Summary
Ralstonia solanacearum
, one of the most destructive plant bacterial pathogens, delivers an array of effector proteins via its type III secretion system for pathogenesis. However, the biochemical functions of most of these proteins remain unclear. RipN is a type III effector with unknown function(s) from the pathogen
R. solanacearum
. Here, we demonstrate that RipN is a conserved type III effector found within the
R. solanacearum
species complex that contains a putative Nudix hydrolase domain and has ADPâribose/NADH pyrophosphorylase activity
in vitro
. Further analysis shows that RipN localizes to the endoplasmic reticulum (ER) and nucleus in
Nicotiana tabacum
leaf cells and Arabidopsis protoplasts, and truncation of the Câterminus of RipN results in a loss of nuclear and ER targeting. Furthermore, the expression of RipN in
Arabidopsis
suppresses callose deposition and the transcription of pathogenâassociated molecular pattern (PAMP)âtriggered immunity (PTI) marker genes under flg22 treatment, and promotes bacterial growth
in planta
. In addition, the expression of RipN in plant cells alters NADH/NAD
+
, but not GSH/GSSG, ratios, and its Nudix hydrolase activity is indispensable for such biochemical function. These results suggest that RipN acts as a Nudix hydrolase, alters the NADH/NAD
+
ratio of the plant and contributes to
R. solanacearum
virulence by suppression of PTI of the host.