Proteomic analysis of the venom of the predatory ant Pachycondyla striata (Hymenoptera: Formicidae)

Detalhes bibliográficos
Autor(a) principal: Santos, Pollyanna Pereira
Data de Publicação: 2017
Outros Autores: Games, Patricia Dias, Azevedo, Dihego Oliveira, Barros, Edvaldo, Oliveira, Leandro Licursi de, Ramos, Humberto Josué de Oliveira, Baracat-Pereira, Maria Cristina, Serrão, José Eduardo
Tipo de documento: Artigo
Idioma: eng
Título da fonte: LOCUS Repositório Institucional da UFV
Texto Completo: http://dx.doi.org/10.1002/arch.21424
http://www.locus.ufv.br/handle/123456789/16509
Resumo: The ants use their venom for predation, defense, and communication. The venom of these insects is rich in peptides and proteins, and compared with other animal venoms, ant venoms remain poorly explored. The objective of this study was to evaluate the protein content of the venom in the Ponerinae ant Pachycondyla striata. Venom samples were collected by manual gland reservoir dissection, and samples were submitted to two-dimensional gel electrophoresis and separation by ion-exchange and reverse-phase high-performance liquid chromatography followed by mass spectrometry using tanden matrix-assisted laser desorption/ionization with time-of-flight (MALDI-TOF/TOF) mass spectrometry and electrospray ionization-quadrupole with time-of-flight (ESI-Q/TOF) mass spectrometry for obtaining amino acid sequence. Spectra obtained were searched against the NCBInr and SwissProt database. Additional analysis was performed using PEAKS Studio 7.0 (Sequencing de novo). The venom of P. striata has a complex mixture of proteins from which 43 were identified. Within the identified proteins are classical venom proteins (phospholipase A, hyaluronidase, and aminopeptidase N), allergenic proteins (different venom allergens), and bioactive peptides (U10-ctenitoxin Pn1a). Venom allergens are among the most expressed proteins, suggesting that P. striata venom has high allergenic potential. This study discusses the possible functions of the proteins identified in the venom of P. striata.
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spelling Santos, Pollyanna PereiraGames, Patricia DiasAzevedo, Dihego OliveiraBarros, EdvaldoOliveira, Leandro Licursi deRamos, Humberto Josué de OliveiraBaracat-Pereira, Maria CristinaSerrão, José Eduardo2018-01-18T16:27:57Z2018-01-18T16:27:57Z2017-10-101520-6327http://dx.doi.org/10.1002/arch.21424http://www.locus.ufv.br/handle/123456789/16509The ants use their venom for predation, defense, and communication. The venom of these insects is rich in peptides and proteins, and compared with other animal venoms, ant venoms remain poorly explored. The objective of this study was to evaluate the protein content of the venom in the Ponerinae ant Pachycondyla striata. Venom samples were collected by manual gland reservoir dissection, and samples were submitted to two-dimensional gel electrophoresis and separation by ion-exchange and reverse-phase high-performance liquid chromatography followed by mass spectrometry using tanden matrix-assisted laser desorption/ionization with time-of-flight (MALDI-TOF/TOF) mass spectrometry and electrospray ionization-quadrupole with time-of-flight (ESI-Q/TOF) mass spectrometry for obtaining amino acid sequence. Spectra obtained were searched against the NCBInr and SwissProt database. Additional analysis was performed using PEAKS Studio 7.0 (Sequencing de novo). The venom of P. striata has a complex mixture of proteins from which 43 were identified. Within the identified proteins are classical venom proteins (phospholipase A, hyaluronidase, and aminopeptidase N), allergenic proteins (different venom allergens), and bioactive peptides (U10-ctenitoxin Pn1a). Venom allergens are among the most expressed proteins, suggesting that P. striata venom has high allergenic potential. 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dc.title.en.fl_str_mv Proteomic analysis of the venom of the predatory ant Pachycondyla striata (Hymenoptera: Formicidae)
