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Volumn 194, Issue 18, 2012, Pages 5054-5064

Pseudomonas syringae catalases are collectively required for plant pathogenesis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CATALASE; HYDROGEN PEROXIDE; KATG PROTEIN; PROTEIN KATB; PROTEIN KATE; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 84866374255     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00999-12     Document Type: Article
Times cited : (40)

References (50)
  • 1
    • 79551688310 scopus 로고    scopus 로고
    • Plant targets for Pseudomonas syringae type III effectors: virulence targets or guarded decoys?
    • Block A, Alfano JR. 2011. Plant targets for Pseudomonas syringae type III effectors: virulence targets or guarded decoys? Curr. Opin. Microbiol. 14:39-46.
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 39-46
    • Block, A.1    Alfano, J.R.2
  • 2
    • 66249135697 scopus 로고    scopus 로고
    • A renaissance of elicitors: perception of microbeassociated molecular patterns and danger signals by pattern-recognition receptors
    • Boller T, Felix G. 2009. A renaissance of elicitors: perception of microbeassociated molecular patterns and danger signals by pattern-recognition receptors. Annu. Rev. Plant Biol. 60:379-406.
    • (2009) Annu. Rev. Plant Biol. , vol.60 , pp. 379-406
    • Boller, T.1    Felix, G.2
  • 3
    • 0028889269 scopus 로고
    • Cloning and characterization of the katB gene of Pseudomonas aeruginosa encoding a hydrogen peroxide-inducible catalase: purification of KatB, cellular localization, and demonstration that it is essential for optimal resistance to hydrogen peroxide
    • Brown SM, Howell ML, Vasil ML, Anderson AJ, Hassett DJ. 1995. Cloning and characterization of the katB gene of Pseudomonas aeruginosa encoding a hydrogen peroxide-inducible catalase: purification of KatB, cellular localization, and demonstration that it is essential for optimal resistance to hydrogen peroxide. J. Bacteriol. 177:6536-6544.
    • (1995) J. Bacteriol. , vol.177 , pp. 6536-6544
    • Brown, S.M.1    Howell, M.L.2    Vasil, M.L.3    Anderson, A.J.4    Hassett, D.J.5
  • 4
    • 0041335630 scopus 로고    scopus 로고
    • The complete sequence of the Arabidopsis and tomato pathogen Pseudomonas syringae pv. tomato DC3000
    • Buell CR, et al. 2003. The complete sequence of the Arabidopsis and tomato pathogen Pseudomonas syringae pv. tomato DC3000. Proc. Natl. Acad. Sci. U. S. A. 100:10181-10186.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 10181-10186
    • Buell, C.R.1
  • 5
    • 0034152767 scopus 로고    scopus 로고
    • Oxidative stress in bacteria and protein damage by reactive oxygen species
    • Cabiscol E, Tamarit J, Ros J. 2000. Oxidative stress in bacteria and protein damage by reactive oxygen species. Int. Microbiol. 3:3-8.
    • (2000) Int. Microbiol. , vol.3 , pp. 3-8
    • Cabiscol, E.1    Tamarit, J.2    Ros, J.3
  • 6
    • 84856730796 scopus 로고    scopus 로고
    • AtRbohF is a crucial modulator of defence-associated metabolism and a key actor in the interplay between intracellular oxidative stress and pathogenesis responses in Arabidopsis
    • Chaouch S, Queval G, Noctor G. 2012. AtRbohF is a crucial modulator of defence-associated metabolism and a key actor in the interplay between intracellular oxidative stress and pathogenesis responses in Arabidopsis. Plant J. 69:613-627.
    • (2012) Plant J. , vol.69 , pp. 613-627
    • Chaouch, S.1    Queval, G.2    Noctor, G.3
  • 7
    • 21444457864 scopus 로고    scopus 로고
    • A Tn7-based broad-range bacterial cloning and expression system
    • Choi KH, et al. 2005. A Tn7-based broad-range bacterial cloning and expression system. Nat. Methods 2:443-448.
