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Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae

Author

Listed:
  • David Vizarraga

    (Instituto de Biología Molecular de Barcelona (IBMB-CSIC))

  • Akihiro Kawamoto

    (Osaka University
    Osaka University)

  • U. Matsumoto

    (Osaka City University)

  • Ramiro Illanes

    (Instituto de Biología Molecular de Barcelona (IBMB-CSIC))

  • Rosa Pérez-Luque

    (Instituto de Biología Molecular de Barcelona (IBMB-CSIC))

  • Jesús Martín

    (Instituto de Biología Molecular de Barcelona (IBMB-CSIC))

  • Rocco Mazzolini

    (The Barcelona Institute of Science and Technology)

  • Paula Bierge

    (Universitat Autònoma de Barcelona)

  • Oscar Q. Pich

    (Universitat Autònoma de Barcelona
    Universitat Autònoma de Barcelona)

  • Mateu Espasa

    (Universitat Autònoma de Barcelona)

  • Isabel Sanfeliu

    (Universitat Autònoma de Barcelona)

  • Juliana Esperalba

    (Universitat Autònoma de Barcelona)

  • Miguel Fernández-Huerta

    (Universitat Autònoma de Barcelona)

  • Margot P. Scheffer

    (Buchmann Institute for Molecular Life Sciences)

  • Jaume Pinyol

    (Universitat Autònoma de Barcelona)

  • Achilleas S. Frangakis

    (Buchmann Institute for Molecular Life Sciences)

  • Maria Lluch-Senar

    (The Barcelona Institute of Science and Technology)

  • Shigetarou Mori

    (National Institute of Infectious Diseases)

  • Keigo Shibayama

    (National Institute of Infectious Diseases)

  • Tsuyoshi Kenri

    (National Institute of Infectious Diseases)

  • Takayuki Kato

    (Osaka University
    Osaka University)

  • Keiichi Namba

    (Osaka University
    RIKEN Center for Biosystems Dynamics Research and SPring-8 Center
    Osaka University)

  • Ignacio Fita

    (Instituto de Biología Molecular de Barcelona (IBMB-CSIC))

  • Makoto Miyata

    (Osaka City University
    Osaka City University)

  • David Aparicio

    (Instituto de Biología Molecular de Barcelona (IBMB-CSIC))

Abstract

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.

Suggested Citation

  • David Vizarraga & Akihiro Kawamoto & U. Matsumoto & Ramiro Illanes & Rosa Pérez-Luque & Jesús Martín & Rocco Mazzolini & Paula Bierge & Oscar Q. Pich & Mateu Espasa & Isabel Sanfeliu & Juliana Esperal, 2020. "Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae," Nature Communications, Nature, vol. 11(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18777-y
    DOI: 10.1038/s41467-020-18777-y
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