103 resultados para Vespa


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The hornet possesses highly toxic venom, which is rich in toxin, enzymes and biologically active peptides. Many bioactive substances were identified from wasp venom. Two families of antimicrobial peptides were purified and characterized from the venom of

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Despite the evolutional distance between wasp and amphibian, vespid chemotactic peptide (VCP), an important component of wasp venom, are found sharing remarkable similarities with the temporin antimicrobial peptides (AMPs) from Ranid frog, Amolops loloens

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Wasp is an important venomous animal that can induce human fatalities. Coagulopathy is a clinical symptom after massive wasp stings, but the reason leading to the envenomation manifestation is still not known. In this paper, a toxin protein is purified and characterized by Sephadex G-75 gel filtration, CM-Sephadex C-25 cationic exchange and fast protein liquid chromatography (FPLC) from the venom of the wasp, Vespa magnifica (Smith). This protein, named magnvesin. contains serine protease-like activity and inhibits blood coagulation. The cDNA encoding magnvesin is cloned from the venom sac cDNA library of the wasp. The deduced protein from the cDNA is composed of 305 amino acid residues. Magnvesin shares 52% identity with allergen serine protease from the wasp Polistes dominulus. Magnvesin exerted its anti-coagulant function by hydrolyzing coagulant factors TF, VII, VIII, IX and X. (c) 2008 Elsevier Ltd. All rights reserved.

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Wasp is an impor tant venomous animal that can induce human fatalities. Aortic thrombosis and cerebral infarction are major clinical symptoms after massive wasp stings but the reason leading to the envenomation manifestation is still not known. In this paper, a toxin protein is purified and characterized by Sephadex G-75 gel filtration, CM-Sephadex C-25 cationic exchange and fast protein liquid chromatography (FPLC) from the venom of the wasp, Vespa magnifica (Smith). This protein, named magnifin, contains phospholipase-like activity and induces platelet aggregation. The cDNA encoding magnifin is cloned from the venom sac cDNA library of the wasp. The predicted protein was deduced from the cDNA with a sequence composed of 337 amino acid residues. Magnifin is very similar to other phospholipase A(1) (PLA(1)), especially to other wasp allergen PLA(1). Magnifin can activate platelet aggregation and induce thrombosis in vivo. The current results proved that PLA(1) in wasp venom could be contributable to aortic thrombosis after massive wasp stings. (c) 2007 Elsevier Ltd. All rights reserved.

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报道胡蜂属Vespa Linnaeus的系统发育研究结果。运用PAUP(SWOFFORD,1993)软件程序对胡蜂属系统发育关系进行研究,结果将胡蜂属分为2个大的类群,即树巢胡蜂类群(Wood-nesting groups),地巢胡蜂类群(earth-nesting groups),各分为4个亚群。文中还给出了胡蜂属18种的系统发育和包括1个新种的形态描述。

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Ciclo biológico da vespa-da-madeira; Como identificar a vespa-da-madeira; Como identificar árvores atacadas; Danos provocados pela praga; Medidas preventivas; Manejo florestal; Quarentena; Monitoramento para detecção precoce - instalação de árvores-armadilha; Medidas a serem adotadas após a detecção da praga; Mapeamento das áreas atacadas pela vespa-da-madeira; Amostragem sequencial; Controle biológico; Utilização do nematóide Beddingia siridicola; Utilização de insetos parasitóides; Avaliação da eficiência dos agentes de controle biológico.

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Amphibian skin secretions are rich sources of cationic amphipathic peptides which often possess potent and broad-spectrum antimicrobial activity. However, the venoms of other animals such as hymenopteran insects, also contain peptides with these characteristics and the literature is unclear as to their antimicrobial potential. Here we subjected the venom of the European hornet, Vespa crabro, to reverse phase HPLC fractionation followed by screening of aliquots of individual fractions in bacterial zonal inhibition assays. Two major peptides possessing activity in these assays were further purified by HPLC and subjected to MALDI-TOF MS analysis and MS/MS fragmentation using an ESI mass spectrometer. The peptides were identified as mastoparan C (LNLKALLAVAKKILamide) and crabrolin (FLPLILRKIVTALamide). Replicates of both peptides were synthesised by solid-phase methodology and mean inhibitory concentrations (MICs) established against Staphylococcus aureus and Escherichia coli. Mastoparan C was found to be a potent antimicrobial with MIC values of 2 µM and 4 µM against S. aureus and E. coli, respectively. Crabrolin was found to be less potent with MIC values of > 160 µM and 40 µM for S. aureus and E. coli. Hornet venom thus contains a potent antimicrobial peptide that has been unambiguously identified as mastoparan C, a peptide that is known to affect profound histamine release from mast cells and to generally activate membrane G protein-linked receptors. It is thus highly probable that its antimicrobial effects, like those previously documented, are a result of a generalized membrane interactive and disruptive function — perhaps reflective of the authentic role of amphibian skin antimicrobials.

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Dissertação apresentada à Escola Superior de Comunicação Social para obtenção de grau de mestre em Publicidade e Marketing.

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Foram realizadas 100 horas de observação usando o método scanning sample para a qualificação e quantificação dos atos comportamentais de rainhas e operárias de quinze colônias de Polistes canadensis canadensis. Foi descrito um repertório comportamental com 28 atos, no qual rainhas executam 19 atos na colônia, enquanto operárias 26, ocorrendo 17 atos em comum entre as duas castas. Dentre esses atos, dois foram exclusivos do repertório de rainhas e nove de operárias. O resultado do teste do qui-quadrado apontou diferenças significativas entre os repertórios das duas castas, sendo que rainhas permanecem mais tempo no ninho e executam com maior freqüência atividades intra-nidais, ligadas à reprodução, enquanto que as operárias executam mais freqüentemente atividades relacionadas à manutenção das colônias, como a atividade de forrageamento que demanda um maior risco e alto custo energético.

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

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

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Pós-graduação em Ciências Biológicas (Biologia Celular e Molecular) - IBRC