A J domain virulence effector of Pseudomonas syringae remodels host chloroplasts and suppresses defenses

Background: The plant pathogen Pseudomonas syringae injects 20-40 different proteins called effectors into host plant cells, yet the functions and sites of action of these effectors in promoting pathogenesis are largely unknown. Plants in turn defend themselves against P. syringae by activating the salicylic acid (SA)-mediated signaling pathway. The P. syringae-specific Hopl1 effector has a putative chloroplast-targeting sequence and a J domain. J domains function by activating 70 kDa heat-shock proteins (Hsp70). Results: Hopl1 is a ubiquitous P. syringae virulence effector that acts inside plant cells. When expressed in plants, Hopl1 localizes to chloroplasts, the site of SA synthesis. Hopi1 causes chloroplast thylakoid structure remodeling and suppresses SA accumulation. Hopi1's C terminus has bona fide J domain activity that is necessary for Hopi1 -mediated virulence and thylakoid remodeling. Furthermore, Hopi1-expressing plants have increased heat tolerance, establishing that Hopi1 can engage the plant stress-response machinery. Conclusions: These results strongly suggest that chloroplast Hsp70 is targeted by the P. syringae Hopi1 effector to promote bacterial virulence by suppressing plant defenses. The targeting of Hsp70 function through J domain proteins is known to occur in a mammalian virus, SV40. However, this is the first example of a bacterial pathogen exploiting a J domain protein to promote pathogenesis through alterations of chloroplast structure and function.