The Apoplastic Oxidative Burst Peroxidase in Arabidopsis Is a Major Component of Pattern-Triggered Immunity
In plants, reactive oxygen species (ROS) associated with the response to pathogen attack are generated by NADPH oxidases or apoplastic peroxidases. Antisense expression of a heterologous French bean (Phaseolus vulgaris) peroxidase (FBP1) cDNA in Arabidopsis thaliana was previously shown to diminish...
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| Veröffentlicht in: | The Plant cell 2012-01, Vol.24 (1), p.275-287 |
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| creator | Daudi, Arsalan Cheng, Zhenyu O'Brien, Jose A. Mammarella, Nicole Khan, Satina Ausubel, Frederick M. Bolwell, G. Paul |
| description | In plants, reactive oxygen species (ROS) associated with the response to pathogen attack are generated by NADPH oxidases or apoplastic peroxidases. Antisense expression of a heterologous French bean (Phaseolus vulgaris) peroxidase (FBP1) cDNA in Arabidopsis thaliana was previously shown to diminish the expression of two Arabidopsis peroxidases (peroxidase 33 [PRX33] and PRX34), block the oxidative burst in response to a fungal elicitor, and cause enhanced susceptibility to a broad range of fungal and bacterial pathogens. Here we show that mature leaves of T-DNA insertion lines with diminished expression of PRX33 and PRX34 exhibit reduced ROS and callose deposition in response to microbeassociated molecular patterns (MAMPs), including the synthetic peptides Flg22 and Elf26 corresponding to bacterial flagellili and elongation factor Tu, respectively. PRX33 and PRX34 knockdown lines also exhibited diminished activation of Flg22-activated genes after Flg22 treatment. These MAMP-activated genes were also downregulated in unchallenged leaves of the peroxidase knockdown lines, suggesting that a low level of apoplastic ROS production may be required to preprime basal resistance. Finally, the PRX33 knockdown line is more susceptible to Pseudomonas syringae than wild-type plants. In aggregate, these data demonstrate that the peroxidase-dependent oxidative burst plays an important role in Arabidopsis basal resistance mediated by the recognition of MAMPs. |
| doi_str_mv | 10.1105/tpc.111.093039 |
| format | Article |
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Paul</creator><creatorcontrib>Daudi, Arsalan ; Cheng, Zhenyu ; O'Brien, Jose A. ; Mammarella, Nicole ; Khan, Satina ; Ausubel, Frederick M. ; Bolwell, G. Paul</creatorcontrib><description>In plants, reactive oxygen species (ROS) associated with the response to pathogen attack are generated by NADPH oxidases or apoplastic peroxidases. Antisense expression of a heterologous French bean (Phaseolus vulgaris) peroxidase (FBP1) cDNA in Arabidopsis thaliana was previously shown to diminish the expression of two Arabidopsis peroxidases (peroxidase 33 [PRX33] and PRX34), block the oxidative burst in response to a fungal elicitor, and cause enhanced susceptibility to a broad range of fungal and bacterial pathogens. Here we show that mature leaves of T-DNA insertion lines with diminished expression of PRX33 and PRX34 exhibit reduced ROS and callose deposition in response to microbeassociated molecular patterns (MAMPs), including the synthetic peptides Flg22 and Elf26 corresponding to bacterial flagellili and elongation factor Tu, respectively. PRX33 and PRX34 knockdown lines also exhibited diminished activation of Flg22-activated genes after Flg22 treatment. These MAMP-activated genes were also downregulated in unchallenged leaves of the peroxidase knockdown lines, suggesting that a low level of apoplastic ROS production may be required to preprime basal resistance. Finally, the PRX33 knockdown line is more susceptible to Pseudomonas syringae than wild-type plants. In aggregate, these data demonstrate that the peroxidase-dependent oxidative burst plays an important role in Arabidopsis basal resistance mediated by the recognition of MAMPs.