    • (2005) Methods. Nat. , vol.2 , pp. 443-448
    • Choi, K.H.1
  • 8
    • 77956694805 scopus 로고    scopus 로고
    • Plant immunity directly or indirectly restricts the injection of type III effectors by the Pseudomonas syringae type III secretion system
    • Crabill E, Joe A, Block A, van Rooyen JM, Alfano JR. 2010. Plant immunity directly or indirectly restricts the injection of type III effectors by the Pseudomonas syringae type III secretion system. Plant Physiol. 154:233-244.
    • (2010) Plant Physiol. , vol.154 , pp. 233-244
    • Crabill, E.1    Joe, A.2    Block, A.3    Rooyen, V.J.M.4    Alfano, J.R.5
  • 9
    • 0022595516 scopus 로고
    • Generation and characterization of Tn5 insertion mutations in Pseudomonas syringae pv. tomato
    • Cuppels DA. 1986. Generation and characterization of Tn5 insertion mutations in Pseudomonas syringae pv. tomato. Appl. Environ. Microbiol. 51:323-327.
    • (1986) Appl. Environ. Microbiol. , vol.51 , pp. 323-327
    • Cuppels, D.A.1
  • 10
    • 84857771627 scopus 로고    scopus 로고
    • The apoplastic oxidative burst peroxidase in Arabidopsis is a major component of pattern-triggered immunity
    • Daudi A, et al. 2012. The apoplastic oxidative burst peroxidase in Arabidopsis is a major component of pattern-triggered immunity. Plant Cell. 24:275-287.
    • (2012) Plant Cell. , vol.24 , pp. 275-287
    • Daudi, A.1
  • 11
    • 0025786078 scopus 로고
    • Oxidative stress responses in Escherichia coli and Salmonella typhimurium
    • Farr SB, Kogoma T. 1991. Oxidative stress responses in Escherichia coli and Salmonella typhimurium. Microbiol. Rev. 55:561-585.
    • (1991) Microbiol. Rev. , vol.55 , pp. 561-585
    • Farr, S.B.1    Kogoma, T.2
  • 12
    • 23344451933 scopus 로고    scopus 로고
    • Comparison of the complete genome sequences of Pseudomonas syringae pv. syringae B728a and pv. tomato DC3000
    • Feil H, et al. 2005. Comparison of the complete genome sequences of Pseudomonas syringae pv. syringae B728a and pv. tomato DC3000. Proc. Natl. Acad. Sci. U. S. A. 102:11064-11069.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 11064-11069
    • Feil, H.1
  • 13
    • 0027483385 scopus 로고
    • Saccharomyces cerevisiae has an inducible response to menadione which differs from that to hydrogen peroxide
    • Flattery-O'Brien J, Collinson LP, Dawes IW. 1993. Saccharomyces cerevisiae has an inducible response to menadione which differs from that to hydrogen peroxide. J. Gen. Microbiol. 139:501-507.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 501-507
    • Flattery-O'brien, J.1    Collinson, L.P.2    Dawes, I.W.3
  • 14
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 15
    • 62649149896 scopus 로고    scopus 로고
    • Functional differences of two distinct catalases in Mesorhizobium loti MAFF303099 under freeliving and symbiotic conditions
    • Hanyu M, Fujimoto H, Tejima K, Saeki K. 2009. Functional differences of two distinct catalases in Mesorhizobium loti MAFF303099 under freeliving and symbiotic conditions. J. Bacteriol. 191:1463-1471.
    • (2009) J. Bacteriol. , vol.191 , pp. 1463-1471
    • Hanyu, M.1    Fujimoto, H.2    Tejima, K.3    Saeki, K.4
  • 16
    • 0029830431 scopus 로고    scopus 로고
    • Cloning and characterization of the katA gene of Rhizobium meliloti encoding a hydrogen peroxide-inducible catalase
    • Herouart D, et al. 1996. Cloning and characterization of the katA gene of Rhizobium meliloti encoding a hydrogen peroxide-inducible catalase. J. Bacteriol. 178:6802-6809.
