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

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 Esperalba, Miguel Fernández-Huerta, Margot P. Scheffer, Jaume Pinyol, Achilleas S. Frangakis, Maria Lluch-Senar, Shigetarou Mori, Keigo Shibayama, Tsuyoshi Kenri, Takayuki Kato, Keiichi Namba, Ignacio Fita, Makoto Miyata () and David Aparicio ()
Additional contact information
David Vizarraga: Instituto de Biología Molecular de Barcelona (IBMB-CSIC)
Akihiro Kawamoto: 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
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
Keiichi Namba: Osaka University
Ignacio Fita: Instituto de Biología Molecular de Barcelona (IBMB-CSIC)
Makoto Miyata: Osaka City University
David Aparicio: Instituto de Biología Molecular de Barcelona (IBMB-CSIC)

Nature Communications, 2020, vol. 11, issue 1, 1-16

Abstract: 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.

Date: 2020
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18777-y

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DOI: 10.1038/s41467-020-18777-y

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