Genome wide comprehensive analysis and web resource development on cell wall degrading enzymes from phyto-parasitic nematodes
The plant cell wall serves as a primary barrier against pathogen invasion. The success of a plant pathogen largely depends on its ability to overcome this barrier. During the infection process, plant parasitic nematodes secrete cell wall degrading enzymes (CWDEs) apart from piercing with their style...
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description | The plant cell wall serves as a primary barrier against pathogen invasion. The success of a plant pathogen largely depends on its ability to overcome this barrier. During the infection process, plant parasitic nematodes secrete cell wall degrading enzymes (CWDEs) apart from piercing with their stylet, a sharp and hard mouthpart used for successful infection. CWDEs typically consist of cellulases, hemicellulases, and pectinases, which help the nematode to infect and establish the feeding structure or form a cyst. The study of nematode cell wall degrading enzymes not only enhance our understanding of the interaction between nematodes and their host, but also provides information on a novel source of enzymes for their potential use in biomass based biofuel/bioproduct industries. Although there is comprehensive information available on genome wide analysis of CWDEs for bacteria, fungi, termites and plants, but no comprehensive information available for plant pathogenic nematodes. Herein we have performed a genome wide analysis of CWDEs from the genome sequenced phyto pathogenic nematode species and developed a comprehensive publicly available database.
In the present study, we have performed a genome wide analysis for the presence of CWDEs from five plant parasitic nematode species with fully sequenced genomes covering three genera viz. Bursaphelenchus, Glorodera and Meloidogyne. Using the Hidden Markov Models (HMM) conserved domain profiles of the respective gene families, we have identified 530 genes encoding CWDEs that are distributed among 24 gene families of glycoside hydrolases (412) and polysaccharide lyases (118). Furthermore, expression profiles of these genes were analyzed across the life cycle of a potato cyst nematode. Most genes were found to have moderate to high expression from early to late infectious stages, while some clusters were invasion stage specific, indicating the role of these enzymes in the nematode's infection and establishment process. Additionally, we have also developed a Nematode's Plant Cell Wall Degrading Enzyme (NCWDE) database as a platform to provide a comprehensive outcome of the present study.
Our study provides collective information about different families of CWDEs from five different sequenced plant pathogenic nematode species. The outcomes of this study will help in developing better strategies to curtail the nematode infection, as well as help in identification of novel cell wall degrading enzymes for biofuel/biopro |
doi_str_mv | 10.1186/s12870-015-0576-4 |
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In the present study, we have performed a genome wide analysis for the presence of CWDEs from five plant parasitic nematode species with fully sequenced genomes covering three genera viz. Bursaphelenchus, Glorodera and Meloidogyne. Using the Hidden Markov Models (HMM) conserved domain profiles of the respective gene families, we have identified 530 genes encoding CWDEs that are distributed among 24 gene families of glycoside hydrolases (412) and polysaccharide lyases (118). Furthermore, expression profiles of these genes were analyzed across the life cycle of a potato cyst nematode. Most genes were found to have moderate to high expression from early to late infectious stages, while some clusters were invasion stage specific, indicating the role of these enzymes in the nematode's infection and establishment process. Additionally, we have also developed a Nematode's Plant Cell Wall Degrading Enzyme (NCWDE) database as a platform to provide a comprehensive outcome of the present study.
