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Novel protein interactions with an actin homolog (MreB) of Helicobacter pylori determined by bacterial two-hybrid system.
Zepeda Gurrola, Reyna Cristina; Fu, Yajuan; Rodríguez Luna, Isabel Cristina; Benítez Cardoza, Claudia Guadalupe; López López, María de Jesús; López Vidal, Yolanda; Gutíerrez, Germán Rubén Aguilar; Rodríguez Pérez, Mario A; Guo, Xianwu.
Afiliação
  • Zepeda Gurrola RC; Centro de Biotecnología Genómica, Instituto Politécnico Nacional, Cd. Reynosa Tamaulipas, Mexico.
  • Fu Y; Centro de Biotecnología Genómica, Instituto Politécnico Nacional, Cd. Reynosa Tamaulipas, Mexico.
  • Rodríguez Luna IC; Centro de Biotecnología Genómica, Instituto Politécnico Nacional, Cd. Reynosa Tamaulipas, Mexico.
  • Benítez Cardoza CG; Escuela Nacional de Medicina y Homeopatía, Instituto Politécnico Nacional, Guillermo Massieu Helguera, México, D.F., Mexico.
  • López López MJ; Centro de Biotecnología Genómica, Instituto Politécnico Nacional, Cd. Reynosa Tamaulipas, Mexico.
  • López Vidal Y; Facultad de Medicina, División de Investigación, Universidad Nacional Autónoma de Mexico.
  • Gutíerrez GRA; Centro de Investigación sobre Enfermedades Infecciosas, Instituto Nacional de Salud Pública, Cuernavaca, Morelos, Mexico.
  • Rodríguez Pérez MA; Centro de Biotecnología Genómica, Instituto Politécnico Nacional, Cd. Reynosa Tamaulipas, Mexico.
  • Guo X; Centro de Biotecnología Genómica, Instituto Politécnico Nacional, Cd. Reynosa Tamaulipas, Mexico. Electronic address: xguo@ipn.mx.
Microbiol Res ; 201: 39-45, 2017 Aug.
Article em En | MEDLINE | ID: mdl-28602400
The bacterium Helicobacter pylori infects more than 50% of the world population and causes several gastroduodenal diseases, including gastric cancer. Nevertheless, we still need to explore some protein interactions that may be involved in pathogenesis. MreB, an actin homolog, showed some special characteristics in previous studies, indicating that it could have different functions. Protein functions could be realized via protein-protein interactions. In the present study, the MreB protein from H. pylori 26695 fused with two tags 10×His and GST in tandem was overexpressed and purified from Escherchia coli. The purified recombinant protein was used to perform a pull-down assay with H. pylori 26695 cell lysate. The pulled-down proteins were identified by mass spectrometry (MALDI-TOF), in which the known important proteins related to morphogenesis were absent but several proteins related to pathogenesis process were observed. The bacterial two-hybrid system was further used to evaluate the protein interactions and showed that new interactions of MreB respectively with VacA, UreB, HydB, HylB and AddA were confirmed but the interaction MreB-MreC was not validated. These results indicated that the protein MreB in H. pylori has a distinct interactome, does not participate in cell morphogenesis via MreB-MreC but could be related to pathogenesis.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Helicobacter pylori / Actinas / Técnicas do Sistema de Duplo-Híbrido / Domínios e Motivos de Interação entre Proteínas Tipo de estudo: Prognostic_studies Idioma: En Revista: Microbiol Res Assunto da revista: MICROBIOLOGIA / SAUDE AMBIENTAL Ano de publicação: 2017 Tipo de documento: Article País de afiliação: México País de publicação: Alemanha
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Helicobacter pylori / Actinas / Técnicas do Sistema de Duplo-Híbrido / Domínios e Motivos de Interação entre Proteínas Tipo de estudo: Prognostic_studies Idioma: En Revista: Microbiol Res Assunto da revista: MICROBIOLOGIA / SAUDE AMBIENTAL Ano de publicação: 2017 Tipo de documento: Article País de afiliação: México País de publicação: Alemanha