Mycoplasma pneumoniae and Mycoplasma genitalium are closely related organisms that cause distinct clinical manifestations and possess different tissue predilections despite their high degree of genome homology. We reported earlier that surface-localized M. pneumoniae elongation factor Tu (EF-Tu Mp) mediates binding to the extracellular matrix component fibronectin (Fn) through the carboxyl region of EF-Tu. In this study, we demonstrate that surface-associated M. genitalium EF-Tu (EF-TuMg), in spite of sharing 96% identity with EF-TuMp, does not bind Fn. We utilized this finding to identify the essential amino acids of EF-Tu Mp that mediate Fn interactions by generating modified recombinant EF-Tu proteins with amino acid changes corresponding to those of EF-Tu Mg. Amino acid changes in serine 343, proline 345, and threonine 357 were sufficient to significantly reduce the Fn binding of EF-TuMp. Synthetic peptides corresponding to this region of EF-TuMp (EF-TuMp 340-358) blocked both recombinant EF-TuMp and radiolabeled M. pneumoniae cell binding to Fn. In contrast, EF-TuMg 340-358 peptides exhibited minimal blocking activity, reinforcing the specificity of EF-Tu-Fn interactions as mediators of microbial colonization and tissue tropism.
ASJC Scopus subject areas
- Infectious Diseases