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

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.

Vizarraga, D., Kawamoto, A., Matsumoto, U. et al. Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae. Nat Commun 11, 5188 (2020). https://doi.org/10.1038/s41467-020-18777-y

nature communications

A phase-contrast immunofluorescence microscopy image (left) and three-dimensionally printed model of M. pneumoniae cells (right). The positions of the attachment organelle and the Nap structure are indicated. The cell surface is partly modeled as a transparent canopy to show the internal core structure of the organelle. The arrow indicates gliding direction.