Taxonomic notes on the primary types of some species of Centris bees described by some entomologists from the Americas (Hymenoptera: Apidae) / Notas taxonômicas sobre os tipos primários de algumas espécies de abelhas do gênero Centris descritas por alguns entomologistas das Américas (Hymenoptera: Apidae)

In this paper are presented notes on the primary types of some species of the oil-collecting bees of the genus Centris Fabricius, 1804 described by Alpheus Packard, Arturo Roig-Alsina, Charles Michener, Flamínio Ruiz, Haroldo Toro, James Crawford, Jesus Santiago Moure, Philip Timberlake, and Roy Snelling. Information on the type status, type locality and depository are provided.(AU)

Neste artigo são apresentadas notas sobre os tipos primários de algumas espécies de abelhas coletoras de óleo do gênero Centris Fabricius, 1804 descritas por Alpheus Packard, Arturo Roig-Alsina, Charles Michener, Flamínio Ruiz, Haroldo Toro, James Crawford, Jesus Santiago Moure, Philip Timberlake e Roy Snelling. São fornecidas informações sobre o status dos tipos, localidade tipo e depositário.(AU)

Report of the nest of Megachile (Moureapis) benigna (Hymenoptera: Megachilidae) from an urban environment, Rio de Janeiro, Brazil / Registro do ninho de Megachile (Moureapis) benigna (Hymenoptera: Megachilidae) em uma área urbana do Rio de Janeiro, Brasil

One nest of Megachile (Moureapis) benigna Mitchell, 1930 (Hymenoptera: Megachilidae) was collected using trap-nests in a forest fragment (Atlantic Forest biome) into an urban matrix in Rio de Janeiro, Brazil, in October/2017. The nest architecture and larval food are presented providing initial data for management and conservation of this species in cities.

Um ninho de Megachile (Moureapis) benigna Mitchell, 1930 (Hymenoptera: Megachilidae) foi coletado usando ninhos-armadilha em um fragmento de floresta (bioma Mata Atlântica) em uma área urbana no Rio de Janeiro, Brasil, em outubro/2017. A arquitetura do ninho e o alimento larval são apresentados fornecendo dados iniciais para o manejo e conservação desta espécie nas cidades.

Report of the nest of Megachile (Moureapis) benigna (Hymenoptera: Megachilidae) from an urban environment, Rio de Janeiro, Brazil

ABSTRACT One nest of Megachile (Moureapis) benigna Mitchell, 1930 (Hymenoptera: Megachilidae) was collected using trap-nests in a forest fragment (Atlantic Forest biome) into an urban matrix in Rio de Janeiro, Brazil, in October/2017. The nest architecture and larval food are presented providing initial data for management and conservation of this species in cities.

RESUMO Um ninho de Megachile (Moureapis) benigna Mitchell, 1930 (Hymenoptera: Megachilidae) foi coletado usando ninhos-armadilha em um fragmento de floresta (bioma Mata Atlântica) em uma área urbana no Rio de Janeiro, Brasil, em outubro/2017. A arquitetura do ninho e o alimento larval são apresentados fornecendo dados iniciais para o manejo e conservação desta espécie nas cidades.

Nesting biology of the oil-collecting bee Epicharis (Hoplepicharis) fasciata (Hymenoptera: Apidae) in an urban area of Rio de Janeiro, RJ, Brazil / Biologia da nidificação da abelha coletora de óleo Epicharis (Hoplepicharis) fasciata (Hymenoptera: Apidae) em uma área urbana do Rio de Janeiro, RJ, Brasil

Nests of the oil-collecting bee Epicharis (Hoplepicharis) fasciata Lepeletier & Serville, 1828 were studied at the Jardim Botânico of Rio de Janeiro, Brazil. The females constructed their nests in an area of 609 m2 of mostly sandy flat soil. The nest architecture was relatively simple, with a main tunnel of approximately 30 cm in depth with one or two lateral tunnels ending in a single brood cell. Adult activity lasted approximately 45 days. The females dug the tunnels, constructed the brood cells, collected provisions and laid the eggs in approximately two days. Diapause occurred in the post defecating larval stage, and there was no cocoon. Nest architecture and the morphology of the brood cells are described and illustrated.(AU)

