Extracellular proteases from Xanthomonas campestris pv. campestris, the black rot pathogen

Dow, J. Maxwell; Clarke, Belinda; Milligan, D. E.; Tang, Ji‐Liang; Daniels, Michael J.

doi:10.1128/aem.56.10.2994-2998.1990

Cited by 95 publications

(42 citation statements)

References 14 publications

(13 reference statements)

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“…This enzyme is responsible for almost all extracellular protease activity of Xcc strain 8004. Inactivation of prtA leads to almost complete loss of extracellular protease activity (Tang et al, 1987;Dow et al, 1990;Barber et al, 1997). In our previous article, we speculated that the expression of extracellular protease genes may be affected by mip Xcc mutation (Zang et al, 2007).…”

Section: Resultsmentioning

confidence: 98%

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

Meng

Tang

Fan

et al. 2011

FEMS Microbiol Lett

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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 Xanthomonas campestris pv. campestris (Xcc) (hereafter called Mip(Xcc)) is also involved in virulence. Inactivation of the mip(Xcc) gene leads to a significant reduction in exopolysaccharide production and extracellular protease activity via an unknown mechanism. The Xcc 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 Xcc's total extracellular proteolytic activity. In this study, Western blotting analysis demonstrated that Mip(Xcc) was located in the periplasm. Bacterial two-hybrid and far-Western analysis indicated that Mip(Xcc) interacted with PrtA directly. Purified Mip(Xcc) was found to be able to rescue the protease activity of periplasmic proteins extracted from the mip(Xcc) mutant. These findings show that Mip(Xcc) plays a role in the maturation of PrtA, which is the novel native target for at least one Mip or Mip-like protein.

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Section: Resultsmentioning

confidence: 98%

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

Meng

Tang

Fan

et al. 2011

FEMS Microbiol Lett

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“…Srivastava and Prasad (1989) found a several-fold increase in protease activity in susceptible bean leaves inoculated with X. c. phaseoli and very little activity in inoculated resistant plants. For X. c. campestris, a closely related pathogen of crucifers, protease is an important factor in virulence (Dow et al, 1990), and a gene with homology to a protease gene of X. c. campestris has been identified in X. c. phaseoli (Fujirnoto et al, 1991). Perhaps large amounts of protease is being expressed by the plant during this phase of the host-pathogen interaction making it dilficult to determine bacterial protease activity in the intercellular wash fluid.…”

Section: Discussionmentioning

confidence: 99%

Multiplication of Xanthomonas campestris pv. Phaseoli and Intercellular Enzyme Activities in Resistant and Susceptible Beans

Sopher

Michaels

1995

Journal of Phytopathology

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In order to assess resistance to common bean blight, populations of two isolates of Xanthomonas campestris pv. phaseoli were monitored in leaves of two Phaseolus vulgaris breeding lines, BLT87‐2 (susceptible) and OAC88‐1 (partially resistant) and a resistant tepary bean accession, P. acutifolius P. I. 440795. The breeding line OAC88‐1 possesses resistance to common bacterial blight which was incorporated from P. acutifolius by an interspecific cross. In susceptible, leaves, bacterial populations increased to 108 CFU/g leaf at 3 wk after inoculation whereas, in resistant leaves, bacterial populations declined to 101 ‐ 103 CFU/g leaf. In partially resistant leaves the population first declined similar to that in resistant P. acutifolius but later increased, and typical bacterial blight symptoms appeared. Cellulase, protease and amylase activities were monitored in culture and intercellular leaf spaces. Only cellulase activity was, clearly related to bacterial growth in the susceptible host; other enzyme activities were variable in their relationship to host resistance and bacterial growth. Differences between strains in cellulase activity inside partially resistant leaves corresponded to their ability to secrete cellulase in culture. Measuring cellulase activity in intercellular wash fluids may be a simple and sensitive method for determining X. c. phaseoli populations in leaves.

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“…As a pathogenicity factor, serine protease has been reported from various pathosystems (Dow et al, 1990;Dreier et al, 1997;Nissinen et al, 2009;Redman and Rodriguez, 2002). Dow et al (1990) suggested that the role of bacterial proteases may be nutritional or, alternatively, that they could aid in the infection process through the proteolysis of structural proteins in plant cell walls. Although our data for Pro1 cannot distinguish between these two possibilities, they do indicate that the products of proteolysis serve as stimulators to enhance the germination of resting spores.…”

Section: Pro1 As a Pathogenicity Factormentioning

confidence: 99%

“…A serine protease and a metalloprotease from Xanthomonas campestris pv. campestris play important roles for pathogenesis in black rot on turnip leaves (Dow et al, 1990). In addition, a serine protease (pat-1) has been shown to serve as a pathogenicity factor in Clavibacter michiganensis ssp.…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization of a serine protease Pro1 from Plasmodiophora brassicae that stimulates resting spore germination

Feng

Hwang

et al. 2010

Molecular Plant Pathology

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Clubroot, caused by Plasmodiophora brassicae, is one of the most serious diseases of cultivated cruciferous crops in the world. However, the basis for pathogenicity in P. brassicae is not well understood. In this study, a serine protease gene (PRO1) was cloned from P. brassicae and its molecular characteristics were investigated. Southern analysis and specific polymerase chain reaction (PCR) amplification indicated that PRO1 is a single-copy gene present in a broad range of P. brassicae pathotypes. Northern analysis revealed that the expression of PRO1 was induced during plant infection, and that the quantity of transcript fluctuated according to the stage of pathogenesis. Amino acid sequence analysis suggested that the encoded protein (Pro1) belongs to the S28 family of proteases, with a predicted signal peptide and a theoretical molecular mass of 49.4 kDa. The open reading frame (ORF) of PRO1 was transferred into Pichia pastoris and Pro1 was heterologously produced. Pro1 showed proteolytic activity on skimmed milk and N-succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin, and the activity could be inhibited by serine protease inhibitors and the chelating agent ethylenediaminetetraacetic acid. The optimal temperature of Pro1 was 25 degrees C, and it exhibited high activity at pH 6.0-6.4. These values coincide with the temperature and pH conditions favourable for P. brassicae resting spore germination in the field. When Pro1 was used to treat canola root exudates, it enhanced the stimulating effect of the root exudates on P. brassicae resting spore germination, indicating that Pro1 may play a role during clubroot pathogenesis by stimulating resting spore germination through its proteolytic activity.

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Extracellular proteases from Xanthomonas campestris pv. campestris, the black rot pathogen

Cited by 95 publications

References 14 publications

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

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

Multiplication of Xanthomonas campestris pv. Phaseoli and Intercellular Enzyme Activities in Resistant and Susceptible Beans

Molecular characterization of a serine protease Pro1 from Plasmodiophora brassicae that stimulates resting spore germination

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