Comparative Appraisal of Leaf Proteomic and Mass Spectrometry Analyses During Fusarium Wilt Infection in Resistance and Susceptible Genotypes of Castor (Ricinus communis L.)
The resistant and susceptible genotypes of castor were utilized for leaf proteomic study during Fusarium wilt infection. The histopathological study was observed under SEM and it confirmed that the infection of Fusarium oxysporum f. sp. ricini was higher in the root of susceptible JI-35, while incom...
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| Veröffentlicht in: | The Protein Journal 2022-12, Vol.41 (6), p.638-658 |
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| creator | Kachhadiya, Harshita J. Gajera, H. P. Mehta, D. R. Hirpara, Darshna G. Bhadani, Rushita V. Dave, R. A. |
| description | The resistant and susceptible genotypes of castor were utilized for leaf proteomic study during
Fusarium
wilt infection. The histopathological study was observed under SEM and it confirmed that the infection of
Fusarium oxysporum
f. sp.
ricini
was higher in the root of susceptible JI-35, while incompatible interaction is observed in resistant SKI-215 genotype. The acidic and neutral proteins were maximally up-expressed with 2 to 171 kDa in treated resistant and 2 to 150 kDa in treated susceptible interactions. In resistant genotype, the leaf proteins were recognized with 3.0- and 5.8-fold higher at infection stage and post-infection stage, respectively, as compared to susceptible genotype. The highly up expressions of leaf acidic (4.76 pI) and basic (8.77 pI) proteins were found with 224.94- and 61.68-fold change, respectively during the post-infection stage in treated resistance compared to its control. The protein spots at 4.76 pI and 8.77 pI were characterized with nanoLC–MS Triple TOF and were recognized as signalling molecules small GTP binding protein (23 kDa) and actin (8 kDa), respectively, on the basis of mass spectrometry and peptide sequences. However, basic and neutral proteins were up regulated as 30.11- and 20.30-fold changes in treated susceptible compared to its control. These proteins were identified as HSP90 (10 kDa) and LEA (27 kDa) proteins. The 148 kDa protein is recognized as histidine kinase in incompatible resistant interaction compared to compatible susceptible (serine threonine protein kinase, 65 kDa) as common acidic protein at 3.80 pI during infection stage. Some acidic proteins were maximally up-regulated in the leaf of resistant castor genotype and played a significant role in defense response. |
| doi_str_mv | 10.1007/s10930-022-10083-4 |
| format | Article |
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Fusarium
wilt infection. The histopathological study was observed under SEM and it confirmed that the infection of
Fusarium oxysporum
f. sp.
ricini
was higher in the root of susceptible JI-35, while incompatible interaction is observed in resistant SKI-215 genotype. The acidic and neutral proteins were maximally up-expressed with 2 to 171 kDa in treated resistant and 2 to 150 kDa in treated susceptible interactions. In resistant genotype, the leaf proteins were recognized with 3.0- and 5.8-fold higher at infection stage and post-infection stage, respectively, as compared to susceptible genotype. The highly up expressions of leaf acidic (4.76 pI) and basic (8.77 pI) proteins were found with 224.94- and 61.68-fold change, respectively during the post-infection stage in treated resistance compared to its control. The protein spots at 4.76 pI and 8.77 pI were characterized with nanoLC–MS Triple TOF and were recognized as signalling molecules small GTP binding protein (23 kDa) and actin (8 kDa), respectively, on the basis of mass spectrometry and peptide sequences. However, basic and neutral proteins were up regulated as 30.11- and 20.30-fold changes in treated susceptible compared to its control. These proteins were identified as HSP90 (10 kDa) and LEA (27 kDa) proteins. The 148 kDa protein is recognized as histidine kinase in incompatible resistant interaction compared to compatible susceptible (serine threonine protein kinase, 65 kDa) as common acidic protein at 3.80 pI during infection stage. Some acidic proteins were maximally up-regulated in the leaf of resistant castor genotype and played a significant role in defense response.