Quantitative proteomic analyses reveal that RBBI3.3, a trypsin inhibitor protein, plays an important role in Magnaporthe oryzae infection in rice
Magnaporthe oryzae ( M. oryzae ) is the causative agent of rice blast, the most destructive rice disease in China. This study was designed to ascertain the molecular mechanisms of the response of rice to M. oryzae infection to facilitate the breeding of new high-quality and disease-resistant rice va...
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creator | Cui, Shujian Wang, Jiaoyu Gao, Feiyan Sun, Guochang Liang, Jiansheng |
description | Magnaporthe oryzae
(
M. oryzae
) is the causative agent of rice blast, the most destructive rice disease in China. This study was designed to ascertain the molecular mechanisms of the response of rice to
M. oryzae
infection to facilitate the breeding of new high-quality and disease-resistant rice varieties using isobaric tags for relative and absolute quantification (iTRAQ) combined with a high-throughput mass spectrometry identification platform.
M. oryzae
infection models were constructed with the resistant rice cultivar Gumei2 and the non-resistant cultivar Lijiangxintuanheigu (LTH). The results showed that total of 1541 proteins were identified, among which 843 proteins were overlapping between the two biological replicates analyses. Seventy-one proteins were classified as fungi-responsive. Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway enrichment analyses revealed the important roles of these proteins in metabolic processes. Detailed phenotypic analyses revealed that the trypsin inhibitor RBBI3.3 was effective in inhibiting the initial formation of appressoria. Our quantitative proteomic study provides insights into the molecular mechanism underlying
M. oryzae
resistance in the incompatible rice Gumei2. The identification of RBBI3.3 as a key defense regulator highlights a new possibility for disease control. |
doi_str_mv | 10.1007/s10725-018-0435-z |
format | Article |
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(
M. oryzae
) is the causative agent of rice blast, the most destructive rice disease in China. This study was designed to ascertain the molecular mechanisms of the response of rice to
M. oryzae
infection to facilitate the breeding of new high-quality and disease-resistant rice varieties using isobaric tags for relative and absolute quantification (iTRAQ) combined with a high-throughput mass spectrometry identification platform.
M. oryzae
infection models were constructed with the resistant rice cultivar Gumei2 and the non-resistant cultivar Lijiangxintuanheigu (LTH). The results showed that total of 1541 proteins were identified, among which 843 proteins were overlapping between the two biological replicates analyses. Seventy-one proteins were classified as fungi-responsive. Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway enrichment analyses revealed the important roles of these proteins in metabolic processes. Detailed phenotypic analyses revealed that the trypsin inhibitor RBBI3.3 was effective in inhibiting the initial formation of appressoria. Our quantitative proteomic study provides insights into the molecular mechanism underlying
M. oryzae
resistance in the incompatible rice Gumei2. The identification of RBBI3.3 as a key defense regulator highlights a new possibility for disease control.</description><identifier>ISSN: 0167-6903</identifier><identifier>EISSN: 1573-5087</identifier><identifier>DOI: 10.1007/s10725-018-0435-z</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Agriculture ; Appressoria ; Biomedical and Life Sciences ; Disease control ; Encyclopedias ; Fungi ; Genomes ; Infections ; Life Sciences ; Magnaporthe oryzae ; Mass spectrometry ; Mass spectroscopy ; Molecular modelling ; Original Paper ; Plant Anatomy/Development ; Plant breeding ; Plant Physiology ; Plant Sciences ; Proteins ; Rice blast ; Trypsin ; Trypsin inhibitors</subject><ispartof>Plant growth regulation, 2018-12, Vol.86 (3), p.365-374</ispartof><rights>Springer Nature B.V. 2018</rights><rights>Plant Growth Regulation is a copyright of Springer, (2018). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c316t-7dd2419ece3b7d4883eab9d924114f26e852b7fa7f01a7b6aaa29a1fc568164f3</citedby><cites>FETCH-LOGICAL-c316t-7dd2419ece3b7d4883eab9d924114f26e852b7fa7f01a7b6aaa29a1fc568164f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10725-018-0435-z$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10725-018-0435-z$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids></links><search><creatorcontrib>Cui, Shujian</creatorcontrib><creatorcontrib>Wang, Jiaoyu</creatorcontrib><creatorcontrib>Gao, Feiyan</creatorcontrib><creatorcontrib>Sun, Guochang</creatorcontrib><creatorcontrib>Liang, Jiansheng</creatorcontrib><title>Quantitative proteomic analyses reveal that RBBI3.3, a trypsin inhibitor protein, plays an important role in Magnaporthe oryzae infection in rice</title><title>Plant growth regulation</title><addtitle>Plant Growth Regul</addtitle><description>Magnaporthe oryzae
(
M. oryzae
) is the causative agent of rice blast, the most destructive rice disease in China. This study was designed to ascertain the molecular mechanisms of the response of rice to
M. oryzae
infection to facilitate the breeding of new high-quality and disease-resistant rice varieties using isobaric tags for relative and absolute quantification (iTRAQ) combined with a high-throughput mass spectrometry identification platform.