    • (1996) J. Bacteriol. , vol.178 , pp. 6802-6809
    • Herouart, D.1
  • 17
    • 2442646859 scopus 로고    scopus 로고
    • New recombination methods for Sinorhizobium meliloti genetics
    • House BL, Mortimer MW, Kahn ML. 2004. New recombination methods for Sinorhizobium meliloti genetics. Appl. Environ. Microbiol. 70:2806-2815.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 2806-2815
    • House, B.L.1    Mortimer, M.W.2    Kahn, M.L.3
  • 18
    • 0023886170 scopus 로고
    • DNA damage and oxygen radical toxicity
    • Imlay JA, Linn S. 1988. DNA damage and oxygen radical toxicity. Science 240:1302-1309.
    • (1988) Science , vol.240 , pp. 1302-1309
    • Imlay, J.A.1    Linn, S.2
  • 19
    • 11144308938 scopus 로고    scopus 로고
    • The katA catalase gene is regulated by OxyR in both free-living and symbiotic Sinorhizobium meliloti
    • Jamet A, Kiss E, Batut J, Puppo A, Herouart D. 2005. The katA catalase gene is regulated by OxyR in both free-living and symbiotic Sinorhizobium meliloti. J. Bacteriol. 187:376-381.
    • (2005) J. Bacteriol. , vol.187 , pp. 376-381
    • Jamet, A.1    Kiss, E.2    Batut, J.3    Puppo, A.4    Herouart, D.5
  • 20
    • 0037370853 scopus 로고    scopus 로고
    • Expression of the bacterial catalase genes during Sinorhizobium meliloti-Medicago sativa symbiosis and their crucial role during the infection process
    • Jamet A, Sigaud S, Van de Sype G, Puppo A, Herouart D. 2003. Expression of the bacterial catalase genes during Sinorhizobium meliloti-Medicago sativa symbiosis and their crucial role during the infection process. Mol. Plant Microbe Interact. 16:217-225.
    • (2003) Mol. Plant Microbe Interact. , vol.16 , pp. 217-225
    • Jamet, A.1    Sigaud, S.2    Sype, V.D.G.3    Puppo, A.4    Herouart, D.5
  • 22
    • 24944453122 scopus 로고    scopus 로고
    • Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola 1448A reveals divergence among pathovars in genes involved in virulence and transposition
    • Joardar V, et al. 2005. Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola 1448A reveals divergence among pathovars in genes involved in virulence and transposition. J. Bacteriol. 187:6488-6498.
    • (2005) J. Bacteriol. , vol.187 , pp. 6488-6498
    • Joardar, V.1
  • 24
    • 0000534380 scopus 로고
    • Response of plant-colonizing pseudomonads to hydrogen peroxide
    • Katsuwon J, Anderson AJ. 1989. Response of plant-colonizing pseudomonads to hydrogen peroxide. Appl. Environ. Microbiol. 55:2985-2989.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 2985-2989
    • Katsuwon, J.1    Anderson, A.J.2
  • 25
    • 0001459504 scopus 로고
    • --initiated lipid-peroxidation in a bacteria-induced hypersensitive reaction in tobacco cell-suspensions
    • --initiated lipid-peroxidation in a bacteria-induced hypersensitive reaction in tobacco cell-suspensions. Phytopathology 79:555-562.
    • (1989) Phytopathology , vol.79 , pp. 555-562
    • Keppler, L.D.1    Baker, C.J.2
  • 26
    • 43349086724 scopus 로고
    • Two simple media for the demonstration of pyocyanin and fluorescein
    • King EO, Ward MK, Raney DE. 1954. Two simple media for the demonstration of pyocyanin and fluorescein. J. Lab. Med. 22:301-307.
