Increased Motility in and Changes in Its Virulence, Fitness, and Morphology Following Protein Expression on Ribosomes with Altered RsmA Methylation.

Infection with is the major cause of human gastroenteritis in the United States and Europe, leading to debilitating autoimmune sequelae in many cases. While considerable progress has been made in detailing the infectious cycle of , a full understanding of the molecular mechanisms responsible for virulence remains to be elucidated. Here, we apply a novel approach by modulating protein expression on the pathogen's ribosomes by inactivating a highly conserved rRNA methyltransferase. Loss of the RsmA methyltransferase results in a more motile strain with greater adhesive and cell-invasive properties. These phenotypical effects correlate with enhanced expression of specific proteins related to flagellar formation and function, together with enzymes involved in cell wall/membrane and amino acid synthesis. Despite the enhancement of certain virulent traits, the null strain grows poorly on minimal media and is rapidly out-competed by the wild-type strain. Complementation with an active copy of the gene rescues most of the traits changed in the mutant. However, the complemented strain overexpresses and displays new flaws, including loss of the spiral cell shape, which is distinctive for . Proteins linked with altered virulence and morphology are identified here by mass spectrometry proteomic analyses of the strains.