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

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

Journal Nat. Commun. 11:5188 (2020)
Title Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae
Laboratory JEOL YOKOGUSHI Research Alliance Laboratories〈SA Prof. NAMBA Keiichi〉
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.

Fig.
Three views, 90° apart from each other, of the Nap surface depicting the sialic acid compound 3SL (spheres in red and sky blue) bound to the binding site of the two P40/P90 subunits of a Nap.

Authors

David Vizarraga (1), Akihiro Kawamoto (2, 3), U. Matsumoto (4), Ramiro Illanes (1), Rosa Pérez-Luque (1), Jesús Martín (1), Rocco Mazzolini (5), Paula Bierge (6), Oscar Q. Pich (6, 7), Mateu Espasa (8), Isabel Sanfeliu (8), Juliana Esperalba (9), Miguel Fernández-Huerta (9), Margot P. Scheffer (10), Jaume Pinyol (7), Achilleas S. Frangakis (10), Maria Lluch-Senar (5), Shigetarou Mori (11), Keigo Shibayama (11), Tsuyoshi Kenri (11), Takayuki Kato (2, 3), Keiichi Namba (2, 12, 13), Ignacio Fita, Makoto Miyata (4, 14), David Aparicio (1)

  1. Instituto de Biología Molecular de Barcelona (IBMB-CSIC), Parc Científic de Barcelona, Baldiri Reixac 10, 08028, Barcelona, Spain.
  2. Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka, 565-0871, Japan.
  3. Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
  4. Graduate School of Science, Osaka City University, Osaka, 558-8585, Japan.
  5. EMBL/CRG Systems Biology Research Unit, Centre for Genomic Regulation (CRG), The Barcelona Institute of Science and Technology, Dr Aiguader 88, 08003, Barcelona, Spain.
  6. 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.
  7. Departament de Bioquímica i Biologia Molecular, Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, 08193, Bellaterra, Barcelona, Spain.
  8. Departament de Microbiologia, Hospital Universitari Parc Taulí, Universitat Autònoma de Barcelona, 08208, Sabadell, Spain.
  9. Departament de Microbiologia, Hospital Universitari Vall d´Hebron, Universitat Autònoma de Barcelona, 08035, Barcelona, Spain.
  10. Buchmann Institute for Molecular Life Sciences, Max-von-Laue Str. 15, 60438, Frankfurt, Germany.
  11. Department of Bacteriology II, National Institute of Infectious Diseases, Tokyo, Japan.
  12. RIKEN Center for Biosystems Dynamics Research and SPring-8 Center, 1-3 Yamadaoka, Suita, Osaka, 565-0871, Japan.
  13. JEOL YOKOGUSHI Research Alliance Laboratories, Osaka University, 1-3 Yamadaoka, Suita, Osaka, 565-0871, Japan.
  14. The OCU Advanced Research Institute for Natural Science and Technology (OCARINA), Osaka City University, Osaka, 558-8585, Japan.
PubMed 33057023

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