    • (1954) J. Lab. Med. , vol.22 , pp. 301-307
    • King, E.O.1    Ward, M.K.2    Raney, D.E.3
  • 27
    • 0026643264 scopus 로고
    • Multiple periplasmic catalases in phytopathogenic strains of Pseudomonas syringae
    • Klotz MG, Hutcheson SW. 1992. Multiple periplasmic catalases in phytopathogenic strains of Pseudomonas syringae. Appl. Environ. Microbiol. 58:2468-2473.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 2468-2473
    • Klotz, M.G.1    Hutcheson, S.W.2
  • 28
    • 0029132272 scopus 로고
    • Cloning, characterization and phenotypic expression in Escherichia coli of catF, which encodes the catalytic subunit of catalase isozyme CatF of Pseudomonas syringae
    • Klotz MG, Kim YC, Katsuwon J, Anderson AJ. 1995. Cloning, characterization and phenotypic expression in Escherichia coli of catF, which encodes the catalytic subunit of catalase isozyme CatF of Pseudomonas syringae. Appl. Microbiol. Biotechnol. 43:656-666.
    • (1995) Appl. Microbiol. Biotechnol. , vol.43 , pp. 656-666
    • Klotz, M.G.1    Kim, Y.C.2    Katsuwon, J.3    Anderson, A.J.4
  • 29
    • 0037507299 scopus 로고    scopus 로고
    • NADPH oxidase AtrbohD and AtrbohF genes function in ROS-dependent ABA signaling in Arabidopsis
    • Kwak JM, et al. 2003. NADPH oxidase AtrbohD and AtrbohF genes function in ROS-dependent ABA signaling in Arabidopsis. EMBO J. 22:2623-2633.
    • (2003) EMBO J. , vol.22 , pp. 2623-2633
    • Kwak, J.M.1
  • 31
    • 0029971105 scopus 로고    scopus 로고
    • 2 toxicity protection of a superoxideinducible monofunctional catalase gene from Xanthomonas oryzae pv. oryzae
    • 2 toxicity protection of a superoxideinducible monofunctional catalase gene from Xanthomonas oryzae pv. oryzae. J. Bacteriol. 178:3578-3584.
    • (1996) J. Bacteriol. , vol.178 , pp. 3578-3584
    • Mongkolsuk, S.1
  • 32
    • 31744440140 scopus 로고    scopus 로고
    • Defects in a quinol oxidase lead to loss of KatC catalase activity in Pseudomonas aeruginosa: KatC activity is temperature dependent and it requires an intact disulphide bond formation system
    • Mossialos D, Tavankar GR, Zlosnik JE, Williams HD. 2006. Defects in a quinol oxidase lead to loss of KatC catalase activity in Pseudomonas aeruginosa: KatC activity is temperature dependent and it requires an intact disulphide bond formation system. Biochem. Biophys. Res. Commun. 341:697-702.
    • (2006) Biochem. Biophys. Res. Commun. , vol.341 , pp. 697-702
    • Mossialos, D.1    Tavankar, G.R.2    Zlosnik, J.E.3    Williams, H.D.4
  • 33
    • 3042530074 scopus 로고    scopus 로고
    • The transcriptional innate immune response to flg22. Interplay and overlap with Avr gene-dependent defense responses and bacterial pathogenesis
    • Navarro L, et al. 2004. The transcriptional innate immune response to flg22. Interplay and overlap with Avr gene-dependent defense responses and bacterial pathogenesis. Plant Physiol. 135:1113-1128.
    • (2004) Plant Physiol. , vol.135 , pp. 1113-1128
    • Navarro, L.1
  • 34
    • 0033874090 scopus 로고    scopus 로고
    • Role of the Pseudomonas aeruginosa oxyR-recG operon in oxidative stress defense andDNArepair: OxyR-dependent regulation of katB-ankB, ahpB, and ahpC-ahpF
    • Ochsner UA, Vasil ML, Alsabbagh E, Parvatiyar K, Hassett DJ. 2000. Role of the Pseudomonas aeruginosa oxyR-recG operon in oxidative stress defense andDNArepair: OxyR-dependent regulation of katB-ankB, ahpB, and ahpC-ahpF. J. Bacteriol. 182:4533-4544.