Ninhos da abelha coletora de óleo Epicharis (Hoplepicharis) fasciata Lepeletier & Serville, 1828 foram estudados no Jardim Botânico do Rio de Janeiro, Brasil. As fêmeas construíram seus ninhos em uma área de 609 m2 de solo plano principalmente arenoso. A arquitetura do ninho é relativamente simples, com um túnel principal de aproximadamente 30 cm de profundidade, com um ou dois túneis laterais terminando em uma única célula de cria. A atividade dos adultos se estendeu por cerca de 45 dias. As fêmeas cavam os túneis, constroem as células de cria, coletam as provisões e depositam os ovos em aproximadamente dois dias. A diapausa ocorreu no estágio de larva pós-defecante e não houve casulo. A arquitetura dos ninhos e a morfologia das células de cria são descritas e ilustradas.(AU)

Nesting biology of the oil-collecting bee Epicharis (Hoplepicharis) fasciata (Hymenoptera: Apidae) in an urban area of Rio de Janeiro, RJ, Brazil / Biologia da nidificação da abelha coletora de óleo Epicharis (Hoplepicharis) fasciata (Hymenoptera: Apidae) em uma área urbana do Rio de Janeiro, RJ, Brasil

Nests of the oil-collecting bee Epicharis (Hoplepicharis) fasciata Lepeletier & Serville, 1828 were studied at the Jardim Botânico of Rio de Janeiro, Brazil. The females constructed their nests in an area of 609 m2 of mostly sandy flat soil. The nest architecture was relatively simple, with a main tunnel of approximately 30 cm in depth with one or two lateral tunnels ending in a single brood cell. Adult activity lasted approximately 45 days. The females dug the tunnels, constructed the brood cells, collected provisions and laid the eggs in approximately two days. Diapause occurred in the post defecating larval stage, and there was no cocoon. Nest architecture and the morphology of the brood cells are described and illustrated.

Ninhos da abelha coletora de óleo Epicharis (Hoplepicharis) fasciata Lepeletier & Serville, 1828 foram estudados no Jardim Botânico do Rio de Janeiro, Brasil. As fêmeas construíram seus ninhos em uma área de 609 m2 de solo plano principalmente arenoso. A arquitetura do ninho é relativamente simples, com um túnel principal de aproximadamente 30 cm de profundidade, com um ou dois túneis laterais terminando em uma única célula de cria. A atividade dos adultos se estendeu por cerca de 45 dias. As fêmeas cavam os túneis, constroem as células de cria, coletam as provisões e depositam os ovos em aproximadamente dois dias. A diapausa ocorreu no estágio de larva pós-defecante e não houve casulo. A arquitetura dos ninhos e a morfologia das células de cria são descritas e ilustradas.

Nesting biology of the oil-collecting bee Epicharis (Hoplepicharis) fasciata (Hymenoptera: Apidae) in an urban area of Rio de Janeiro, RJ, Brazil

ABSTRACT Nests of the oil-collecting bee Epicharis (Hoplepicharis) fasciata Lepeletier & Serville, 1828 were studied at the Jardim Botânico of Rio de Janeiro, Brazil. The females constructed their nests in an area of 609 m2 of mostly sandy flat soil. The nest architecture was relatively simple, with a main tunnel of approximately 30 cm in depth with one or two lateral tunnels ending in a single brood cell. Adult activity lasted approximately 45 days. The females dug the tunnels, constructed the brood cells, collected provisions and laid the eggs in approximately two days. Diapause occurred in the post defecating larval stage, and there was no cocoon. Nest architecture and the morphology of the brood cells are described and illustrated.

RESUMO Ninhos da abelha coletora de óleo Epicharis (Hoplepicharis) fasciata Lepeletier & Serville, 1828 foram estudados no Jardim Botânico do Rio de Janeiro, Brasil. As fêmeas construíram seus ninhos em uma área de 609 m2 de solo plano principalmente arenoso. A arquitetura do ninho é relativamente simples, com um túnel principal de aproximadamente 30 cm de profundidade, com um ou dois túneis laterais terminando em uma única célula de cria. A atividade dos adultos se estendeu por cerca de 45 dias. As fêmeas cavam os túneis, constroem as células de cria, coletam as provisões e depositam os ovos em aproximadamente dois dias. A diapausa ocorreu no estágio de larva pós-defecante e não houve casulo. A arquitetura dos ninhos e a morfologia das células de cria são descritas e ilustradas.