M. oryzae
infection models were constructed with the resistant rice cultivar Gumei2 and the non-resistant cultivar Lijiangxintuanheigu (LTH). The results showed that total of 1541 proteins were identified, among which 843 proteins were overlapping between the two biological replicates analyses. Seventy-one proteins were classified as fungi-responsive. Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway enrichment analyses revealed the important roles of these proteins in metabolic processes. Detailed phenotypic analyses revealed that the trypsin inhibitor RBBI3.3 was effective in inhibiting the initial formation of appressoria. Our quantitative proteomic study provides insights into the molecular mechanism underlying
M. oryzae
resistance in the incompatible rice Gumei2. The identification of RBBI3.3 as a key defense regulator highlights a new possibility for disease control.</description><subject>Agriculture</subject><subject>Appressoria</subject><subject>Biomedical and Life Sciences</subject><subject>Disease control</subject><subject>Encyclopedias</subject><subject>Fungi</subject><subject>Genomes</subject><subject>Infections</subject><subject>Life Sciences</subject><subject>Magnaporthe oryzae</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Molecular modelling</subject><subject>Original Paper</subject><subject>Plant Anatomy/Development</subject><subject>Plant breeding</subject><subject>Plant Physiology</subject><subject>Plant Sciences</subject><subject>Proteins</subject><subject>Rice blast</subject><subject>Trypsin</subject><subject>Trypsin inhibitors</subject><issn>0167-6903</issn><issn>1573-5087</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp1kMFq3DAURUVJoZO0H9CdoNs41ZNsS14mIWkDKaWlXYtnz3NGwWM5kmbA8xf948o40FVXgss9h6fL2EcQVyCE_hxBaFkVAkwhSlUVpzdsA5VWRSWMPmMbAbUu6kaod-w8xmchhDEVbNifHwcck0uY3JH4FHwiv3cdxxGHOVLkgY6EA087TPznzc2DulKXHHkK8xTdyN24c61LPqysGy_5NOAcs4C7_eRDynoe_EC5yr_h04hLuCPuw3zCJe2pS84vKh5cR-_Z2x6HSB9e3wv2-_7u1-3X4vH7l4fb68eiU1CnQm-3soSGOlKt3pbGKMK22TY5hLKXNZlKtrpH3QtA3daIKBuEvqtqA3XZqwv2afXmw18OFJN99oeQvx2tBJCNUtLUuQVrqws-xkC9nYLbY5gtCLssb9flbV7eLsvbU2bkysTcHZ8o_DP_H_oLpX-JfA</recordid><startdate>20181201</startdate><enddate>20181201</enddate><creator>Cui, Shujian</creator><creator>Wang, Jiaoyu</creator><creator>Gao, Feiyan</creator><creator>Sun, Guochang</creator><creator>Liang, Jiansheng</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X2</scope><scope>7XB</scope><scope>8FE</scope><scope>8FH</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M0K</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope></search><sort><creationdate>20181201</creationdate><title>Quantitative proteomic analyses reveal that RBBI3.3, a trypsin inhibitor protein, plays an important role in Magnaporthe oryzae infection in rice</title><author>Cui, Shujian ; Wang, Jiaoyu ; Gao, Feiyan ; Sun, Guochang ; Liang, Jiansheng</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c316t-7dd2419ece3b7d4883eab9d924114f26e852b7fa7f01a7b6aaa29a1fc568164f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Agriculture</topic><topic>Appressoria</topic><topic>Biomedical and Life Sciences</topic><topic>Disease control</topic><topic>Encyclopedias</topic><topic>Fungi</topic><topic>Genomes</topic><topic>Infections</topic><topic>Life Sciences</topic><topic>Magnaporthe oryzae</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Molecular modelling</topic><topic>Original