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, São 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.

Myotoxic effects of mastoparan from Polybia paulista (Hymenoptera, Epiponini) wasp venom in mice skeletal muscle

In a previous study, we showed that the Polybia paulista wasp venom causes strong myonecrosis. This study was undertaken to characterize the myotoxic potency of mastoparan (Polybia-MPII) isolated from venom (0.25 mu g/mu l) and injected in the tibial anterior (TA) muscle (i.m.) of Balb/c mice. The time course of the changes was followed at muscle degenerative (3 and 24 h) and regenerative (3, 7, and 21 days) periods (n = 6) after injection and compared to matched controls by calculation of the percentage of cross-sectional area affected and determination of creatine kinase (CK) activity (n = 10). The results showed that although NIP was strongly myotoxic, its capacity for regeneration was maintained high. Since the extent of tissue damage was not correlated with the CK serum levels, which remained very low, we raised the hypothesis that the enzyme underwent denaturation by the peptide. Evidence suggested that MP induced the death of TA fibers by necrosis and apoptosis and had the sarcolemma as its primordial target. Given its amphiphilic polycationic nature and based on the vast spectrum of functions attributed to the peptide, we suggest that MP interaction with cell membrane impaired the phosphorylation of dystrophin essential for sarcolemma mechanical stability, and disturbed Ca2+ mobilization with obvious implications on sarcoplasmic reticulum and mitochondrial functioning. (c) 2007 Elsevier Ltd. All rights reserved.

Purification, sequencing and structural characterization of the phospholipase A(1) from the venom of the social wasp Polybia paulista (Hymenoptera, Vespidae)

The biochemical and functional characterization of wasp venom toxins is an important prerequisite for the development of new tools both for the therapy of the toxic reactions due to envenomation caused by multiple stinging accidents and also for the diagnosis and therapy of allergic reactions caused by this type of venom. PLA(1) was purified from the venom of the neotropical social wasp Polybia paulista by using molecular exclusion and cation exchange chromatographies; its amino acid sequence was determined by using automated Edman degradation and compared to the sequences of other vespid venom PLA(1)'s. The enzyme exists as a 33,961.40 da protein, which was identified as a lipase of the GX class, liprotein lipase superfamily, pancreatic lipases (ab20.3) homologous family and RP2 sub-group of phospholipase. P. paulista PLA(1) is 53-82% identical to the phospholipases from wasp species from Northern Hemisphere. The use restrained-based modeling permitted to describe the 3-D structure of the enzyme, revealing that its molecule presents 23% alpha-helix, 28% beta-sheet and 49% coil. The protein structure has the alpha/beta fold common to many lipases; the core consists of a tightly packed beta-sheet constituted of six-stranded parallel and one anti-parallel beta-strand, surrounded by four alpha-helices. P. paulista PLA(1) exhibits direct hemolytic action against washed red blood cells with activity similar to the Cobra cardiotoxin from Naja naja atra. In addition to this, PLA(1) was immunoreactive to specific IgE from the sera of P. paulista-sensitive patients. (c) 2007 Elsevier Ltd. All rights reserved.

Environmental factors influencing foraging activity in the social wasp Polybia paulista (Hymenoptera: Vespidae: Epiponini)

Foraging behavior in social wasps is important in the development of the colony and reflects an important ecological interaction between the colony and the environment. Although the social traits of the colony play a role in the foraging activities, the conditions that establish the space and time limits are mainly physical. Here, we evaluate colonies of Polybia paulista throughout one year in order to verify the foraging activities and the items collected, as well as the importance of temperature, relative humidity, and solar radiation on motivating foraging. Collection of liquids was always higher than that of solids; preys were collected all year long, and nests showed two annual episodic expansions. The linear mixed effects (LME) model used to analyze which weather factors influence the foraging showed temperature as the most influencing factor on the collection of materials. © 2011 Naila Cristina de Souza Canevazzi and Fernando Barbosa Noll.