    • (2000) J. Bacteriol. , vol.182 , pp. 4533-4544
    • Ochsner, U.A.1    Vasil, M.L.2    Alsabbagh, E.3    Parvatiyar, K.4    Hassett, D.J.5
  • 35
    • 1842471990 scopus 로고    scopus 로고
    • The role of a bifunctional catalase-peroxidase KatA in protection of Agrobacterium tumefaciens from menadione toxicity
    • Prapagdee B, Vattanaviboon P, Mongkolsuk S. 2004. The role of a bifunctional catalase-peroxidase KatA in protection of Agrobacterium tumefaciens from menadione toxicity. FEMS Microbiol. Lett. 232:217-223.
    • (2004) FEMS Microbiol. Lett. , vol.232 , pp. 217-223
    • Prapagdee, B.1    Vattanaviboon, P.2    Mongkolsuk, S.3
  • 36
    • 84863230574 scopus 로고    scopus 로고
    • Glycolate oxidase modulates reactive oxygen species-mediated signal transduction during nonhost resistance in Nicotiana benthamiana and Arabidopsis
    • Rojas CM, et al. 2012. Glycolate oxidase modulates reactive oxygen species-mediated signal transduction during nonhost resistance in Nicotiana benthamiana and Arabidopsis. Plant Cell 24:336-352.
    • (2012) Plant Cell. , vol.24 , pp. 336-352
    • Rojas, C.M.1
  • 37
    • 0011264081 scopus 로고
    • Interactions of peroxidases and catalases between Phaseolus vulgaris and Pseudomonas phaseolicola (halo blight of bean)
    • Rudolph K, Stahmann MA. 1964. Interactions of peroxidases and catalases between Phaseolus vulgaris and Pseudomonas phaseolicola (halo blight of bean). Nature 204:474-475.
    • (1964) Nature. , vol.204 , pp. 474-475
    • Rudolph, K.1    Stahmann, M.A.2
  • 38
    • 0019365279 scopus 로고
    • A general method for site-directed mutagenesis in prokaryotes
    • Ruvkun GB, Ausubel FM. 1981. A general method for site-directed mutagenesis in prokaryotes. Nature 289:85-88.
    • (1981) Nature. , vol.289 , pp. 85-88
    • Ruvkun, G.B.1    Ausubel, F.M.2
  • 39
    • 0004136246 scopus 로고    scopus 로고
    • Molecular cloning: a laboratory manual
    • 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sambrook J, Russell DW. 2001. Molecular cloning: a laboratory manual, 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2001)
    • Sambrook, J.1    Russell, D.W.2
  • 40
    • 79551682471 scopus 로고    scopus 로고
    • Activation of plant pattern-recognition receptors by bacteria
    • Segonzac C, Zipfel C. 2011. Activation of plant pattern-recognition receptors by bacteria. Curr. Opin. Microbiol. 14:54-61.
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 54-61
    • Segonzac, C.1    Zipfel, C.2
  • 41
    • 0032929263 scopus 로고    scopus 로고
    • Differential regulation of two divergent Sinorhizobium meliloti genes for HPII-like catalases during free-living growth and protective role of both catalases during symbiosis
    • Sigaud S, Becquet V, Frendo P, Puppo A, Herouart D. 1999. Differential regulation of two divergent Sinorhizobium meliloti genes for HPII-like catalases during free-living growth and protective role of both catalases during symbiosis. J. Bacteriol. 181:2634-2639.
    • (1999) J. Bacteriol. , vol.181 , pp. 2634-2639
    • Sigaud, S.1    Becquet, V.2    Frendo, P.3    Puppo, A.4    Herouart, D.5
  • 42
    • 39749141713 scopus 로고    scopus 로고
    • Comparative study of catalase-peroxidases (KatGs)
    • Singh R, et al. 2008. Comparative study of catalase-peroxidases (KatGs).Arch. Biochem. Biophys. 471:207-214.
