Proteomic and Phenotypic Analyses of a Putative YggS Family Pyridoxal Phosphate-Dependent Enzyme in Acidovorax citrulli

Abstract

<i>Acidovorax citrulli</i> (<i>Ac</i>) is a phytopathogenic bacterium that causes bacterial fruit blotch (BFB) in cucurbit crops, including watermelon. However, there are no effective methods to control this disease. YggS family pyridoxal phosphate-dependent enzyme acts as a coenzyme in all transamination reactions, but its function in <i>Ac</i> is poorly understood. Therefore, this study uses proteomic and phenotypic analyses to characterize the functions. The <i>Ac</i> strain lacking the YggS family pyridoxal phosphate-dependent enzyme, <i>AcΔyppAc</i>(EV), virulence was wholly eradicated in geminated seed inoculation and leaf infiltration. <i>AcΔyppAc</i>(EV) propagation was inhibited when exposed to L-homoserine but not pyridoxine. Wild-type and mutant growth were comparable in the liquid media but not in the solid media in the minimal condition. The comparative proteomic analysis revealed that YppAc is primarily involved in cell motility and wall/membrane/envelop biogenesis. In addition, <i>AcΔyppAc</i>(EV) reduced biofilm formation and twitching halo production, indicating that YppAc is involved in various cellular mechanisms and possesses pleiotropic effects. Therefore, this identified protein is a potential target for developing an efficient anti-virulence reagent to control BFB.