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TitleImmunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 5188, Year 2020
Publish dateOct 14, 2020
AuthorsDavid 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 / David Aparicio /
PubMed AbstractMycoplasma 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 ...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.
External linksNat Commun / PubMed:33057023 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.94 - 3.1 Å
Structure data

30233

7bwm

EMDB-30233, PDB-7bwm:
Cryo-EM structure of the human pathogen Mycoplasma pneumoniae P1
Method: EM (single particle) / Resolution: 2.9 Å

PDB-6rc9:
P1 Mycoplasma pneumoniae
Method: X-RAY DIFFRACTION / Resolution: 1.94 Å

PDB-6rj1:
N-Domain P40/P90 Mycoplasma pneumoniae
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

PDB-6tlz:
N-Domain P40/P90 Mycoplasma pneumoniae complexed with 3'SL
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-6tm0:
N-Domain P40/P90 Mycoplasma pneumoniae complexed with 6'SL
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-HOH:
WATER / Water

ChemComp-SIA:
N-acetyl-alpha-neuraminic acid / Sialic acid

Source
  • mycoplasma pneumoniae m129 (bacteria)
  • mycoplasma pneumoniae (strain atcc 29342 / m129) (bacteria)
KeywordsCELL ADHESION / adhesin / extracellular / transmembrane-complex / immunodominant protein. / Adhesion / Sugars / STRUCTURAL PROTEIN / Sialic acid receptor

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