Peptidomic analysis of the venom of the solitary bee Xylocopa appendiculata circumvolans

Background: Among the hymenopteran insect venoms, those from social wasps and bees - such as honeybee, hornets and paper wasps - have been well documented. Their venoms are composed of a number of peptides and proteins and used for defending their nests and themselves from predators. In contrast, the venoms of solitary wasps and bees have not been the object of further research. In case of solitary bees, only major peptide components in a few venoms have been addressed. Therefore, the aim of the present study was to explore the peptide component profile of the venom from the solitary bee Xylocopa appendiculata circumvolans by peptidomic analysis with using LC-MS. Methods: A reverse-phase HPLC connected to ESI-OrbiTrap MS was used for LC-MS. On-line mass fingerprinting was made from TIC, and data-dependent tandem mass spectrometry gave MSMS spectra. A major peptide component was isolated by reverse-phase HPLC by conventional way, and its sequence was determined by Edman degradation, which was finally corroborated by solid phase synthesis. Using the synthetic specimen, biological activities (antimicrobial activity, mast cell devaluation, hemolysis, leishmanicidal activity) and pore formation in artificial lipid bilayer were evaluated. Results: On-line mass fingerprinting revealed that the crude venom contained 124 components. MS/MS analysis gave 75 full sequences of the peptide components. Most of these are related to the major and novel peptide, xylopin. Its sequence, GFVALLKKLPLILKHLH-NH2, has characteristic features of linear cationic α-helical peptides; rich in hydrophobic and basic amino acids with no disulfide bond, and accordingly, it can be predicted to adopt an amphipathic α-helix secondary structure. In biological evaluation, xylopin exhibited broad-spectrum antimicrobial activity, and moderate mast cell degranulation and leishmanicidal activities, but showed virtually no hemolytic activity. Additionally, the peptide was able to incorporate pores in artificial lipid bilayers of azolectin, confirming the mechanism of the cytolytic activity by pore formation in biological membranes. Conclusions: LC-ESI-MS and MS/MS analysis of the crude venom extract from a solitary bee Xylocopa appendiculata circumvolans revealed that the component profile of this venom mostly consisted of small peptides. The major peptide components, xylopin and xylopinin, were purified and characterized in a conventional manner. Their chemical and biological characteristics, belonging to linear cationic α-helical peptides, are similar to the known solitary bee venom peptides, melectin and osmin. Pore formation in artificial lipid bilayers was demonstrated for the first time with a solitary bee peptide.(AU)

Isolation of biologically active peptides from the venom of Japanese carpenter bee, Xylocopa appendiculata

Background Mass spectrometry-guided venom peptide profiling is a powerful tool to explore novel substances from venomous animals in a highly sensitive manner. In this study, this peptide profiling approach is successfully applied to explore the venom peptides of a Japanese solitary carpenter bee, Xylocopa appendiculata (Hymenoptera: Apoidea: Apidae: Anthophila: Xylocopinae: Xylocopini). Although interesting biological effects of the crude venom of carpenter bees have been reported, the structure and biological function of the venom peptides have not been elucidated yet. Methods The venom peptide profiling of the crude venom of X. appendiculata was performed by matrix-assisted laser desorption/ionization-time of flight mass spectroscopy. The venom was purified by a reverse-phase HPLC. The purified peptides were subjected to the Edman degradation, MS/MS analysis, and/or molecular cloning methods for peptide sequencing. Biological and functional characterization was performed by circular dichroism analysis, liposome leakage assay, and antimicrobial, histamine releasing and hemolytic activity tests. Results Three novel peptides with m/z 16508, 1939.3, and 1900.3 were isolated from the venom of X. appendiculata. The peptide with m/z 16508 was characterized as a secretory phospholipase A2 (PLA2) homolog in which the characteristic cysteine residues as well as the active site residues found in bee PLA2s are highly conserved. Two novel peptides with m/z 1939.3 and m/z 1900.3 were named as Xac-1 and Xac-2, respectively. These peptides are found to be amphiphilic and displayed antimicrobial and hemolytic activities. The potency was almost the same as that of mastoparan isolated from the wasp venom. Conclusion We found three novel biologically active peptides in the venom of X. appendiculata and analyzed their molecular functions, and compared their sequential homology to discuss their molecular diversity. Highly sensitive mass analysis plays an important role in this study.(AU)

