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 Quijada 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; David Aparicio Alarcón

doi:10.1038/s41467-020-18777-y

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 Quijada 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 KenriTakayuki Kato, Keiichi Namba, Ignacio Fita, Makoto Miyata, David Aparicio Alarcón

Institute of Biotechnology and Biomedicine "Vicent Villar Palasi" (IBB)

Research output: Contribution to journal › Article › Research › peer-review

27 Citations (Scopus)

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.

Original language	English
Journal	Nature Communications
Volume	11
DOIs	https://doi.org/10.1038/s41467-020-18777-y
Publication status	Published - 2020

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10.1038/s41467-020-18777-y

https://ddd.uab.cat/record/252986

Mecanismos de virulencia y regulación en células mínimas: diseño de vacunas contra algunas especies de micoplasmas de interés
Yaguana Navarrete, J. A. (Collaborator), Perez Pons, J. A. (Investigator), Sánchez Alba, L. (Collaborator), Marcos Silva, M. (Collaborator), Piñol Ribas, J. (Principal Investigator), Querol Murillo, E. (Principal Investigator 2), Quijada Pich, O. (Collaborator) & Mozo-Villarías, A. (Investigator)
Spanish Ministry of Economy and Competitiveness (MINECO)
1/01/18 → 30/09/21
Project: Research Projects and Other Grants

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Vizarraga, D., Kawamoto, A., Matsumoto, U., Illanes, R., Pérez-Luque, R., Martín, J., Mazzolini, R., Bierge, P., Quijada Pich, O., Espasa, M., Sanfeliu, I., Esperalba, J., Fernández-Huerta, M., Scheffer, M. P., Pinyol, J., Frangakis, A. S., Lluch Senar, M., Mori, S., Shibayama, K., ... Aparicio Alarcón, D. (2020). Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae. Nature Communications, 11. https://doi.org/10.1038/s41467-020-18777-y

@article{fd84a2dc2a49425eaacc830a4084b407,

title = "Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae",

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.",

author = "David Vizarraga and Akihiro Kawamoto and U. Matsumoto and Ramiro Illanes and Rosa P{\'e}rez-Luque and Jes{\'u}s Mart{\'i}n and Rocco Mazzolini and Paula Bierge and {Quijada Pich}, Oscar and Mateu Espasa and Isabel Sanfeliu and Juliana Esperalba and Miguel Fern{\'a}ndez-Huerta and Scheffer, {Margot P.} and Jaume Pinyol and Frangakis, {Achilleas S.} and {Lluch Senar}, Maria and Shigetarou Mori and Keigo Shibayama and Tsuyoshi Kenri and Takayuki Kato and Keiichi Namba and Ignacio Fita and Makoto Miyata and {Aparicio Alarc{\'o}n}, David",

year = "2020",

doi = "10.1038/s41467-020-18777-y",

language = "English",

volume = "11",

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Vizarraga, D, Kawamoto, A, Matsumoto, U, Illanes, R, Pérez-Luque, R, Martín, J, Mazzolini, R, Bierge, P, Quijada Pich, O, Espasa, M, Sanfeliu, I, Esperalba, J, Fernández-Huerta, M, Scheffer, MP, Pinyol, J, Frangakis, AS, Lluch Senar, M, Mori, S, Shibayama, K, Kenri, T, Kato, T, Namba, K, Fita, I, Miyata, M & Aparicio Alarcón, D 2020, 'Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae', Nature Communications, vol. 11. https://doi.org/10.1038/s41467-020-18777-y

TY - JOUR

T1 - Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae

AU - Vizarraga, David

AU - Kawamoto, Akihiro

AU - Matsumoto, U.

AU - Illanes, Ramiro

AU - Pérez-Luque, Rosa

AU - Martín, Jesús

AU - Mazzolini, Rocco

AU - Bierge, Paula

AU - Quijada Pich, Oscar

AU - Espasa, Mateu

AU - Sanfeliu, Isabel

AU - Esperalba, Juliana

AU - Fernández-Huerta, Miguel

AU - Scheffer, Margot P.

AU - Pinyol, Jaume

AU - Frangakis, Achilleas S.

AU - Lluch Senar, Maria

AU - Mori, Shigetarou

AU - Shibayama, Keigo

AU - Kenri, Tsuyoshi

AU - Kato, Takayuki

AU - Namba, Keiichi

AU - Fita, Ignacio

AU - Miyata, Makoto

AU - Aparicio Alarcón, David

PY - 2020

Y1 - 2020

N2 - 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.

AB - 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.

U2 - 10.1038/s41467-020-18777-y

DO - 10.1038/s41467-020-18777-y

M3 - Article

C2 - 33057023

SN - 2041-1723

VL - 11

JO - Nature Communications

JF - Nature Communications

ER -

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

Abstract

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Mecanismos de virulencia y regulación en células mínimas: diseño de vacunas contra algunas especies de micoplasmas de interés

Cite this