Study of the role of GroEL protein from Leptospira spp. in the host-pathogen Interaction
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Tipo de documento: | Dissertação |
Idioma: | eng |
Título da fonte: | Biblioteca Digital de Teses e Dissertações da USP |
Texto Completo: | https://www.teses.usp.br/teses/disponiveis/10/10134/tde-16032022-080751/ |
Resumo: | Background: Leptospirosis is a zoonotic disease caused by infection with spirochetes from Leptospira genus. It has been classified into at least 17 pathogenic species, with more than 250 serologic variants. This wide distribution may be a result of leptospiral ability to colonize the renal tubules of mammalian hosts, including humans, wildlife, and many domesticated animals. Previous studies showed that the expression of proteins belonging to the microbial heat shock protein (HSP) family is upregulated during infection and also during various stress stimuli. Several proteins of this family are known to have important roles in the infectious processes in other bacteria, but the role of HSPs in Leptospira spp. is poorly understood. In this study, we have evaluated the capacity of the protein GroEL, a member of HSP family, of interacting with host proteins and of stimulating the production of cytokines by macrophages. Results: The binding experiments demonstrated that the recombinant GroEL protein showed interaction with several host components in a dose-dependent manner. It was also observed that GroEL is a surface protein, and it is secreted extracellularly. Moreover, two cytokines (tumor necrosis factor-α and interleukin-6) were produced when macrophages cells were stimulated with this protein. Conclusions: Our findings showed that GroEL protein may contribute to the adhesion of leptospires to host tissues and stimulate the production of proinflammatory cytokines during infection. These features might indicate an important role of GroEL in the pathogen-host interaction in the leptospirosis. |
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Study of the role of GroEL protein from Leptospira spp. in the host-pathogen InteractionEstudo do papel da proteína GroEL de Leptospira spp. na interação patógeno-hospedeiroLeptospiraChaperona 60Chaperonin 60GroELGroELLeptospiraLeptospiroseLeptospirosisMoonlighting proteinProteína MoonlightingBackground: Leptospirosis is a zoonotic disease caused by infection with spirochetes from Leptospira genus. It has been classified into at least 17 pathogenic species, with more than 250 serologic variants. This wide distribution may be a result of leptospiral ability to colonize the renal tubules of mammalian hosts, including humans, wildlife, and many domesticated animals. Previous studies showed that the expression of proteins belonging to the microbial heat shock protein (HSP) family is upregulated during infection and also during various stress stimuli. Several proteins of this family are known to have important roles in the infectious processes in other bacteria, but the role of HSPs in Leptospira spp. is poorly understood. In this study, we have evaluated the capacity of the protein GroEL, a member of HSP family, of interacting with host proteins and of stimulating the production of cytokines by macrophages. Results: The binding experiments demonstrated that the recombinant GroEL protein showed interaction with several host components in a dose-dependent manner. It was also observed that GroEL is a surface protein, and it is secreted extracellularly. Moreover, two cytokines (tumor necrosis factor-α and interleukin-6) were produced when macrophages cells were stimulated with this protein. Conclusions: Our findings showed that GroEL protein may contribute to the adhesion of leptospires to host tissues and stimulate the production of proinflammatory cytokines during infection. These features might indicate an important role of GroEL in the pathogen-host interaction in the leptospirosis.Introdução: Leptospirose é uma zoonose causada pela infecção com espiroquetas do gênero Leptospira. O genêro foi classificado em pelo menos 17 espécies patogênicas, com mais de 250 variantes sorológicas. Esta distribuição abrangente pode ser um resultado da habilidade das leptospiras de colonizar os túbulos renais de hospedeiros mamíferos, incluindo humanos, animais silvestres e muitos animais domésticos. Estudos anteriores mostraram que a expressão de proteínas da família Heat Shock Protein (HSP) é produzida em maior quantidade durante o processo de infecção e também durante estímulos de estresse. Muitas proteínas dessa família são conhecidas por apresentar importante função no processo infeccioso em outras bacterias, mas o papel de HSPs em Leptospira spp. ainda é pouco conhecido. Neste estudo, avaliamos a capacidade da proteína GroEL, membro da família HSP, de interagir com proteínas do hospedeiro e estimular a produção de citocinas por macrófagos. Resultados: Os experimentos de adesão demonstraram que a proteína recombinante GroEL apresenta interação com componentes do hospedeiro na condição dose-dependente. Também foi observado que a GroEL é uma proteína de superfície e é secretada para o meio extracelular. Adicionalmente, duas citocinas (tumor necrosis factor-α e interleukin-6) foram produzidas quando macrófagos foram estimulados com a proteína em questão. Conclusões: Nossos resultados mostraram que a proteína GroEL pode contribuir para a adesão de leptospiras em tecidos do hospedeiro e estimular a produção de citocinas pró-inflamatórias durante a infecção. Essas características podem indicar um