Peptidomic analysis of the venom of the solitary bee Xylocopa appendiculata circumvolans

Background: Among the hymenopteran insect venoms, those from social wasps and bees - such as honeybee, hornets and paper wasps - have been well documented. Their venoms are composed of a number of peptides and proteins and used for defending their nests and themselves from predators. In contrast, the venoms of solitary wasps and bees have not been the object of further research. In case of solitary bees, only major peptide components in a few venoms have been addressed. Therefore, the aim of the present study was to explore the peptide component profile of the venom from the solitary bee Xylocopa appendiculata circumvolans by peptidomic analysis with using LC-MS. Methods: A reverse-phase HPLC connected to ESI-OrbiTrap MS was used for LC-MS. On-line mass fingerprinting was made from TIC, and data-dependent tandem mass spectrometry gave MSMS spectra. A major peptide component was isolated by reverse-phase HPLC by conventional way, and its sequence was determined by Edman degradation, which was finally corroborated by solid phase synthesis. Using the synthetic specimen, biological activities (antimicrobial activity, mast cell devaluation, hemolysis, leishmanicidal activity) and pore formation in artificial lipid bilayer were evaluated. Results: On-line mass fingerprinting revealed that the crude venom contained 124 components. MS/MS analysis gave 75 full sequences of the peptide components. Most of these are related to the major and novel peptide, xylopin. Its sequence, GFVALLKKLPLILKHLH-NH2, has characteristic features of linear cationic α-helical peptides; rich in hydrophobic and basic amino acids with no disulfide bond, and accordingly, it can be predicted to adopt an amphipathic α-helix secondary structure. In biological evaluation, xylopin exhibited broad-spectrum antimicrobial activity, and moderate mast cell degranulation and leishmanicidal activities, but showed virtually no hemolytic activity. Additionally, the peptide was able to incorporate pores in artificial lipid bilayers of azolectin, confirming the mechanism of the cytolytic activity by pore formation in biological membranes. Conclusions: LC-ESI-MS and MS/MS analysis of the crude venom extract from a solitary bee Xylocopa appendiculata circumvolans revealed that the component profile of this venom mostly consisted of small peptides. The major peptide components, xylopin and xylopinin, were purified and characterized in a conventional manner. Their chemical and biological characteristics, belonging to linear cationic α-helical peptides, are similar to the known solitary bee venom peptides, melectin and osmin. Pore formation in artificial lipid bilayers was demonstrated for the first time with a solitary bee peptide.(AU)

Isolation of biologically active peptides from the venom of Japanese carpenter bee, Xylocopa appendiculata

Background Mass spectrometry-guided venom peptide profiling is a powerful tool to explore novel substances from venomous animals in a highly sensitive manner. In this study, this peptide profiling approach is successfully applied to explore the venom peptides of a Japanese solitary carpenter bee, Xylocopa appendiculata (Hymenoptera: Apoidea: Apidae: Anthophila: Xylocopinae: Xylocopini). Although interesting biological effects of the crude venom of carpenter bees have been reported, the structure and biological function of the venom peptides have not been elucidated yet. Methods The venom peptide profiling of the crude venom of X. appendiculata was performed by matrix-assisted laser desorption/ionization-time of flight mass spectroscopy. The venom was purified by a reverse-phase HPLC. The purified peptides were subjected to the Edman degradation, MS/MS analysis, and/or molecular cloning methods for peptide sequencing. Biological and functional characterization was performed by circular dichroism analysis, liposome leakage assay, and antimicrobial, histamine releasing and hemolytic activity tests. Results Three novel peptides with m/z 16508, 1939.3, and 1900.3 were isolated from the venom of X. appendiculata. The peptide with m/z 16508 was characterized as a secretory phospholipase A2 (PLA2) homolog in which the characteristic cysteine residues as well as the active site residues found in bee PLA2s are highly conserved. Two novel peptides with m/z 1939.3 and m/z 1900.3 were named as Xac-1 and Xac-2, respectively. These peptides are found to be amphiphilic and displayed antimicrobial and hemolytic activities. The potency was almost the same as that of mastoparan isolated from the wasp venom. Conclusion We found three novel biologically active peptides in the venom of X. appendiculata and analyzed their molecular functions, and compared their sequential homology to discuss their molecular diversity. Highly sensitive mass analysis plays an important role in this study.(AU)