Hyaluronidase from the venom of the social wasp Polybia paulista (Hymenoptera, Vespidae): Cloning, structural modeling, purification, and immunological analysis

In this study, we describe the cDNA cloning, sequencing, and 3-D structure of the allergen hyaluronidase from Polybia paulista venom (Pp-Hyal). Using a proteomic approach, the native form of Pp-Hyal was purified to homogeneity and used to produce a Pp-specific polyclonal antibody. The results revealed that Pp-Hyal can be classified as a glycosyl hydrolase and that the full-length Pp-Hyal cDNA (1315 bp; GI: 302201582) is similar (80-90%) to hyaluronidase from the venoms of endemic Northern wasp species. The isolated mature protein is comprised of 338 amino acids, with a theoretical pI of 8.77 and a molecular mass of 39,648.8 Da versus a pI of 8.13 and 43,277.0 Da indicated by MS. The Pp-Hyal 3D-structural model revealed a central core (α/β)7 barrel, two sulfide bonds (Cys 19-308 and Cys 185-197), and three putative glycosylation sites (Asn79, Asn187, and Asn325), two of which are also found in the rVes v 2 protein. Based on the model, residues Ser299, Asp107, and Glu109 interact with the substrate and potential epitopes (five conformational and seven linear) located at surface-exposed regions of the structure. Purified native Pp-Hyal showed high similarity (97%) with hyaluronidase from Polistes annularis venom (Q9U6V9). Immunoblotting analysis confirmed the specificity of the Pp-Hyal-specific antibody as it recognized the Pp-Hyal protein in both the purified fraction and P. paulista crude venom. No reaction was observed with the venoms of Apis mellifera, Solenopsis invicta, Agelaia pallipes pallipes, and Polistes lanio lanio, with the exception of immune cross-reactivity with venoms of the genus Polybia (sericea and ignobilis). Our results demonstrate cross-reactivity only between wasp venoms from the genus Polybia. The absence of cross-reactivity between the venoms of wasps and bees observed here is important because it allows identification of the insect responsible for sensitization, or at least of the phylogenetically closest insect, in order to facilitate effective immunotherapy in allergic patients. © 2013 Elsevier Ltd.

Caracterização molecular e expressão heteróloga do alérgeno fosfolipase A1 do veneno de Polybia paulista (Hymenoptera; Vespidae)

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Clonagem, análise estrutural e imunológica do alérgeno antígeno 5 do veneno da vespa Polybia paulista (Hymenoptera : Vespidae)

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Determinação da seqüência de cDNA da enzima hialuronidase do veneno de Polybia paulista (Hymenoptera : vespidae)

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Análise imunológica comparada da eficiência e especificidade da hialuronidase recombinante de Polybia paulista (Hymenoptera, Vespidae) expressa em bactéria e levedura

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

Bioprospecção e caracterização químico-funcional de compostos orgânicos da baixas massas molecularesde venenos das vespas sociais: Agelaia pallipes pallipes, Agelaia vicina e Polybia paulista (Hymenoptera - Vespidae)

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

Reactivity of IgE to the allergen hyaluronidase from Polybia paulista (Hymenoptera, Vespidae) venom

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

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)

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.

Profiling the Proteome of the Venom from the Social Wasp Polybia paulista: A Clue to Understand the Envenoming Mechanism

The study reported here is a classical bottom-up proteomic approach where proteins from wasp venom were extracted and separated by 2-DE; the individual protein spots were proteolytically digested and subsequently identified by using tandem mass spectrometry and database query with the protein search engine MASCOT. Eighty-four venom proteins belonging to 12 different molecular functions were identified. These proteins were classified into three groups; the first is constituted of typical venom proteins: antigens-5, hyaluronidases, phospholipases, heat shock proteins, metalloproteinases, metalloproteinase-desintegrin like proteins, serine proteinases, proteinase inhibitors, vascular endothelial growth factor-related protein, arginine kinases, Sol i-II and -II like proteins, alpha-glucosidase, and superoxide dismutases. The second contained proteins structurally related to the muscles that involves the venom reservoir. The third group, associated with the housekeeping of cells from venom glands, was composed of enzymes, membrane proteins of different types, and transcriptional factors. The composition of P. paulista venom permits us to hypothesize about a general envenoming mechanism based on five actions: (i) diffusion of venom through the tissues and to the blood, (ii) tissue, (iii) hemolysis, (iv) inflammation, and (v) allergy-played by antigen-5, PLA1, hyaluronidase, HSP 60, HSP 90, and arginine kinases.

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

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