Our study provides collective information about different families of CWDEs from five different sequenced plant pathogenic nematode species. The outcomes of this study will help in developing better strategies to curtail the nematode infection, as well as help in identification of novel cell wall degrading enzymes for biofuel/bioproduct industries.</description><identifier>ISSN: 1471-2229</identifier><identifier>EISSN: 1471-2229</identifier><identifier>DOI: 10.1186/s12870-015-0576-4</identifier><identifier>PMID: 26232118</identifier><language>eng</language><publisher>England: BioMed Central Ltd</publisher><subject>Analysis ; Animals ; Cell Wall - physiology ; Cellulose ; Genetic aspects ; Genome-Wide Association Study ; Glycoside Hydrolases - genetics ; Glycoside Hydrolases - metabolism ; Health aspects ; Helminth Proteins - genetics ; Helminth Proteins - metabolism ; Markov processes ; Nematoda ; Physiological aspects ; Plant Cells - physiology ; Polysaccharide-Lyases - genetics ; Polysaccharide-Lyases - metabolism ; Termites ; Tylenchida - enzymology ; Tylenchida - genetics</subject><ispartof>BMC plant biology, 2015-08, Vol.15 (1), p.187-187, Article 187</ispartof><rights>COPYRIGHT 2015 BioMed Central Ltd.</rights><rights>Copyright BioMed Central 2015</rights><rights>Rai et al. 2015</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c528t-c699b5ccb766c73f19f972b20e115c11e5e5500ba77d212ea8ccda8f2a0b555c3</citedby><cites>FETCH-LOGICAL-c528t-c699b5ccb766c73f19f972b20e115c11e5e5500ba77d212ea8ccda8f2a0b555c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4521475/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4521475/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27922,27923,53789,53791</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26232118$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rai, Krishan Mohan</creatorcontrib><creatorcontrib>Balasubramanian, Vimal Kumar</creatorcontrib><creatorcontrib>Welker, Cassie Marie</creatorcontrib><creatorcontrib>Pang, Mingxiong</creatorcontrib><creatorcontrib>Hii, Mei Mei</creatorcontrib><creatorcontrib>Mendu, Venugopal</creatorcontrib><title>Genome wide comprehensive analysis and web resource development on cell wall degrading enzymes from phyto-parasitic nematodes</title><title>BMC plant biology</title><addtitle>BMC Plant Biol</addtitle><description>The plant cell wall serves as a primary barrier against pathogen invasion. The success of a plant pathogen largely depends on its ability to overcome this barrier. During the infection process, plant parasitic nematodes secrete cell wall degrading enzymes (CWDEs) apart from piercing with their stylet, a sharp and hard mouthpart used for successful infection. CWDEs typically consist of cellulases, hemicellulases, and pectinases, which help the nematode to infect and establish the feeding structure or form a cyst. The study of nematode cell wall degrading enzymes not only enhance our understanding of the interaction between nematodes and their host, but also provides information on a novel source of enzymes for their potential use in biomass based biofuel/bioproduct industries. Although there is comprehensive information available on genome wide analysis of CWDEs for bacteria, fungi, termites and plants, but no comprehensive information available for plant pathogenic nematodes. Herein we have performed a genome wide analysis of CWDEs from the genome sequenced phyto pathogenic nematode species and developed a comprehensive publicly available database.
In the present study, we have performed a genome wide analysis for the presence of CWDEs from five plant parasitic nematode species with fully sequenced genomes covering three genera viz. Bursaphelenchus, Glorodera and Meloidogyne. Using the Hidden Markov Models (HMM) conserved domain profiles of the respective gene families, we have identified 530 genes encoding CWDEs that are distributed among 24 gene families of glycoside hydrolases (412) and polysaccharide lyases (118). Furthermore, expression profiles of these genes were analyzed across the life cycle of a potato cyst nematode. Most genes were found to have moderate to high expression from early to late infectious stages, while some clusters were invasion stage specific, indicating the role of these enzymes in the nematode's infection and establishment process. Additionally, we have also developed a Nematode's Plant Cell Wall Degrading Enzyme (NCWDE) database as a platform to provide a comprehensive outcome of the present study.