</description><identifier>ISSN: 1040-4651</identifier><identifier>EISSN: 1532-298X</identifier><identifier>DOI: 10.1105/tpc.111.093039</identifier><identifier>PMID: 22247251</identifier><language>eng</language><publisher>United States: American Society of Plant Biologists</publisher><subject>Arabidopsis ; Arabidopsis - enzymology ; Arabidopsis - immunology ; Arabidopsis - metabolism ; Arabidopsis - microbiology ; Arabidopsis Proteins ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Arabidopsis thaliana ; Cell walls ; complementary DNA ; enzymology ; flagellin ; gene activation ; Gene Expression Regulation, Plant ; genes ; genetics ; Glucans ; Glucans - metabolism ; green beans ; Hydrogen ; immunity ; immunology ; Leaves ; Messenger RNA ; metabolism ; microbiology ; NADP (coenzyme) ; Oxidases ; Pathogens ; Peptides ; peroxidase ; Peroxidases ; Peroxidases - genetics ; Peroxidases - metabolism ; Peroxides ; Phaseolus vulgaris ; physiology ; Plant cells ; Plant Immunity ; Plant Immunity - genetics ; Plant Immunity - physiology ; Plant Leaves ; Plant Leaves - enzymology ; Plant Leaves - immunology ; Plant Leaves - metabolism ; Plant Leaves - microbiology ; Plants ; Plants, Genetically Modified ; Plants, Genetically Modified - enzymology ; Plants, Genetically Modified - immunology ; Plants, Genetically Modified - metabolism ; Plants, Genetically Modified - microbiology ; Pseudomonas syringae ; Pseudomonas syringae - physiology ; Reactive oxygen species ; Reactive Oxygen Species - metabolism ; synthetic peptides ; transfer DNA</subject><ispartof>The Plant cell, 2012-01, Vol.24 (1), p.275-287</ispartof><rights>2012 American Society of Plant Biologists</rights><rights>Copyright American Society of Plant Biologists Jan 2012</rights><rights>2012 American Society of Plant Biologists. All rights reserved. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c571t-ddb97da5ec07ddc76da670f14bb6ab8cd0095f53e073757ad86be3e8fa8c3723</citedby><cites>FETCH-LOGICAL-c571t-ddb97da5ec07ddc76da670f14bb6ab8cd0095f53e073757ad86be3e8fa8c3723</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41433965$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41433965$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22247251$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Daudi, Arsalan</creatorcontrib><creatorcontrib>Cheng, Zhenyu</creatorcontrib><creatorcontrib>O'Brien, Jose A.</creatorcontrib><creatorcontrib>Mammarella, Nicole</creatorcontrib><creatorcontrib>Khan, Satina</creatorcontrib><creatorcontrib>Ausubel, Frederick M.</creatorcontrib><creatorcontrib>Bolwell, G. Paul</creatorcontrib><title>The Apoplastic Oxidative Burst Peroxidase in Arabidopsis Is a Major Component of Pattern-Triggered Immunity</title><title>The Plant cell</title><addtitle>Plant Cell</addtitle><description>In plants, reactive oxygen species (ROS) associated with the response to pathogen attack are generated by NADPH oxidases or apoplastic peroxidases. Antisense expression of a heterologous French bean (Phaseolus vulgaris) peroxidase (FBP1) cDNA in Arabidopsis thaliana was previously shown to diminish the expression of two Arabidopsis peroxidases (peroxidase 33 [PRX33] and PRX34), block the oxidative burst in response to a fungal elicitor, and cause enhanced susceptibility to a broad range of fungal and bacterial pathogens. Here we show that mature leaves of T-DNA insertion lines with diminished expression of PRX33 and PRX34 exhibit reduced ROS and callose deposition in response to microbeassociated molecular patterns (MAMPs), including the synthetic peptides Flg22 and Elf26 corresponding to bacterial flagellili and elongation factor Tu, respectively. PRX33 and PRX34 knockdown lines also exhibited diminished activation of Flg22-activated genes after Flg22 treatment. These MAMP-activated genes were also downregulated in unchallenged leaves of the peroxidase knockdown lines, suggesting that a low level of apoplastic ROS production may be required to preprime basal resistance. Finally, the PRX33 knockdown line is more susceptible to Pseudomonas syringae than wild-type plants. In aggregate, these data demonstrate that the peroxidase-dependent oxidative burst plays an important role in Arabidopsis basal resistance mediated by the recognition of MAMPs.