</description><identifier>ISSN: 1572-3887</identifier><identifier>EISSN: 1875-8355</identifier><identifier>EISSN: 1573-4943</identifier><identifier>DOI: 10.1007/s10930-022-10083-4</identifier><identifier>PMID: 36251227</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Actin ; Animal Anatomy ; Biochemistry ; Bioorganic Chemistry ; Chemistry ; Chemistry and Materials Science ; Fusarium ; Fusarium - metabolism ; Fusarium oxysporum ; Genotype ; Genotype & phenotype ; Genotypes ; GTP-binding protein ; Histidine ; Histidine kinase ; Histology ; Hsp90 protein ; Infections ; Kinases ; Leaves ; Mass Spectrometry ; Mass spectroscopy ; Morphology ; Organic Chemistry ; Plant Diseases - genetics ; Plant Leaves - genetics ; Protein kinase ; Proteins ; Proteomics ; Ricinus ; Scientific imaging ; Spectroscopy ; Threonine ; Wilt</subject><ispartof>The Protein Journal, 2022-12, Vol.41 (6), p.638-658</ispartof><rights>The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2022. Springer Nature or its licensor holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2022. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c326t-9fdea5afaee1759d0d9e62cf2b2957ebb105c3c462e5470d44b85c05e3b2391b3</cites><orcidid>0000-0001-6177-5414</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10930-022-10083-4$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10930-022-10083-4$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36251227$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kachhadiya, Harshita J.</creatorcontrib><creatorcontrib>Gajera, H. P.</creatorcontrib><creatorcontrib>Mehta, D. R.</creatorcontrib><creatorcontrib>Hirpara, Darshna G.</creatorcontrib><creatorcontrib>Bhadani, Rushita V.</creatorcontrib><creatorcontrib>Dave, R. A.</creatorcontrib><title>Comparative Appraisal of Leaf Proteomic and Mass Spectrometry Analyses During Fusarium Wilt Infection in Resistance and Susceptible Genotypes of Castor (Ricinus communis L.)</title><title>The Protein Journal</title><addtitle>Protein J</addtitle><addtitle>Protein J</addtitle><description>The resistant and susceptible genotypes of castor were utilized for leaf proteomic study during
Fusarium
wilt infection. The histopathological study was observed under SEM and it confirmed that the infection of
Fusarium oxysporum
f. sp.
ricini
was higher in the root of susceptible JI-35, while incompatible interaction is observed in resistant SKI-215 genotype. The acidic and neutral proteins were maximally up-expressed with 2 to 171 kDa in treated resistant and 2 to 150 kDa in treated susceptible interactions. In resistant genotype, the leaf proteins were recognized with 3.0- and 5.8-fold higher at infection stage and post-infection stage, respectively, as compared to susceptible genotype. The highly up expressions of leaf acidic (4.76 pI) and basic (8.77 pI) proteins were found with 224.94- and 61.68-fold change, respectively during the post-infection stage in treated resistance compared to its control. The protein spots at 4.76 pI and 8.77 pI were characterized with nanoLC–MS Triple TOF and were recognized as signalling molecules small GTP binding protein (23 kDa) and actin (8 kDa), respectively, on the basis of mass spectrometry and peptide sequences. However, basic and neutral proteins were up regulated as 30.11- and 20.30-fold changes in treated susceptible compared to its control. These proteins were identified as HSP90 (10 kDa) and LEA (27 kDa) proteins. The 148 kDa protein is recognized as histidine kinase in incompatible resistant interaction compared to compatible susceptible (serine threonine protein kinase, 65 kDa) as common acidic protein at 3.80 pI during infection stage. Some acidic proteins were maximally up-regulated in the leaf of resistant castor genotype and played a significant role in defense response.</description><subject>Actin</subject><subject>Animal Anatomy</subject><subject>Biochemistry</subject><subject>Bioorganic Chemistry</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Fusarium</subject><subject>Fusarium - metabolism</subject><subject>Fusarium oxysporum</subject><subject>Genotype</subject><subject>Genotype & phenotype</subject><subject>Genotypes</subject><subject>GTP-binding protein</subject><subject>Histidine</subject><subject>Histidine kinase</subject><subject>Histology</subject><subject>Hsp90 protein</subject><subject>Infections</subject><subject>Kinases</subject><subject>Leaves</subject><subject>Mass Spectrometry</subject><subject>Mass spectroscopy</subject><subject>Morphology</subject><subject>Organic Chemistry</subject><subject>Plant Diseases - genetics</subject><subject>Plant