Isolation of biologically active peptides from the venom of Japanese carpenter bee, Xylocopa appendiculata

Abstract Background Mass spectrometry-guided venom peptide profiling is a powerful tool to explore novel substances from venomous animals in a highly sensitive manner. In this study, this peptide profiling approach is successfully applied to explore the venom peptides of a Japanese solitary carpenter bee, Xylocopa appendiculata (Hymenoptera: Apoidea: Apidae: Anthophila: Xylocopinae: Xylocopini). Although interesting biological effects of the crude venom of carpenter bees have been reported, the structure and biological function of the venom peptides have not been elucidated yet. Methods The venom peptide profiling of the crude venom of X. appendiculata was performed by matrix-assisted laser desorption/ionization-time of flight mass spectroscopy. The venom was purified by a reverse-phase HPLC. The purified peptides were subjected to the Edman degradation, MS/MS analysis, and/or molecular cloning methods for peptide sequencing. Biological and functional characterization was performed by circular dichroism analysis, liposome leakage assay, and antimicrobial, histamine releasing and hemolytic activity tests. Results Three novel peptides with m/z 16508, 1939.3, and 1900.3 were isolated from the venom of X. appendiculata. The peptide with m/z 16508 was characterized as a secretory phospholipase A2 (PLA2) homolog in which the characteristic cysteine residues as well as the active site residues found in bee PLA2s are highly conserved. Two novel peptides with m/z 1939.3 and m/z 1900.3 were named as Xac-1 and Xac-2, respectively. These peptides are found to be amphiphilic and displayed antimicrobial and hemolytic activities. The potency was almost the same as that of mastoparan isolated from the wasp venom. Conclusion We found three novel biologically active peptides in the venom of X. appendiculata and analyzed their molecular functions, and compared their sequential homology to discuss their molecular diversity. Highly sensitive mass analysis plays an important role in this study.

Peptidomic analysis of the venom of the solitary bee Xylocopa appendiculata circumvolans

Abstract Background: Among the hymenopteran insect venoms, those from social wasps and bees - such as honeybee, hornets and paper wasps - have been well documented. Their venoms are composed of a number of peptides and proteins and used for defending their nests and themselves from predators. In contrast, the venoms of solitary wasps and bees have not been the object of further research. In case of solitary bees, only major peptide components in a few venoms have been addressed. Therefore, the aim of the present study was to explore the peptide component profile of the venom from the solitary bee Xylocopa appendiculata circumvolans by peptidomic analysis with using LC-MS. Methods: A reverse-phase HPLC connected to ESI-OrbiTrap MS was used for LC-MS. On-line mass fingerprinting was made from TIC, and data-dependent tandem mass spectrometry gave MSMS spectra. A major peptide component was isolated by reverse-phase HPLC by conventional way, and its sequence was determined by Edman degradation, which was finally corroborated by solid phase synthesis. Using the synthetic specimen, biological activities (antimicrobial activity, mast cell devaluation, hemolysis, leishmanicidal activity) and pore formation in artificial lipid bilayer were evaluated. Results: On-line mass fingerprinting revealed that the crude venom contained 124 components. MS/MS analysis gave 75 full sequences of the peptide components. Most of these are related to the major and novel peptide, xylopin. Its sequence, GFVALLKKLPLILKHLH-NH2, has characteristic features of linear cationic -helical peptides; rich in hydrophobic and basic amino acids with no disulfide bond, and accordingly, it can be predicted to adopt an amphipathic -helix secondary structure. In biological evaluation, xylopin exhibited broad-spectrum antimicrobial activity, and moderate mast cell degranulation and leishmanicidal activities, but showed virtually no hemolytic activity. Additionally, the peptide was able to incorporate pores in artificial lipid bilayers of azolectin, confirming the mechanism of the cytolytic activity by pore formation in biological membranes. Conclusions: LC-ESI-MS and MS/MS analysis of the crude venom extract from a solitary bee Xylocopa appendiculata circumvolans revealed that the component profile of this venom mostly consisted of small peptides. The major peptide components, xylopin and xylopinin, were purified and characterized in a conventional manner. Their chemical and biological characteristics, belonging to linear cationic -helical peptides, are similar to the known solitary bee venom peptides, melectin and osmin. Pore formation in artificial lipid bilayers was demonstrated for the first time with a solitary bee peptide.