</description><subject>Arabidopsis</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis - immunology</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis - microbiology</subject><subject>Arabidopsis Proteins</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Arabidopsis thaliana</subject><subject>Cell walls</subject><subject>complementary DNA</subject><subject>enzymology</subject><subject>flagellin</subject><subject>gene activation</subject><subject>Gene Expression Regulation, Plant</subject><subject>genes</subject><subject>genetics</subject><subject>Glucans</subject><subject>Glucans - metabolism</subject><subject>green beans</subject><subject>Hydrogen</subject><subject>immunity</subject><subject>immunology</subject><subject>Leaves</subject><subject>Messenger RNA</subject><subject>metabolism</subject><subject>microbiology</subject><subject>NADP (coenzyme)</subject><subject>Oxidases</subject><subject>Pathogens</subject><subject>Peptides</subject><subject>peroxidase</subject><subject>Peroxidases</subject><subject>Peroxidases - genetics</subject><subject>Peroxidases - metabolism</subject><subject>Peroxides</subject><subject>Phaseolus vulgaris</subject><subject>physiology</subject><subject>Plant cells</subject><subject>Plant Immunity</subject><subject>Plant Immunity - genetics</subject><subject>Plant Immunity - physiology</subject><subject>Plant Leaves</subject><subject>Plant Leaves - enzymology</subject><subject>Plant Leaves - immunology</subject><subject>Plant Leaves - metabolism</subject><subject>Plant Leaves - microbiology</subject><subject>Plants</subject><subject>Plants, Genetically Modified</subject><subject>Plants, Genetically Modified - enzymology</subject><subject>Plants, Genetically Modified - immunology</subject><subject>Plants, Genetically Modified - metabolism</subject><subject>Plants, Genetically Modified - microbiology</subject><subject>Pseudomonas syringae</subject><subject>Pseudomonas syringae - physiology</subject><subject>Reactive oxygen species</subject><subject>Reactive Oxygen Species - metabolism</subject><subject>synthetic peptides</subject><subject>transfer DNA</subject><issn>1040-4651</issn><issn>1532-298X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkktv1DAUhSMEoqWwZQeyxAI2GfyM7Q3SMOIxUlG7mAU7y7GdqYckDrZT0X-PoykjYAErX_l-Puf66lTVcwRXCEH2Nk-mFGgFJYFEPqjOESO4xlJ8fVhqSGFNG4bOqicpHSCEiCP5uDrDGFOOGTqvvu1uHFhPYep1yt6Aqx_e6uxvHXg_x5TBtYthuUoO-BGso269DVPyCWwT0OCLPoQINmGYwujGDEIHrnXOLo71Lvr93kVnwXYY5tHnu6fVo073yT27Py-q3ccPu83n-vLq03azvqwN4yjX1raSW82cgdxawxurGw47RNu20a0wFkLJOkYc5IQzrq1oWkec6LQwhGNyUb07yk5zOzhrylxR92qKftDxTgXt1Z-d0d-ofbhVBAvJuCwCr-8FYvg-u5TV4JNxfa9HF-akJC5zCiYWqzf_JBEtK8eMSvh_FEIhCIWEF_TVX-ghzHEsK1soSIs7XrxXR8rEkFJ03emHCKolG6pkoxRIHbNRHrz8fS8n_FcYCvDiCBxSDvHUp4gSIhtGfgJru7_X</recordid><startdate>20120101</startdate><enddate>20120101</enddate><creator>Daudi, Arsalan</creator><creator>Cheng, Zhenyu</creator><creator>O'Brien, Jose A.</creator><creator>Mammarella, Nicole</creator><creator>Khan, Satina</creator><creator>Ausubel, Frederick M.</creator><creator>Bolwell, G. 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Paul</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c571t-ddb97da5ec07ddc76da670f14bb6ab8cd0095f53e073757ad86be3e8fa8c3723</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Arabidopsis</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis - immunology</topic><topic>Arabidopsis - metabolism</topic><topic>Arabidopsis - microbiology</topic><topic>Arabidopsis Proteins</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>Arabidopsis thaliana</topic><topic>Cell walls</topic><topic>complementary DNA</topic><topic>enzymology</topic><topic>flagellin</topic><topic>gene activation</topic><topic>Gene Expression Regulation, Plant</topic><topic>genes</topic><topic>genetics</topic><topic>Glucans</topic><topic>Glucans - metabolism</topic><topic>green beans</topic><topic>Hydrogen</topic><topic>immunity</topic><topic>immunology</topic><topic>Leaves</topic><topic>Messenger RNA</topic><topic>metabolism</topic><topic>microbiology</topic><topic>NADP (coenzyme)</topic><topic>Oxidases</topic><topic>Pathogens</topic><topic>Peptides</topic><topic>peroxidase</topic><topic>Peroxidases</topic><topic>Peroxidases - genetics</topic><topic>Peroxidases - metabolism</topic><topic>Peroxides</topic><topic>Phaseolus vulgaris</topic><topic>physiology</topic><topic>Plant cells</topic><topic>Plant Immunity</topic><topic>Plant Immunity - genetics</topic><topic>Plant Immunity - physiology</topic><topic>Plant Leaves</topic><topic>Plant Leaves - enzymology</topic><topic>Plant Leaves - immunology</topic><topic>Plant Leaves - metabolism</topic><topic>Plant Leaves - microbiology</topic><topic>Plants</topic><topic>Plants, Genetically Modified</topic><topic>Plants, Genetically Modified - enzymology</topic><topic>Plants, Genetically Modified - immunology</topic><topic>Plants, Genetically Modified - metabolism</topic><topic>Plants, Genetically Modified - microbiology</topic><topic>Pseudomonas syringae</topic><topic>Pseudomonas syringae - physiology</topic><topic>Reactive oxygen species</topic><topic>Reactive Oxygen Species - metabolism</topic><topic>synthetic peptides</topic><topic>transfer DNA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Daudi, Arsalan</creatorcontrib><creatorcontrib>Cheng, Zhenyu</creatorcontrib><creatorcontrib>O'Brien, Jose A.