70kDa) do veneno de P. paulista previamente obtida mediante expressão heteróloga no sistema procariótico, Escherichia coli. Os resultados aqui obtidos contribuirão para aumentar as quantidades do r Poly p 1 necessárias para sua avaliação bioquímica e imunológica, e finalmente para melhorar os resultados do diagnóstico e imunoterapia específica de alergia ao veneno de P. paulista

EXTERNAL MORPHOLOGY OF THE IMMATURES OF POLYBIA PAULISTA (HYMENOPTERA: VESPIDAE)

The immatures of Polybia paulista Ihering were described using light and scanning electron microscopy and the results are compared with previous descriptions within the same or related wasps. This study is based on 2 whole nests collected in the municipality of Rio Claro, Sao Paulo, in Brazil. We have detected the existence of 5 larval instars. The main morphological alterations over development occur in the relative size of structures, yet certain structures appear with subsequent instars and become more evident later in development: increasing density in the number of body spines and papillae; the appearance of body setae in fifth-instar larvae; opening of spiracles upon second-instar larvae; 2 body shapes in fifth-instar larvae; the appearance of a lateral tooth on the mandibles of fourth instar; presence of spines on the maxillae of fifth-instar larvae; altered shape of galea and palps upon third-instar larvae from a cluster of sensilla to a conical elevation; and the appearance of spines on postmentum upon fourth-instar larvae. This way, the present study presents a detailed description of the immatures of P. paulista, and we hope the presented information can be useful to morphological, taxonomic, and phylogenetic studies.

Renal- and calcium-dependent vascular effects of Polybia paulista wasp venom

In the present study, the effects of Polybia paulista venom (PPV) on renal and vascular tissues were investigated. Isolated kidneys perfused with PPV (1 and 3 mu g/mL) had increased perfusion pressure, renal vascular resistance, urinary flow, and glomerular filtration rate; and reduced sodium tubular transport. Histological evaluation demonstrated deposits of proteins in Bowman's space and tubular lumen, and focal areas of necrosis. The venom promoted a cytotoxic effect on Madin-Darby canine kidney (MDCK) cells. A significant increase in lactic dehydrogenase levels was observed in response to venom exposure. In isolated mesenteric vascular beds, pressure and vascular resistance augmented in a dose-dependent manner. PPV increased the contractility of aortic rings maintained under basal tension. This contractile response was inhibited when preparations were maintained in Ca2+-free medium. Likewise, verapamil, a voltage-gated calcium channel blocker, also inhibited the contractile response. In this study, phentolamine, a blocker of a-adrenergic receptor blocker, significantly reduced the contractile effect of PPV in the aortic ring. In conclusion, PPV produced nephrotoxicity, which suggests a direct effect on necrotic cellular death in renal tubule cells. The vascular contractile effect of PPV appears to involve calcium influx through voltage-gated calcium channels via adrenergic regulation.

Selectivity in the mechanism of action of antimicrobial mastoparan peptide Polybia-MP1

Many potent antimicrobial peptides also present hemolytic activity, an undesired collateral effect for the therapeutic application. Unlike other mastoparan peptides, Polybia-MP1 (IDWKKLLDAAKQIL), obtained from the venom of the social wasp Polybia paulista, is highly selective of bacterial cells. The study of its mechanism of action demonstrated that it permeates vesicles at a greater rate of leakage on the anionic over the zwitterionic, impaired by the presence of cholesterol or cardiolipin; its lytic activity is characterized by a threshold peptide to lipid molar ratio that depends on the phospholipid composition of the vesicles. At these particular threshold concentrations, the apparent average pore number is distinctive between anionic and zwitterionic vesicles, suggesting that pores are similarly formed depending on the ionic character of the bilayer. To prospect the molecular reasons for the strengthened selectivity in Polybia-MP1 and its absence in Mastoparan-X, MD simulations were carried out. Both peptides presented amphipathic alpha-helical structures, as previously observed in Circular Dichroism spectra, with important differences in the extension and stability of the helix; their backbone solvation analysis also indicate a different profile, suggesting that the selectivity of Polybia-MP1 is a consequence of the distribution of the charged and polar residues along the peptide helix, and on how the solvent molecules orient themselves according to these electrostatic interactions. We suggest that the lack of hemolytic activity of Polybia-MP1 is due to the presence and position of Asp residues that enable the equilibrium of electrostatic interactions and favor the preference for the more hydrophilic environment.

Inflammation and apoptosis induced by mastoparan Polybia-MPII on skeletal muscle

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

The neurotoxicological effects of mastoparan Polybia-MPII at the murine neuromuscular junction: an ultrastructural and immunocytochemical study

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Influence of the Bilayer Composition on the Binding and Membrane Disrupting Effect of Polybia-MP1, an Antimicrobial Mastoparan Peptide with Leukemic T-Lymphocyte Cell Selectivity

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Selectivity in the mechanism of action of antimicrobial mastoparan peptide Polybia-MP1

Many potent antimicrobial peptides also present hemolytic activity, an undesired collateral effect for the therapeutic application. Unlike other mastoparan peptides, Polybia-MP1 (IDWKKLLDAAKQIL), obtained from the venom of the social wasp Polybia paulista, is highly selective of bacterial cells. The study of its mechanism of action demonstrated that it permeates vesicles at a greater rate of leakage on the anionic over the zwitterionic, impaired by the presence of cholesterol or cardiolipin; its lytic activity is characterized by a threshold peptide to lipid molar ratio that depends on the phospholipid composition of the vesicles. At these particular threshold concentrations, the apparent average pore number is distinctive between anionic and zwitterionic vesicles, suggesting that pores are similarly formed depending on the ionic character of the bilayer. To prospect the molecular reasons for the strengthened selectivity in Polybia-MP1 and its absence in Mastoparan-X, MD simulations were carried out. Both peptides presented amphipathic alpha-helical structures, as previously observed in Circular Dichroism spectra, with important differences in the extension and stability of the helix; their backbone solvation analysis also indicate a different profile, suggesting that the selectivity of Polybia-MP1 is a consequence of the distribution of the charged and polar residues along the peptide helix, and on how the solvent molecules orient themselves according to these electrostatic interactions. We suggest that the lack of hemolytic activity of Polybia-MP1 is due to the presence and position of Asp residues that enable the equilibrium of electrostatic interactions and favor the preference for the more hydrophilic environment.