6RJ1

N-Domain P40/P90 Mycoplasma pneumoniae

Summary for 6RJ1

• Entry DOI: 10.2210/pdb6rj1/pdb
• Descriptor: Mgp-operon protein 3 (2 entities in total)
• Functional Keywords: adhesion, extracellular, sugars, cell adhesion
• Biological source: Mycoplasma pneumoniae (strain ATCC 29342 / M129)
• Total number of polymer chains: 2
• Total formula weight: 208647.20

Authors

Vizarraga, D.,Aparicio, D.,Illanes, R.,Fita, I. (deposition date: 2019-04-25, release date: 2020-11-04, Last modification date: 2024-01-24)

Primary citation

Vizarraga, D.,Kawamoto, A.,Matsumoto, U.,Illanes, R.,Perez-Luque, R.,Martin, J.,Mazzolini, R.,Bierge, P.,Pich, O.Q.,Espasa, M.,Sanfeliu, I.,Esperalba, J.,Fernandez-Huerta, M.,Scheffer, M.P.,Pinyol, J.,Frangakis, A.S.,Lluch-Senar, M.,Mori, S.,Shibayama, K.,Kenri, T.,Kato, T.,Namba, K.,Fita, I.,Miyata, M.,Aparicio, D.
Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae.
Nat Commun, 11:5188-5188, 2020

PubMed 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.

PubMed: 33057023
DOI: 10.1038/s41467-020-18777-y

Experimental method

X-RAY DIFFRACTION (2.65 Å)