importante papel da proteína GroEL na interação patógeno-hospedeiro na leptospirose.Biblioteca Digitais de Teses e Dissertações da USPAniz, Patricia Antonia Estima Abreu deHo, Joana Dias2021-08-10info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisapplication/pdfhttps://www.teses.usp.br/teses/disponiveis/10/10134/tde-16032022-080751/reponame:Biblioteca Digital de Teses e Dissertações da USPinstname:Universidade de São Paulo (USP)instacron:USPLiberar o conteúdo para acesso público.info:eu-repo/semantics/openAccesseng2024-08-15T19:12:02Zoai:teses.usp.br:tde-16032022-080751Biblioteca Digital de Teses e Dissertaçõeshttp://www.teses.usp.br/PUBhttp://www.teses.usp.br/cgi-bin/mtd2br.plvirginia@if.usp.br|| atendimento@aguia.usp.br||virginia@if.usp.bropendoar:27212024-08-15T19:12:02Biblioteca Digital de Teses e Dissertações da USP - Universidade de São Paulo (USP)false |
dc.title.none.fl_str_mv |
Study of the role of GroEL protein from Leptospira spp. in the host-pathogen Interaction Estudo do papel da proteína GroEL de Leptospira spp. na interação patógeno-hospedeiro |
title |
Study of the role of GroEL protein from Leptospira spp. in the host-pathogen Interaction |
spellingShingle |
Study of the role of GroEL protein from Leptospira spp. in the host-pathogen Interaction Ho, Joana Dias Leptospira Chaperona 60 Chaperonin 60 GroEL GroEL Leptospira Leptospirose Leptospirosis Moonlighting protein Proteína Moonlighting |
title_short |
Study of the role of GroEL protein from Leptospira spp. in the host-pathogen Interaction |
title_full |
Study of the role of GroEL protein from Leptospira spp. in the host-pathogen Interaction |
title_fullStr |
Study of the role of GroEL protein from Leptospira spp. in the host-pathogen Interaction |
title_full_unstemmed |
Study of the role of GroEL protein from Leptospira spp. in the host-pathogen Interaction |
title_sort |
Study of the role of GroEL protein from Leptospira spp. in the host-pathogen Interaction |
author |
Ho, Joana Dias |
author_facet |
Ho, Joana Dias |
author_role |
author |
dc.contributor.none.fl_str_mv |
Aniz, Patricia Antonia Estima Abreu de |
dc.contributor.author.fl_str_mv |
Ho, Joana Dias |
dc.subject.por.fl_str_mv |
Leptospira Chaperona 60 Chaperonin 60 GroEL GroEL Leptospira Leptospirose Leptospirosis Moonlighting protein Proteína Moonlighting |
topic |
Leptospira Chaperona 60 Chaperonin 60 GroEL GroEL Leptospira Leptospirose Leptospirosis Moonlighting protein Proteína Moonlighting |
description |
Background: Leptospirosis is a zoonotic disease caused by infection with spirochetes from Leptospira genus. It has been classified into at least 17 pathogenic species, with more than 250 serologic variants. This wide distribution may be a result of leptospiral ability to colonize the renal tubules of mammalian hosts, including humans, wildlife, and many domesticated animals. Previous studies showed that the expression of proteins belonging to the microbial heat shock protein (HSP) family is upregulated during infection and also during various stress stimuli. Several proteins of this family are known to have important roles in the infectious processes in other bacteria, but the role of HSPs in Leptospira spp. is poorly understood. In this study, we have evaluated the capacity of the protein GroEL, a member of HSP family, of interacting with host proteins and of stimulating the production of cytokines by macrophages. Results: The binding experiments demonstrated that the recombinant GroEL protein showed interaction with several host components in a dose-dependent manner. It was also observed that GroEL is a surface protein, and it is secreted extracellularly. Moreover, two cytokines (tumor necrosis factor-α and interleukin-6) were produced when macrophages cells were stimulated with this protein. Conclusions: Our findings showed that GroEL protein may contribute to the adhesion of leptospires to host tissues and stimulate the production of proinflammatory cytokines during infection. These features might indicate an important role of GroEL in the pathogen-host interaction in the leptospirosis. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-08-10 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/masterThesis |
format |
masterThesis |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
https://www.teses.usp.br/teses/disponiveis/10/10134/tde-16032022-080751/ |
url |
https://www.teses.usp.br/teses/disponiveis/10/10134/tde-16032022-080751/ |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
|
dc.rights.driver.fl_str_mv |
Liberar o conteúdo para acesso público. info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
Liberar o conteúdo para acesso público. |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.coverage.none.fl_str_mv |
|
dc.publisher.none.fl_str_mv |
Biblioteca Digitais de Teses e Dissertações da USP |
publisher.none.fl_str_mv |
Biblioteca Digitais de Teses e Dissertações da USP |
dc.source.none.fl_str_mv |
reponame:Biblioteca Digital de Teses e Dissertações da USP instname:Universidade de São Paulo (USP) instacron:USP |
instname_str |
Universidade de São Paulo (USP) |
instacron_str |
USP |
institution |
USP |
reponame_str |
Biblioteca Digital de Teses e Dissertações da USP |
collection |
Biblioteca Digital de Teses e Dissertações da USP |
repository.name.fl_str_mv |
Biblioteca Digital de Teses e Dissertações da USP - Universidade de São Paulo (USP) |
repository.mail.fl_str_mv |
virginia@if.usp.br|| atendimento@aguia.usp.br||virginia@if.usp.br |
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1809090763850514432 |