title Proteomic analysis of the venom of the predatory ant Pachycondyla striata (Hymenoptera: Formicidae)
spellingShingle Proteomic analysis of the venom of the predatory ant Pachycondyla striata (Hymenoptera: Formicidae)
Santos, Pollyanna Pereira
MALDI-TOF/TOF
Peptides
Proteins
Q-TOF
Toxin
Venom
title_short Proteomic analysis of the venom of the predatory ant Pachycondyla striata (Hymenoptera: Formicidae)
title_full Proteomic analysis of the venom of the predatory ant Pachycondyla striata (Hymenoptera: Formicidae)
title_fullStr Proteomic analysis of the venom of the predatory ant Pachycondyla striata (Hymenoptera: Formicidae)
title_full_unstemmed Proteomic analysis of the venom of the predatory ant Pachycondyla striata (Hymenoptera: Formicidae)
title_sort Proteomic analysis of the venom of the predatory ant Pachycondyla striata (Hymenoptera: Formicidae)
author Santos, Pollyanna Pereira
author_facet Santos, Pollyanna Pereira
Games, Patricia Dias
Azevedo, Dihego Oliveira
Barros, Edvaldo
Oliveira, Leandro Licursi de
Ramos, Humberto Josué de Oliveira
Baracat-Pereira, Maria Cristina
Serrão, José Eduardo
author_role author
author2 Games, Patricia Dias
Azevedo, Dihego Oliveira
Barros, Edvaldo
Oliveira, Leandro Licursi de
Ramos, Humberto Josué de Oliveira
Baracat-Pereira, Maria Cristina
Serrão, José Eduardo
author2_role author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Santos, Pollyanna Pereira
Games, Patricia Dias
Azevedo, Dihego Oliveira
Barros, Edvaldo
Oliveira, Leandro Licursi de
Ramos, Humberto Josué de Oliveira
Baracat-Pereira, Maria Cristina
Serrão, José Eduardo
dc.subject.pt-BR.fl_str_mv MALDI-TOF/TOF
Peptides
Proteins
Q-TOF
Toxin
Venom
topic MALDI-TOF/TOF
Peptides
Proteins
Q-TOF
Toxin
Venom
description The ants use their venom for predation, defense, and communication. The venom of these insects is rich in peptides and proteins, and compared with other animal venoms, ant venoms remain poorly explored. The objective of this study was to evaluate the protein content of the venom in the Ponerinae ant Pachycondyla striata. Venom samples were collected by manual gland reservoir dissection, and samples were submitted to two-dimensional gel electrophoresis and separation by ion-exchange and reverse-phase high-performance liquid chromatography followed by mass spectrometry using tanden matrix-assisted laser desorption/ionization with time-of-flight (MALDI-TOF/TOF) mass spectrometry and electrospray ionization-quadrupole with time-of-flight (ESI-Q/TOF) mass spectrometry for obtaining amino acid sequence. Spectra obtained were searched against the NCBInr and SwissProt database. Additional analysis was performed using PEAKS Studio 7.0 (Sequencing de novo). The venom of P. striata has a complex mixture of proteins from which 43 were identified. Within the identified proteins are classical venom proteins (phospholipase A, hyaluronidase, and aminopeptidase N), allergenic proteins (different venom allergens), and bioactive peptides (U10-ctenitoxin Pn1a). Venom allergens are among the most expressed proteins, suggesting that P. striata venom has high allergenic potential. This study discusses the possible functions of the proteins identified in the venom of P. striata.
publishDate 2017
dc.date.issued.fl_str_mv 2017-10-10
dc.date.accessioned.fl_str_mv 2018-01-18T16:27:57Z
dc.date.available.fl_str_mv 2018-01-18T16:27:57Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1002/arch.21424
http://www.locus.ufv.br/handle/123456789/16509
dc.identifier.issn.none.fl_str_mv 1520-6327
identifier_str_mv 1520-6327
url http://dx.doi.org/10.1002/arch.21424
http://www.locus.ufv.br/handle/123456789/16509
dc.language.iso.fl_str_mv eng
language eng
dc.relation.ispartofseries.pt-BR.fl_str_mv 96(3), e21424, Nov. 2017
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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dc.publisher.none.fl_str_mv Archives of Insect Biochemistry and Physiology
publisher.none.fl_str_mv Archives of Insect Biochemistry and Physiology
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