title: Requirement of a mip-like gene for virulence in the phytopathogenic bacterium Xanthomonas campestris pv. campestris.
abstract: Macrophage infectivity potentiators (Mips) are FKBP domain-containing proteins reported as virulence factors in several human pathogens, such as members of genera Legionella, Salmonella and Chlamydia. The putative peptidylprolyl cis-trans isomerase (PPIase) encoded by XC2699 of the plant bacterial pathogen Xanthomonas campestris pv. campestris 8004 exhibits a 49% similarity at the amino-acid level to the Mip protein of Legionella pneumophila. This mip-like gene, XC2699, was overexpressed in Escherichia coli and the purified (His)6-tagged Mip-like protein encoded by XC2699 exhibited a PPIase activity specifically inhibited by FK-506. A mutation in the mip-like gene XC2699 led to significant reductions in virulence and replication capacity in the host plant Chinese radish (Raphanus sativus L. var. radiculus Pers.). Furthermore, the production of exopolysaccharide and the activity of extracellular proteases, virulence factors of X. campestris pv. campestris, were significantly decreased in the mip-like mutant. These results reveal that the mip-like gene is involved in the pathogenesis of X. campestris pv. campestris through an effect on the production of these virulence factors.
authors.affiliation: College of Agriculture and Biotechnology, Zhejiang University, Hangzhou 310029, China.
authors.forename: Ning
authors.initials: N
authors.lastname: Zang
authors.forename: Dong-Jie
authors.initials: DJ
authors.lastname: Tang
authors.forename: Mei-Liang
authors.initials: ML
authors.lastname: Wei
authors.forename: Yong-Qiang
authors.initials: YQ
authors.lastname: He
authors.forename: Baoshan
authors.initials: B
authors.lastname: Chen
authors.forename: Jia-Xun
authors.initials: JX
authors.lastname: Feng
authors.forename: Jing
authors.initials: J
authors.lastname: Xu
authors.forename: Yong-Qi
authors.initials: YQ
authors.lastname: Gan
authors.forename: Bo-Le
authors.initials: BL
authors.lastname: Jiang
authors.forename: Ji-Liang
authors.initials: JL
authors.lastname: Tang
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D016572:Cyclosporine / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D008070:Lipopolysaccharides / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation; D010447:Peptide Hydrolases / Q000378:metabolism; D019696:Peptidylprolyl Isomerase / Q000235:genetics* / Q000378:metabolism; D019897:Periplasm / Q000201:enzymology; D010935:Plant Diseases / Q000382:microbiology; D011994:Recombinant Proteins / Q000378:metabolism; D016415:Sequence Alignment; D016559:Tacrolimus / Q000494:pharmacology; D013997:Time Factors; D014774:Virulence / Q000235:genetics; D037521:Virulence Factors / Q000235:genetics / Q000378:metabolism; D016959:Xanthomonas campestris / Q000235:genetics* / Q000378:metabolism / Q000472:pathogenicity
chemical_list: D001426:Bacterial Proteins; D008070:Lipopolysaccharides; D011994:Recombinant Proteins; D037521:Virulence Factors; D016572:Cyclosporine; D010447:Peptide Hydrolases; C519620:XC2699 protein, Xanthomonas campestris; C512922:Mip protein, Legionella pneumophila; D019696:Peptidylprolyl Isomerase; D016559:Tacrolimus