Leaves - genetics</subject><subject>Protein kinase</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Ricinus</subject><subject>Scientific imaging</subject><subject>Spectroscopy</subject><subject>Threonine</subject><subject>Wilt</subject><issn>1572-3887</issn><issn>1875-8355</issn><issn>1573-4943</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kc9u1DAQhyMEoqXwAhyQJS7lkNZ_4jg5rra0VFpU1II4Ro4zQa4SO3hspH0bnoCH6JPV2y0gceA0Humbb6z5FcVrRk8YpeoUGW0FLSnnZe4bUVZPikPWKFk2Qsqn-S0VL0XTqIPiBeItpbxpFX9eHIiaS8a5Oix-rf286KCj_QFktSxBW9QT8SPZgB7Jp-Aj-Nkaot1APmpEcrOAicHPEMOWrJyetghIzlKw7hs5T6iDTfPdz692iuTSjRm23hHryDWgxaidgQfZTUIDS7T9BOQCnI_bJXvy4rXG6AM5vrbGuoTE-HlOziLZnLx7WTwb9YTw6rEeFV_O339efyg3VxeX69WmNILXsWzHAbTUowZgSrYDHVqouRl5z1upoO8ZlUaYquYgK0WHquobaagE0XPRsl4cFcd77xL89wQYu9nm706TduATdlxxWVWsbpuMvv0HvfUp5LvsKFG3opacZ4rvKRM8YoCxW4Kdddh2jHa7NLt9ml1Os3tIs6vy0JtHdepnGP6M_I4vA2IP4LI7P4S_u_-jvQdrD63h</recordid><startdate>20221201</startdate><enddate>20221201</enddate><creator>Kachhadiya, Harshita J.</creator><creator>Gajera, H. 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P.</au><au>Mehta, D. R.</au><au>Hirpara, Darshna G.</au><au>Bhadani, Rushita V.</au><au>Dave, R. A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparative Appraisal of Leaf Proteomic and Mass Spectrometry Analyses During Fusarium Wilt Infection in Resistance and Susceptible Genotypes of Castor (Ricinus communis L.)</atitle><jtitle>The Protein Journal</jtitle><stitle>Protein J</stitle><addtitle>Protein J</addtitle><date>2022-12-01</date><risdate>2022</risdate><volume>41</volume><issue>6</issue><spage>638</spage><epage>658</epage><pages>638-658</pages><issn>1572-3887</issn><eissn>1875-8355</eissn><eissn>1573-4943</eissn><abstract>The resistant and susceptible genotypes of castor were utilized for leaf proteomic study during
Fusarium
wilt infection. The histopathological study was observed under SEM and it confirmed that the infection of
Fusarium oxysporum
f. sp.
ricini
was higher in the root of susceptible JI-35, while incompatible interaction is observed in resistant SKI-215 genotype. The acidic and neutral proteins were maximally up-expressed with 2 to 171 kDa in treated resistant and 2 to 150 kDa in treated susceptible interactions. In resistant genotype, the leaf proteins were recognized with 3.0- and 5.8-fold higher at infection stage and post-infection stage, respectively, as compared to susceptible genotype. The highly up expressions of leaf acidic (4.76 pI) and basic (8.77 pI) proteins were found with 224.94- and 61.68-fold change, respectively during the post-infection stage in treated resistance compared to its control. The protein spots at 4.76 pI and 8.77 pI were characterized with nanoLC–MS Triple TOF and were recognized as signalling molecules small GTP binding protein (23 kDa) and actin (8 kDa), respectively, on the basis of mass spectrometry and peptide sequences. However, basic and neutral proteins were up regulated as 30.11- and 20.30-fold changes in treated susceptible compared to its control. These proteins were identified as HSP90 (10 kDa) and LEA (27 kDa) proteins. The 148 kDa protein is recognized as histidine kinase in incompatible resistant interaction compared to compatible susceptible (serine threonine protein kinase, 65 kDa) as common acidic protein at 3.80 pI during infection stage. Some acidic proteins were maximally up-regulated in the leaf of resistant castor genotype and played a significant role in defense response.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>36251227</pmid><doi>10.1007/s10930-022-10083-4</doi><tpages>21</tpages><orcidid>https://orcid.org/0000-0001-6177-5414</orcidid></addata></record> |
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| subjects | Actin Animal Anatomy Biochemistry Bioorganic Chemistry Chemistry Chemistry and Materials Science Fusarium Fusarium - metabolism Fusarium oxysporum Genotype Genotype & phenotype Genotypes GTP-binding protein Histidine Histidine kinase Histology Hsp90 protein Infections Kinases Leaves Mass Spectrometry Mass spectroscopy Morphology Organic Chemistry Plant Diseases - genetics Plant Leaves - genetics Protein kinase Proteins Proteomics Ricinus Scientific imaging Spectroscopy Threonine Wilt |
| title | Comparative Appraisal of Leaf Proteomic and Mass Spectrometry Analyses During Fusarium Wilt Infection in Resistance and Susceptible Genotypes of Castor (Ricinus communis L.) |
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