    • (2008) Arch. Biochem. Biophys. , vol.471 , pp. 207-214
    • Singh, R.1
  • 43
    • 20644441568 scopus 로고    scopus 로고
    • Growth deficiency of a Xanthomonas oryzae pv. oryzae fur mutant in rice leaves is rescued by ascorbic acid supplementation
    • Subramoni S, Sonti RV. 2005. Growth deficiency of a Xanthomonas oryzae pv. oryzae fur mutant in rice leaves is rescued by ascorbic acid supplementation. Mol. Plant Microbe Interact. 18:644-651.
    • (2005) Mol. Plant Microbe Interact. , vol.18 , pp. 644-651
    • Subramoni, S.1    Sonti, R.V.2
  • 44
    • 0037324536 scopus 로고    scopus 로고
    • Quantitative nature of Arabidopsis responses during compatible and incompatible interactions with the bacterial pathogen Pseudomonas syringae
    • Tao Y, et al. 2003. Quantitative nature of Arabidopsis responses during compatible and incompatible interactions with the bacterial pathogen Pseudomonas syringae. Plant Cell 15:317-330.
    • (2003) Plant Cell. , vol.15 , pp. 317-330
    • Tao, Y.1
  • 45
    • 77956289414 scopus 로고    scopus 로고
    • The monofunctional catalase KatE of Xanthomonas axonopodis pv. citri is required for full virulence in citrus plants
    • doi:10.1371/journal.pone.0010803
    • Tondo ML, Petrocelli S, Ottado J, Orellano EG. 2010. The monofunctional catalase KatE of Xanthomonas axonopodis pv. citri is required for full virulence in citrus plants. PLoS One 5:e10803. doi:10.1371/journal.pone.0010803.
    • (2010) PLoS One , vol.5
    • Tondo, M.L.1    Petrocelli, S.2    Ottado, J.3    Orellano, E.G.4
  • 46
    • 77952089074 scopus 로고    scopus 로고
    • ROS in biotic interactions
    • Torres MA. 2010. ROS in biotic interactions. Physiol. Plant. 138:414-429.
    • (2010) Physiol. Plant. , vol.138 , pp. 414-429
    • Torres, M.A.1
  • 47
    • 27144431765 scopus 로고    scopus 로고
    • Pathogen-induced, NADPH oxidase-derived reactive oxygen intermediates suppress spread of cell death in Arabidopsis thaliana
    • Torres MA, Jones JD, Dangl JL. 2005. Pathogen-induced, NADPH oxidase-derived reactive oxygen intermediates suppress spread of cell death in Arabidopsis thaliana. Nat. Genet. 37:1130-1134.
    • (2005) Nat. Genet. , vol.37 , pp. 1130-1134
    • Torres, M.A.1    Jones, J.D.2    Dangl, J.L.3
  • 48
    • 33745662410 scopus 로고    scopus 로고
    • Reactive oxygen species signaling in response to pathogens
    • Torres MA, Jones JD, Dangl JL. 2006. Reactive oxygen species signaling in response to pathogens. Plant Physiol. 141:373-378.
    • (2006) Plant Physiol. , vol.141 , pp. 373-378
    • Torres, M.A.1    Jones, J.D.2    Dangl, J.L.3
  • 49
    • 0033967375 scopus 로고    scopus 로고
    • An Agrobacterium catalase is a virulence factor involved in tumorigenesis
    • Xu XQ, Pan SQ. 2000. An Agrobacterium catalase is a virulence factor involved in tumorigenesis. Mol. Microbiol. 35:407-414.
    • (2000) Mol. Microbiol. , vol.35 , pp. 407-414
    • Xu, X.Q.1    Pan, S.Q.2
  • 50
    • 34248218612 scopus 로고    scopus 로고
    • A Pseudomonas syringae effector inactivates MAPKs to suppress PAMP-induced immunity in plants
    • Zhang J, et al. 2007. A Pseudomonas syringae effector inactivates MAPKs to suppress PAMP-induced immunity in plants. Cell Host Microbe 1:175-185.
    • (2007) Cell Host Microbe. , vol.1 , pp. 175-185
    • Zhang, J.1


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