Gingipains as a virulence factor in the oral cavity
Autor(a) principal: | |
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Data de Publicação: | 2012 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.14/35508 |
Resumo: | Aim: The objective of this study is to demonstrate the molecular action of Porphyromonas gingivalis cysteine proteases such as gingipains (R1, R2 and K) upon human molecules. Materials and methods: Using the information on protein structure and function available in international databases (UniProtKB and Merops Database), the molecular interactions already described between gingipains and host molecules were clarified. Results: Possible cleavage sites were identified in host-produced elastase inhibitors and in pro-Matrix MetalloProteinase (MMP)1. Analysis of the results leads to the suggestion that the elastase inhibitor alpha1-antitrypsin is also degraded by interpain A, a cystein protease of Prevotella intermedia sharing a high homology with the PrtT and periodontain of P. gingivalis. Conclusion: The information obtained suggests a synergistic molecular mechanism by which cysteine proteases of different bacteria can be responsible for the clinical manifestations of periodontal disease, and illustrates the use of bioinformatics to establish and predict molecular mechanisms. |
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Gingipains as a virulence factor in the oral cavityGingipains como fatores de virulência na cavidade oralBioinformaticsElastasePeriodontitisPorphyromonas gingivalisProteasesPeriodontiteBioinformáticaElastaseAim: The objective of this study is to demonstrate the molecular action of Porphyromonas gingivalis cysteine proteases such as gingipains (R1, R2 and K) upon human molecules. Materials and methods: Using the information on protein structure and function available in international databases (UniProtKB and Merops Database), the molecular interactions already described between gingipains and host molecules were clarified. Results: Possible cleavage sites were identified in host-produced elastase inhibitors and in pro-Matrix MetalloProteinase (MMP)1. Analysis of the results leads to the suggestion that the elastase inhibitor alpha1-antitrypsin is also degraded by interpain A, a cystein protease of Prevotella intermedia sharing a high homology with the PrtT and periodontain of P. gingivalis. Conclusion: The information obtained suggests a synergistic molecular mechanism by which cysteine proteases of different bacteria can be responsible for the clinical manifestations of periodontal disease, and illustrates the use of bioinformatics to establish and predict molecular mechanisms.Objetivo: O objetivo deste trabalho é verificar o detalhe molecular da ação de proteases de cisteína de Porphyromonas gingivalis como as gingipains (R1, R2 e K) em moléculas do hospedeiro. Material e métodos: Utilizando a informação disponível sobre estrutura e função de proteínas nas bases de dados internacionais (UniProtKB e Merops Database) as interações já descritas entre gingipains e moléculas do hospedeiro são clarificadas. Resultados: São identificados possíveis locais de corte das gingipains em inibidores naturais das elastases e a identificação molecular de um local de corte na pro MetaloProteinase da Matriz (MMP) 1. A análise dos resultados sugere que a interpain A, uma protease de cisteína de Prevotella intermedia com elevada homologia estrutural com as proteases de cisteína PrtT e periodontain de P. gingivalis, também degrada o inibidor de elastases, alfa1antitripsina. Conclusão Com a integração da informação obtida, sugere-se um possível mecanismo molecular da sinergia criada entre proteinases de cisteína no sentido de promover a doença periodontal. Este estudo ilustra a forma como as ferramentas bioinformáticas podem ser úteis no esclarecimento dos mecanismos moleculares e na previsão de resultados experimentais, melhorando o desenho de estudos laboratoriais.Veritati - Repositório Institucional da Universidade Católica PortuguesaLopes, Pedro CamposBarros, MarleneCorreia, Maria José2021-10-12T13:50:55Z2012-102012-10-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.14/35508eng1646-289010.1016/j.rpemd.2012.07.00284870239265info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-12T17:41:02Zoai:repositorio.ucp.pt:10400.14/35508Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:28:50.416010Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Gingipains as a virulence factor in the oral cavity Gingipains como fatores de virulência na cavidade oral |
title |
Gingipains as a virulence factor in the oral cavity |
spellingShingle |
Gingipains as a virulence factor in the oral cavity Lopes, Pedro Campos Bioinformatics Elastase Periodontitis Porphyromonas gingivalis Proteases Periodontite Bioinformática Elastase |
title_short |
Gingipains as a virulence factor in the oral cavity |
title_full |
Gingipains as a virulence factor in the oral cavity |
title_fullStr |
Gingipains as a virulence factor in the oral cavity |
title_full_unstemmed |
Gingipains as a virulence factor in the oral cavity |
title_sort |
Gingipains as a virulence factor in the oral cavity |
author |
Lopes, Pedro Campos |
author_facet |
Lopes, Pedro Campos Barros, Marlene Correia, Maria José |
author_role |
author |
author2 |
Barros, Marlene Correia, Maria José |
author2_role |
author author |
dc.contributor.none.fl_str_mv |
Veritati - Repositório Institucional da Universidade Católica Portuguesa |
dc.contributor.author.fl_str_mv |
Lopes, Pedro Campos Barros, Marlene Correia, Maria José |
dc.subject.por.fl_str_mv |
Bioinformatics Elastase Periodontitis Porphyromonas gingivalis Proteases Periodontite Bioinformática Elastase |
topic |
Bioinformatics Elastase Periodontitis Porphyromonas gingivalis Proteases Periodontite Bioinformática Elastase |
description |
Aim: The objective of this study is to demonstrate the molecular action of Porphyromonas gingivalis cysteine proteases such as gingipains (R1, R2 and K) upon human molecules. Materials and methods: Using the information on protein structure and function available in international databases (UniProtKB and Merops Database), the molecular interactions already described between gingipains and host molecules were clarified. Results: Possible cleavage sites were identified in host-produced elastase inhibitors and in pro-Matrix MetalloProteinase (MMP)1. Analysis of the results leads to the suggestion that the elastase inhibitor alpha1-antitrypsin is also degraded by interpain A, a cystein protease of Prevotella intermedia sharing a high homology with the PrtT and periodontain of P. gingivalis. Conclusion: The information obtained suggests a synergistic molecular mechanism by which cysteine proteases of different bacteria can be responsible for the clinical manifestations of periodontal disease, and illustrates the use of bioinformatics to establish and predict molecular mechanisms. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-10 2012-10-01T00:00:00Z 2021-10-12T13:50:55Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10400.14/35508 |
url |
http://hdl.handle.net/10400.14/35508 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
1646-2890 10.1016/j.rpemd.2012.07.002 84870239265 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
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1799132007703248896 |