Our study provides collective information about different families of CWDEs from five different sequenced plant pathogenic nematode species. The outcomes of this study will help in developing better strategies to curtail the nematode infection, as well as help in identification of novel cell wall degrading enzymes for biofuel/bioproduct industries.</description><subject>Analysis</subject><subject>Animals</subject><subject>Cell Wall - physiology</subject><subject>Cellulose</subject><subject>Genetic aspects</subject><subject>Genome-Wide Association Study</subject><subject>Glycoside Hydrolases - genetics</subject><subject>Glycoside Hydrolases - metabolism</subject><subject>Health aspects</subject><subject>Helminth Proteins - genetics</subject><subject>Helminth Proteins - metabolism</subject><subject>Markov processes</subject><subject>Nematoda</subject><subject>Physiological aspects</subject><subject>Plant Cells - physiology</subject><subject>Polysaccharide-Lyases - genetics</subject><subject>Polysaccharide-Lyases - metabolism</subject><subject>Termites</subject><subject>Tylenchida - enzymology</subject><subject>Tylenchida - genetics</subject><issn>1471-2229</issn><issn>1471-2229</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</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>eNptkl9rHCEUxYfS0qRpP0BfitCX9mFSdUadeSmE0KSBQKF_nsXRO7uGUac6s9st5LvXYdOwW4qgF_3dox5OUbwm-JyQhn9IhDYCl5iwEjPBy_pJcUpqQUpKafv0oD4pXqR0hzERTd0-L04opxXNEqfF_TX44ABtrQGkgxsjrMEnuwGkvBp2yaZcGLSFDkVIYY4akIENDGF04CcUPNIwDGir8mRgFZWxfoXA_945SKiPwaFxvZtCOaqokp2sRh6cmoKB9LJ41qshwauH9az4cfXp--Xn8vbL9c3lxW2pGW2mUvO27ZjWneBci6onbd8K2lEMhDBNCDBgDONOCWEooaAarY1qeqpwxxjT1Vnxca87zp0Do_PDoxrkGK1TcSeDsvL4xNu1XIWNrBnNJrIs8O5BIIafM6RJOpuWfysPYU6SCEyatuINyejbf9C77Fr2cqEaXGFeiQNqpQaQ1vch36sXUXnBalIJjnmdqfP_UHkYcFYHD73N-0cN748aMjPBr2ml5pTkzbevxyzZszqGlCL0j34QLJd8yX2-ZM6XXPIll543h0Y-dvwNVPUH7MbMUg</recordid><startdate>20150801</startdate><enddate>20150801</enddate><creator>Rai, Krishan Mohan</creator><creator>Balasubramanian, Vimal Kumar</creator><creator>Welker, Cassie Marie</creator><creator>Pang, Mingxiong</creator><creator>Hii, Mei Mei</creator><creator>Mendu, Venugopal</creator><general>BioMed Central Ltd</general><general>BioMed Central</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>ISR</scope><scope>3V.</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</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>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20150801</creationdate><title>Genome wide comprehensive analysis and web resource development on cell wall degrading enzymes from phyto-parasitic nematodes</title><author>Rai, Krishan Mohan ; Balasubramanian, Vimal Kumar ; Welker, Cassie Marie ; Pang, Mingxiong ; Hii, Mei Mei ; Mendu, Venugopal</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c528t-c699b5ccb766c73f19f972b20e115c11e5e5500ba77d212ea8ccda8f2a0b555c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Analysis</topic><topic>Animals</topic><topic>Cell Wall - physiology</topic><topic>Cellulose</topic><topic>Genetic aspects</topic><topic>Genome-Wide Association Study</topic><topic>Glycoside Hydrolases - genetics</topic><topic>Glycoside Hydrolases - metabolism</topic><topic>Health aspects</topic><topic>Helminth Proteins - genetics</topic><topic>Helminth Proteins - metabolism</topic><topic>Markov processes</topic><topic>Nematoda</topic><topic>Physiological aspects</topic><topic>Plant Cells - physiology</topic><topic>Polysaccharide-Lyases - genetics</topic><topic>Polysaccharide-Lyases - metabolism</topic><topic>Termites</topic><topic>Tylenchida - enzymology</topic><topic>Tylenchida - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rai, Krishan Mohan</creatorcontrib><creatorcontrib>Balasubramanian, Vimal Kumar</creatorcontrib><creatorcontrib>Welker, Cassie Marie</creatorcontrib><creatorcontrib>Pang, Mingxiong</creatorcontrib><creatorcontrib>Hii, Mei Mei</creatorcontrib><creatorcontrib>Mendu, Venugopal</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</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 (ProQuest)</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</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 China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>BMC plant biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rai, Krishan Mohan</au><au>Balasubramanian, Vimal Kumar</au><au>Welker, Cassie Marie</au><au>Pang, Mingxiong</au><au>Hii, Mei Mei</au><au>Mendu, Venugopal</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Genome wide comprehensive analysis and web resource development on cell wall degrading enzymes from phyto-parasitic nematodes</atitle><jtitle>BMC plant biology</jtitle><addtitle>BMC Plant Biol</addtitle><date>2015-08-01</date><risdate>2015</risdate><volume>15</volume><issue>1</issue><spage>187</spage><epage>187</epage><pages>187-187</pages><artnum>187</artnum><issn>1471-2229</issn><eissn>1471-2229</eissn><abstract>The plant cell wall serves as a primary barrier against pathogen invasion. The success of a plant pathogen largely depends on its ability to overcome this barrier. During the infection process, plant parasitic nematodes secrete cell wall degrading enzymes (CWDEs) apart from piercing with their stylet, a sharp and hard mouthpart used for successful infection. CWDEs typically consist of cellulases, hemicellulases, and pectinases, which help the nematode to infect and establish the feeding structure or form a cyst. The study of nematode cell wall degrading enzymes not only enhance our understanding of the interaction between nematodes and their host, but also provides information on a novel source of enzymes for their potential use in biomass based biofuel/bioproduct industries. Although there is comprehensive information available on genome wide analysis of CWDEs for bacteria, fungi, termites and plants, but no comprehensive information available for plant pathogenic nematodes. Herein we have performed a genome wide analysis of CWDEs from the genome sequenced phyto pathogenic nematode species and developed a comprehensive publicly available database.
In the present study, we have performed a genome wide analysis for the presence of CWDEs from five plant parasitic nematode species with fully sequenced genomes covering three genera viz. Bursaphelenchus, Glorodera and Meloidogyne. Using the Hidden Markov Models (HMM) conserved domain profiles of the respective gene families, we have identified 530 genes encoding CWDEs that are distributed among 24 gene families of glycoside hydrolases (412) and polysaccharide lyases (118). Furthermore, expression profiles of these genes were analyzed across the life cycle of a potato cyst nematode. Most genes were found to have moderate to high expression from early to late infectious stages, while some clusters were invasion stage specific, indicating the role of these enzymes in the nematode's infection and establishment process. Additionally, we have also developed a Nematode's Plant Cell Wall Degrading Enzyme (NCWDE) database as a platform to provide a comprehensive outcome of the present study.
Our study provides collective information about different families of CWDEs from five different sequenced plant pathogenic nematode species. The outcomes of this study will help in developing better strategies to curtail the nematode infection, as well as help in identification of novel cell wall degrading enzymes for biofuel/bioproduct industries.</abstract><cop>England</cop><pub>BioMed Central Ltd</pub><pmid>26232118</pmid><doi>10.1186/s12870-015-0576-4</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Analysis Animals Cell Wall - physiology Cellulose Genetic aspects Genome-Wide Association Study Glycoside Hydrolases - genetics Glycoside Hydrolases - metabolism Health aspects Helminth Proteins - genetics Helminth Proteins - metabolism Markov processes Nematoda Physiological aspects Plant Cells - physiology Polysaccharide-Lyases - genetics Polysaccharide-Lyases - metabolism Termites Tylenchida - enzymology Tylenchida - genetics |
title | Genome wide comprehensive analysis and web resource development on cell wall degrading enzymes from phyto-parasitic nematodes |
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