Título:	Proteomic mapping of multifunctional complexes within Triatomine saliva
Autor(es):	Santiago, Paula Beatriz Charneau, Sébastien Mandacaru, Samuel Coelho Bentes, Kaio Luís da Silva Bastos, Izabela Marques Dourado Sousa, Marcelo Valle de Ricart, Carlos André Ornelas Araújo, Carla Nunes de Santana, Jaime Martins
Assunto:	Chagas, Doença de Triatomíneos Proteínas salivares Espectrometria de massa
Data de publicação:	2-Set-2020
Editora:	Frontiers
Referência:	SANTIAGO, Paula Beatriz et al. Proteomic mapping of multifunctional complexes within Triatomine saliva. Frontiers Cellular and Infection Microbiology, [S.l.], v. 10, art. 459, 02 set. 2020. DOI: https://doi.org/10.3389/fcimb.2020.00459. Disponível em: https://www.frontiersin.org/articles/10.3389/fcimb.2020.00459/full. Acesso em: 20 dez. 2021.
Abstract:	Triatomines 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.
Licença:	Copyright © 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.
DOI:	https://doi.org/10.3389/fcimb.2020.00459
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