</creatorcontrib><creatorcontrib>Mammarella, Nicole</creatorcontrib><creatorcontrib>Khan, Satina</creatorcontrib><creatorcontrib>Ausubel, Frederick M.</creatorcontrib><creatorcontrib>Bolwell, G. 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Paul</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Apoplastic Oxidative Burst Peroxidase in Arabidopsis Is a Major Component of Pattern-Triggered Immunity</atitle><jtitle>The Plant cell</jtitle><addtitle>Plant Cell</addtitle><date>2012-01-01</date><risdate>2012</risdate><volume>24</volume><issue>1</issue><spage>275</spage><epage>287</epage><pages>275-287</pages><issn>1040-4651</issn><eissn>1532-298X</eissn><abstract>In plants, reactive oxygen species (ROS) associated with the response to pathogen attack are generated by NADPH oxidases or apoplastic peroxidases. Antisense expression of a heterologous French bean (Phaseolus vulgaris) peroxidase (FBP1) cDNA in Arabidopsis thaliana was previously shown to diminish the expression of two Arabidopsis peroxidases (peroxidase 33 [PRX33] and PRX34), block the oxidative burst in response to a fungal elicitor, and cause enhanced susceptibility to a broad range of fungal and bacterial pathogens. Here we show that mature leaves of T-DNA insertion lines with diminished expression of PRX33 and PRX34 exhibit reduced ROS and callose deposition in response to microbeassociated molecular patterns (MAMPs), including the synthetic peptides Flg22 and Elf26 corresponding to bacterial flagellili and elongation factor Tu, respectively. PRX33 and PRX34 knockdown lines also exhibited diminished activation of Flg22-activated genes after Flg22 treatment. These MAMP-activated genes were also downregulated in unchallenged leaves of the peroxidase knockdown lines, suggesting that a low level of apoplastic ROS production may be required to preprime basal resistance. Finally, the PRX33 knockdown line is more susceptible to Pseudomonas syringae than wild-type plants. In aggregate, these data demonstrate that the peroxidase-dependent oxidative burst plays an important role in Arabidopsis basal resistance mediated by the recognition of MAMPs.</abstract><cop>United States</cop><pub>American Society of Plant Biologists</pub><pmid>22247251</pmid><doi>10.1105/tpc.111.093039</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| source | Jstor Complete Legacy; Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Arabidopsis Arabidopsis - enzymology Arabidopsis - immunology Arabidopsis - metabolism Arabidopsis - microbiology Arabidopsis Proteins Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Arabidopsis thaliana Cell walls complementary DNA enzymology flagellin gene activation Gene Expression Regulation, Plant genes genetics Glucans Glucans - metabolism green beans Hydrogen immunity immunology Leaves Messenger RNA metabolism microbiology NADP (coenzyme) Oxidases Pathogens Peptides peroxidase Peroxidases Peroxidases - genetics Peroxidases - metabolism Peroxides Phaseolus vulgaris physiology Plant cells Plant Immunity Plant Immunity - genetics Plant Immunity - physiology Plant Leaves Plant Leaves - enzymology Plant Leaves - immunology Plant Leaves - metabolism Plant Leaves - microbiology Plants Plants, Genetically Modified Plants, Genetically Modified - enzymology Plants, Genetically Modified - immunology Plants, Genetically Modified - metabolism Plants, Genetically Modified - microbiology Pseudomonas syringae Pseudomonas syringae - physiology Reactive oxygen species Reactive Oxygen Species - metabolism synthetic peptides transfer DNA |
| title | The Apoplastic Oxidative Burst Peroxidase in Arabidopsis Is a Major Component of Pattern-Triggered Immunity |
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