Amino acid changes in elongation factor Tu of Mycoplasma pneumoniae and Mycoplasma genitalium influence fibronectin binding.

ABSTRACT: 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-Tu(Mg)), in spite of sharing 96% identity with EF-Tu(Mp), 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

SUBMITTER: Balasubramanian S 

PROVIDER: S-EPMC2738037 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature