Open AccessThe bifunctional effector AvrXccC of Xanthomonas campestris pv. campestris requires plasma membrane‐anchoring for host recognition
Author(s) -
WANG LIFENG,
TANG XIAOYAN,
HE CHAOZU
Publication year - 2007
Publication title -
molecular plant pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.945
H-Index - 103
eISSN - 1364-3703
pISSN - 1464-6722
DOI - 10.1111/j.1364-3703.2007.00409.x
Subject(s) - xanthomonas campestris , biology , effector , xanthomonas campestris pv. campestris , host (biology) , microbiology and biotechnology , anchoring , xanthomonas , bacteria , genetics , structural engineering , engineering
SUMMARY Bacterial pathogens use type III secretion systems (TTSS) to deliver effector proteins into eukaryotic cells for pathogenesis. In bacterial–plant interactions, one effector may function as an avirulence factor to betray the pathogen to the plant surveillance system and induce the hypersensitive response (HR) in the resistant host carrying a corresponding resistance ( R ) gene. However, the same effector can also sustain the growth of the pathogen by acting as a virulence factor to modulate plant physiology in the susceptible host lacking the corresponding R gene. Here, we identified and characterized a bifunctional TTSS effector AvrXccC belonging to the AvrB effector family in Xanthomonas campestris pv. campestris 8004. This effector is required for full bacterial virulence in the susceptible host cabbage ( Brassica oleracea ) and avirulence in the resistant host mustard ( Brassica napiformis L.H. Baily). Expressing avrXccC in mustard‐virulent strain Xcc HRI 3849A converts its virulence to avirulence. The effector AvrXccC is anchored to the plant plasma membrane, and the N‐terminal myristoylation site (amino acids 2–7: GLcaSK) is essential for its localization. In addition, the avirulence function of AvrXccC for host recognition depends on its plasma membrane localization. Promoter activity assays showed that the expression of avrXccC is hrpG/hrpX ‐dependent. Moreover, the secretion of AvrXccC displayed hrp ‐dependency and the core sequence for AvrXccC translocation was defined to the N‐terminal 40 amino acids.