Your browser doesn't support javascript.
loading
Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae.
Vizarraga, David; Kawamoto, Akihiro; Matsumoto, U; Illanes, Ramiro; Pérez-Luque, Rosa; Martín, Jesús; Mazzolini, Rocco; Bierge, Paula; Pich, Oscar Q; Espasa, Mateu; Sanfeliu, Isabel; Esperalba, Juliana; Fernández-Huerta, Miguel; Scheffer, Margot P; Pinyol, Jaume; Frangakis, Achilleas S; Lluch-Senar, Maria; Mori, Shigetarou; Shibayama, Keigo; Kenri, Tsuyoshi; Kato, Takayuki; Namba, Keiichi; Fita, Ignacio; Miyata, Makoto; Aparicio, David.
Afiliación
  • Vizarraga D; Instituto de Biología Molecular de Barcelona (IBMB-CSIC), Parc Científic de Barcelona, Baldiri Reixac 10, 08028, Barcelona, Spain.
  • Kawamoto A; Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka, 565-0871, Japan.
  • Matsumoto U; Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
  • Illanes R; Graduate School of Science, Osaka City University, Osaka, 558-8585, Japan.
  • Pérez-Luque R; Instituto de Biología Molecular de Barcelona (IBMB-CSIC), Parc Científic de Barcelona, Baldiri Reixac 10, 08028, Barcelona, Spain.
  • Martín J; Instituto de Biología Molecular de Barcelona (IBMB-CSIC), Parc Científic de Barcelona, Baldiri Reixac 10, 08028, Barcelona, Spain.
  • Mazzolini R; Instituto de Biología Molecular de Barcelona (IBMB-CSIC), Parc Científic de Barcelona, Baldiri Reixac 10, 08028, Barcelona, Spain.
  • Bierge P; EMBL/CRG Systems Biology Research Unit, Centre for Genomic Regulation (CRG), The Barcelona Institute of Science and Technology, Dr Aiguader 88, 08003, Barcelona, Spain.
  • Pich OQ; Laboratori de Recerca en Microbiologia i Malalties Infeccioses, Institut d'Investigació i Innovació Parc Taulí (I3PT), Hospital Universitari Parc Taulí, Universitat Autònoma de Barcelona, 08208, Sabadell, Spain.
  • Espasa M; Laboratori de Recerca en Microbiologia i Malalties Infeccioses, Institut d'Investigació i Innovació Parc Taulí (I3PT), Hospital Universitari Parc Taulí, Universitat Autònoma de Barcelona, 08208, Sabadell, Spain.
  • Sanfeliu I; Departament de Bioquímica i Biologia Molecular, Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, 08193, Bellaterra, Barcelona, Spain.
  • Esperalba J; Departament de Microbiologia, Hospital Universitari Parc Taulí, Universitat Autònoma de Barcelona, 08208, Sabadell, Spain.
  • Fernández-Huerta M; Departament de Microbiologia, Hospital Universitari Parc Taulí, Universitat Autònoma de Barcelona, 08208, Sabadell, Spain.
  • Scheffer MP; Departament de Microbiologia, Hospital Universitari Vall d´Hebron, Universitat Autònoma de Barcelona, 08035, Barcelona, Spain.
  • Pinyol J; Departament de Microbiologia, Hospital Universitari Vall d´Hebron, Universitat Autònoma de Barcelona, 08035, Barcelona, Spain.
  • Frangakis AS; Buchmann Institute for Molecular Life Sciences, Max-von-Laue Str. 15, 60438, Frankfurt, Germany.
  • Lluch-Senar M; Departament de Bioquímica i Biologia Molecular, Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, 08193, Bellaterra, Barcelona, Spain.
  • Mori S; Buchmann Institute for Molecular Life Sciences, Max-von-Laue Str. 15, 60438, Frankfurt, Germany.
  • Shibayama K; EMBL/CRG Systems Biology Research Unit, Centre for Genomic Regulation (CRG), The Barcelona Institute of Science and Technology, Dr Aiguader 88, 08003, Barcelona, Spain.
  • Kenri T; Department of Bacteriology II, National Institute of Infectious Diseases, Tokyo, Japan.
  • Kato T; Department of Bacteriology II, National Institute of Infectious Diseases, Tokyo, Japan.
  • Namba K; Department of Bacteriology II, National Institute of Infectious Diseases, Tokyo, Japan.
  • Fita I; Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka, 565-0871, Japan.
  • Miyata M; Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
  • Aparicio D; Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Nat Commun ; 11(1): 5188, 2020 10 14.
Article en En | MEDLINE | ID: mdl-33057023
Mycoplasma pneumoniae is a bacterial human pathogen that causes primary atypical pneumonia. M. pneumoniae motility and infectivity are mediated by the immunodominant proteins P1 and P40/P90, which form a transmembrane adhesion complex. Here we report the structure of P1, determined by X-ray crystallography and cryo-electron microscopy, and the X-ray structure of P40/P90. Contrary to what had been suggested, the binding site for sialic acid was found in P40/P90 and not in P1. Genetic and clinical variability concentrates on the N-terminal domain surfaces of P1 and P40/P90. Polyclonal antibodies generated against the mostly conserved C-terminal domain of P1 inhibited adhesion of M. pneumoniae, and serology assays with sera from infected patients were positive when tested against this C-terminal domain. P40/P90 also showed strong reactivity against human infected sera. The architectural elements determined for P1 and P40/P90 open new possibilities in vaccine development against M. pneumoniae infections.
Asunto(s)
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Neumonía por Mycoplasma / Adhesión Bacteriana / Adhesinas Bacterianas / Mycoplasma pneumoniae Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2020 Tipo del documento: Article País de afiliación: España Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Neumonía por Mycoplasma / Adhesión Bacteriana / Adhesinas Bacterianas / Mycoplasma pneumoniae Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2020 Tipo del documento: Article País de afiliación: España Pais de publicación: Reino Unido