Proteomic mapping of multifunctional complexes within Triatomine saliva

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Autor(es): dc.creatorSantiago, Paula Beatriz-
Autor(es): dc.creatorCharneau, Sébastien-
Autor(es): dc.creatorMandacaru, Samuel Coelho-
Autor(es): dc.creatorBentes, Kaio Luís da Silva-
Autor(es): dc.creatorBastos, Izabela Marques Dourado-
Autor(es): dc.creatorSousa, Marcelo Valle de-
Autor(es): dc.creatorRicart, Carlos André Ornelas-
Autor(es): dc.creatorAraújo, Carla Nunes de-
Autor(es): dc.creatorSantana, Jaime Martins-
Data de aceite: dc.date.accessioned2024-10-23T16:13:01Z-
Data de disponibilização: dc.date.available2024-10-23T16:13:01Z-
Data de envio: dc.date.issued2021-12-19-
Data de envio: dc.date.issued2021-12-19-
Data de envio: dc.date.issued2020-09-02-
Fonte completa do material: dc.identifierhttps://repositorio.unb.br/handle/10482/42593-
Fonte completa do material: dc.identifierhttps://doi.org/10.3389/fcimb.2020.00459-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/902728-
Descrição: dc.descriptionTriatomines are hematophagous insects that transmit Trypanosoma cruzi, the etiological agent of Chagas disease. This neglected tropical disease represents a global health issue as it is spreading worldwide. The saliva of Triatominae contains miscellaneous proteins crucial for blood feeding acquisition, counteracting host's hemostasis while performing vasodilatory, anti-platelet and anti-coagulant activities, besides modulating inflammation and immune responses. Since a set of biological processes are mediated by protein complexes, here, the sialocomplexomes (salivary protein complexes) of five species of Triatominae were studied to explore the protein-protein interaction networks. Salivary multiprotein complexes from Triatoma infestans, Triatoma dimidiata, Dipetalogaster maxima, Rhodnius prolixus, and Rhodnius neglectus were investigated by Blue-Native- polyacrylamide gel electrophoresis coupled with liquid chromatography tandem mass spectrometry. More than 70 protein groups, uncovering the landscape of the Triatominae salivary interactome, were revealed. Triabin, actin, thioredoxin peroxidase and an uncharacterized protein were identified in sialocomplexes of the five species, while hexamerin, heat shock protein and histone were identified in sialocomplexes of four species. Salivary proteins related to triatomine immunity as well as those required during blood feeding process such as apyrases, antigen 5, procalins, and nitrophorins compose different complexes. Furthermore, unique proteins for each triatomine species were revealed. This study represents the first Triatominae sialocomplexome reference to date and shows that the approach used is a reliable tool for the analysis of Triatominae salivary proteins assembled into complexes.-
Formato: dc.formatapplication/pdf-
Publicador: dc.publisherFrontiers-
Direitos: dc.rightsAcesso Aberto-
Direitos: dc.rightsCopyright © 2020 Santiago, Charneau, Mandacaru, Bentes, Bastos, de Sousa, Ricart, de Araújo and Santana. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.-
Palavras-chave: dc.subjectChagas, Doença de-
Palavras-chave: dc.subjectTriatomíneos-
Palavras-chave: dc.subjectProteínas salivares-
Palavras-chave: dc.subjectEspectrometria de massa-
Título: dc.titleProteomic mapping of multifunctional complexes within Triatomine saliva-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional – UNB

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