The translocation of type III effectors of plant-pathogenic bacteria is required both for the expression of their role in virulence, and for the triggering of plant defenses. The effector translocation needs molecular associations between bacterial translocators and their recognition compounds situated in plant plasma membranes. We show here that rice aquaporin PIP1;3, a member of the plasma membrane intrinsic protein family, is implicated in translocation of a transcription activator-like (TAL) effector from the bacterial blight pathogen into the cytosol of rice cells. The TAL protein PthXo1 targets rice disease-susceptible gene SWEET11 to determine virulence of the bacterial strain PXO99A on susceptible rice ... More
The translocation of type III effectors of plant-pathogenic bacteria is required both for the expression of their role in virulence, and for the triggering of plant defenses. The effector translocation needs molecular associations between bacterial translocators and their recognition compounds situated in plant plasma membranes. We show here that rice aquaporin PIP1;3, a member of the plasma membrane intrinsic protein family, is implicated in translocation of a transcription activator-like (TAL) effector from the bacterial blight pathogen into the cytosol of rice cells. The TAL protein PthXo1 targets rice disease-susceptible gene SWEET11 to determine virulence of the bacterial strain PXO99A on susceptible rice variety Nipponbare. In Nipponbare, post-transcriptional gene silencing of PIP1;3 results in highly alleviated susceptibility and concomitantly decreased expression of SWEET11 as compared to levels of the bacterial virulence and the plant SWEET11 expression in the wild-type plant with normal transcription of PIP1;3. In coincidence, the efficiency in PthXo1 translocation is substantially reduced in PIP1;3-silenced rice lines in contrast to the wild-type plant. In the case of PIP1;3 silencing, moreover, the bacterial type III translocator Hpa1 loses the ability to mediate PthXo1 translocation from the bacterial cells into the cytosol of rice cells. By contrast, PIP1;3 silencing does not affect the performance of isolated Hpa1 as a pattern molecule to induce immune responses in rice. Our data suggest that rice aquaporin PIP1;3 is a candidate of disease-susceptible factor with functional relevance to PthXo1 translocation as a prerequisite of the bacterial virulence on the susceptible rice variety.
