Effect of interactions between Mip and PrtA on the full extracellular protease activity of Xanthomonas campestris pathovar campestris

Abstract Mip (macrophage infectivity potentiator) and Mip-like proteins have been demonstrated to be involved in virulence of several animal pathogens, but as yet none of their native bacterial targets has been identified. Our previous work demonstrated that the Mip-like protein found in the plant p...

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Bibliographic Details
Published in:FEMS microbiology letters 2011-10, Vol.323 (2), p.180-187
Main Authors: Meng, Qing-Lin, Tang, Dong-Jie, Fan, Ying-Yuan, Li, Zhen-Jiang, Zhang, Hui, He, Yong-Qiang, Jiang, Bo-Le, Lu, Guang-Tao, Tang, Ji-Liang
Format: Article
Language:English
Subjects:
Bacterial plant pathogens
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Bacteriology
Biological and medical sciences
Blotting, Far-Western
Blotting, Western
Deactivation
Exopolysaccharides
extracellular protease
Fundamental and applied biological sciences. Psychology
Gene Knockout Techniques
Genomes
Inactivation
Infectivity
Macrophages
Microbiology
mip‐like
Miscellaneous
Pathogens
Peptide Hydrolases - genetics
Peptide Hydrolases - metabolism
Periplasm
periplasmic PPIase
Periplasmic Proteins - genetics
Periplasmic Proteins - metabolism
Phytopathology. Animal pests. Plant and forest protection
Protease
Protein Binding
Protein Interaction Mapping
Proteins
Proteolysis
PrtA
Secretion
Serine
Serine proteinase
Target recognition
Two-Hybrid System Techniques
Virulence
Virulence Factors - genetics
Virulence Factors - metabolism
Western blotting
Xanthomonas
Xanthomonas campestris
Xanthomonas campestris - enzymology
Xanthomonas campestris - genetics
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Summary:Abstract Mip (macrophage infectivity potentiator) and Mip-like proteins have been demonstrated to be involved in virulence of several animal pathogens, but as yet none of their native bacterial targets has been identified. Our previous work demonstrated that the Mip-like protein found in the plant pathogen anthomonas campestris pv. campestris ( ) (hereafter called MipXcc) is also involved in virulence. Inactivation of the gene leads to a significant reduction in exopolysaccharide production and extracellular protease activity via an unknown mechanism. The genome encodes six extracellular proteases, all of which are secreted via the type II secretion system. The serine protease PrtA makes the largest contribution to 's total extracellular proteolytic activity. In this study, Western blotting analysis demonstrated that MipXcc was located in the periplasm. Bacterial two-hybrid and far-Western analysis indicated that MipXcc interacted with PrtA directly. Purified MipXcc was found to be able to rescue the protease activity of periplasmic proteins extracted from the mutant. These findings show that MipXcc plays a role in the maturation of PrtA, which is the novel native target for at least one Mip or Mip-like protein.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.2011.02377.x