AI Article Synopsis
- Mycoplasma pneumoniae is a bacteria that causes atypical pneumonia, with its motility and infectivity linked to proteins P1 and P40/P90, which form an adhesion complex.
- The study determined the structures of P1 and P40/P90 using advanced techniques, revealing that the binding site for sialic acid is actually in P40/P90, not P1 as previously thought.
- Antibodies against the conserved portion of P1 showed potential in inhibiting the bacteria's adhesion, and findings suggest opportunities for developing new vaccines against M. pneumoniae infections.
Article 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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7560827 | PMC |
| http://dx.doi.org/10.1038/s41467-020-18777-y | DOI Listing |
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