Paper</topic><topic>Plant Anatomy/Development</topic><topic>Plant breeding</topic><topic>Plant Physiology</topic><topic>Plant Sciences</topic><topic>Proteins</topic><topic>Rice blast</topic><topic>Trypsin</topic><topic>Trypsin inhibitors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cui, Shujian</creatorcontrib><creatorcontrib>Wang, Jiaoyu</creatorcontrib><creatorcontrib>Gao, Feiyan</creatorcontrib><creatorcontrib>Sun, Guochang</creatorcontrib><creatorcontrib>Liang, Jiansheng</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Agricultural Science Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Research Library</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><jtitle>Plant growth regulation</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cui, Shujian</au><au>Wang, Jiaoyu</au><au>Gao, Feiyan</au><au>Sun, Guochang</au><au>Liang, Jiansheng</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Quantitative proteomic analyses reveal that RBBI3.3, a trypsin inhibitor protein, plays an important role in Magnaporthe oryzae infection in rice</atitle><jtitle>Plant growth regulation</jtitle><stitle>Plant Growth Regul</stitle><date>2018-12-01</date><risdate>2018</risdate><volume>86</volume><issue>3</issue><spage>365</spage><epage>374</epage><pages>365-374</pages><issn>0167-6903</issn><eissn>1573-5087</eissn><abstract>Magnaporthe oryzae
(
M. oryzae
) is the causative agent of rice blast, the most destructive rice disease in China. This study was designed to ascertain the molecular mechanisms of the response of rice to
M. oryzae
infection to facilitate the breeding of new high-quality and disease-resistant rice varieties using isobaric tags for relative and absolute quantification (iTRAQ) combined with a high-throughput mass spectrometry identification platform.
M. oryzae
infection models were constructed with the resistant rice cultivar Gumei2 and the non-resistant cultivar Lijiangxintuanheigu (LTH). The results showed that total of 1541 proteins were identified, among which 843 proteins were overlapping between the two biological replicates analyses. Seventy-one proteins were classified as fungi-responsive. Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway enrichment analyses revealed the important roles of these proteins in metabolic processes. Detailed phenotypic analyses revealed that the trypsin inhibitor RBBI3.3 was effective in inhibiting the initial formation of appressoria. Our quantitative proteomic study provides insights into the molecular mechanism underlying
M. oryzae
resistance in the incompatible rice Gumei2. The identification of RBBI3.3 as a key defense regulator highlights a new possibility for disease control.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><doi>10.1007/s10725-018-0435-z</doi><tpages>10</tpages></addata></record> |
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subjects | Agriculture Appressoria Biomedical and Life Sciences Disease control Encyclopedias Fungi Genomes Infections Life Sciences Magnaporthe oryzae Mass spectrometry Mass spectroscopy Molecular modelling Original Paper Plant Anatomy/Development Plant breeding Plant Physiology Plant Sciences Proteins Rice blast Trypsin Trypsin inhibitors |
title | Quantitative proteomic analyses reveal that RBBI3.3, a trypsin inhibitor protein, plays an important role in Magnaporthe oryzae infection in rice |
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