The HrpW protein of Lonsdalea quercina N-5-1 has pectate lyase activity and is required for full bacterial virulence.
Identifieur interne : 002019 ( Main/Exploration ); précédent : 002018; suivant : 002020The HrpW protein of Lonsdalea quercina N-5-1 has pectate lyase activity and is required for full bacterial virulence.
Auteurs : Li Yang [République populaire de Chine] ; Bochao Xu ; Wei He ; Liqun ZhangSource :
- Journal of basic microbiology [ 1521-4028 ] ; 2014.
Descripteurs français
- KwdFr :
- Chine (MeSH), Enterobacteriaceae (enzymologie), Enterobacteriaceae (pathogénicité), Gènes bactériens (MeSH), Maladies des plantes (microbiologie), Polysaccharide-lyases (composition chimique), Polysaccharide-lyases (génétique), Polysaccharide-lyases (métabolisme), Populus (microbiologie), Protéines bactériennes (composition chimique), Protéines bactériennes (génétique), Protéines bactériennes (métabolisme), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Virulence (MeSH).
- MESH :
- composition chimique : Polysaccharide-lyases, Protéines bactériennes.
- enzymologie : Enterobacteriaceae.
- génétique : Polysaccharide-lyases, Protéines bactériennes.
- microbiologie : Maladies des plantes, Populus.
- métabolisme : Polysaccharide-lyases, Protéines bactériennes.
- pathogénicité : Enterobacteriaceae.
- Chine, Gènes bactériens, Similitude de séquences d'acides aminés, Séquence d'acides aminés, Virulence.
- Wicri :
- geographic : République populaire de Chine.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Bacterial Proteins (chemistry), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), China (MeSH), Enterobacteriaceae (enzymology), Enterobacteriaceae (pathogenicity), Genes, Bacterial (MeSH), Plant Diseases (microbiology), Polysaccharide-Lyases (chemistry), Polysaccharide-Lyases (genetics), Polysaccharide-Lyases (metabolism), Populus (microbiology), Sequence Homology, Amino Acid (MeSH), Virulence (MeSH).
- MESH :
- chemical , chemistry : Bacterial Proteins, Polysaccharide-Lyases.
- chemical , genetics : Bacterial Proteins, Polysaccharide-Lyases.
- chemical , metabolism : Bacterial Proteins, Polysaccharide-Lyases.
- geographic : China.
- enzymology : Enterobacteriaceae.
- microbiology : Plant Diseases, Populus.
- pathogenicity : Enterobacteriaceae.
- Amino Acid Sequence, Genes, Bacterial, Sequence Homology, Amino Acid, Virulence.
Abstract
Lonsdalea quercina N-5-1 is a bacterial pathogen that causes poplar bark cankers. It has been isolated from the branch of Populus × euramericana cv. "74/76" in Henan, China. Previous studies have revealed that the Type III secretion system (T3SS) acts as an essential pathogenic factor in L. quercina N-5-1. HrpW is a putative effector of T3SS in strain N-5-1, which has a typical harpin domain at the amino terminal and a pectate lyase (Pel) domain at its carboxyl terminal. Genetic evidence had shown that, compared to the wild-type and the complementary strain, the hrpW mutation causes a small but significant reduction in virulence when inoculated on the poplar branches. The amino terminal domain of HrpW was found to trigger tobacco hypersensitive response, but the carboxyl terminal domain of HrpW was not. Unlike most HrpW homologs in other bacteria, the carboxyl terminal domain of HrpW of strain N-5-1 exhibited detectable pectate lyase activity. Site-direction mutations (W104A, W171M) further demonstrated that two tryptophan residues were essential to its pectate lyase activity. The results of the present work suggest that HrpW in L. quercina N-5-1 possesses pectate lyase activity and acts as a nonessential but important pathogenic factor in poplar bark canker disease.
DOI: 10.1002/jobm.201300342
PubMed: 24395334
Affiliations:
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Yang</name><affiliation wicri:level="1"><nlm:affiliation>The Key Laboratory for Silviculture and Conservation of Ministry of Education, Beijing Forestry University, Beijing, 100083, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>The Key Laboratory for Silviculture and Conservation of Ministry of Education, Beijing Forestry University, Beijing, 100083</wicri:regionArea><wicri:noRegion>100083</wicri:noRegion></affiliation></author><author><name sortKey="Xu, Bochao" sort="Xu, Bochao" uniqKey="Xu B" first="Bochao" last="Xu">Bochao Xu</name></author><author><name sortKey="He, Wei" sort="He, Wei" uniqKey="He W" first="Wei" last="He">Wei He</name></author><author><name sortKey="Zhang, Liqun" sort="Zhang, Liqun" uniqKey="Zhang L" first="Liqun" last="Zhang">Liqun Zhang</name></author></analytic><series><title level="j">Journal of basic microbiology</title><idno type="eISSN">1521-4028</idno><imprint><date when="2014" 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(microbiologie)</term><term>Polysaccharide-lyases (composition chimique)</term><term>Polysaccharide-lyases (génétique)</term><term>Polysaccharide-lyases (métabolisme)</term><term>Populus (microbiologie)</term><term>Protéines bactériennes (composition chimique)</term><term>Protéines bactériennes (génétique)</term><term>Protéines bactériennes (métabolisme)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Virulence (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term><term>Polysaccharide-Lyases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Bacterial Proteins</term><term>Polysaccharide-Lyases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>Polysaccharide-Lyases</term></keywords><keywords scheme="MESH" 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xml:lang="en"><term>Enterobacteriaceae</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Enterobacteriaceae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Genes, Bacterial</term><term>Sequence Homology, Amino Acid</term><term>Virulence</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chine</term><term>Gènes bactériens</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term><term>Virulence</term></keywords><keywords scheme="Wicri" type="geographic" xml:lang="fr"><term>République populaire de Chine</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lonsdalea quercina N-5-1 is a bacterial pathogen that causes poplar bark cankers. It has been isolated from the branch of Populus × euramericana cv. "74/76" in Henan, China. Previous studies have revealed that the Type III secretion system (T3SS) acts as an essential pathogenic factor in L. quercina N-5-1. HrpW is a putative effector of T3SS in strain N-5-1, which has a typical harpin domain at the amino terminal and a pectate lyase (Pel) domain at its carboxyl terminal. Genetic evidence had shown that, compared to the wild-type and the complementary strain, the hrpW mutation causes a small but significant reduction in virulence when inoculated on the poplar branches. The amino terminal domain of HrpW was found to trigger tobacco hypersensitive response, but the carboxyl terminal domain of HrpW was not. Unlike most HrpW homologs in other bacteria, the carboxyl terminal domain of HrpW of strain N-5-1 exhibited detectable pectate lyase activity. Site-direction mutations (W104A, W171M) further demonstrated that two tryptophan residues were essential to its pectate lyase activity. The results of the present work suggest that HrpW in L. quercina N-5-1 possesses pectate lyase activity and acts as a nonessential but important pathogenic factor in poplar bark canker disease.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24395334</PMID><DateCompleted><Year>2015</Year><Month>06</Month><Day>11</Day></DateCompleted><DateRevised><Year>2014</Year><Month>10</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1521-4028</ISSN><JournalIssue CitedMedium="Internet"><Volume>54</Volume><Issue>10</Issue><PubDate><Year>2014</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Journal of basic microbiology</Title><ISOAbbreviation>J Basic Microbiol</ISOAbbreviation></Journal><ArticleTitle>The HrpW protein of Lonsdalea quercina N-5-1 has pectate lyase activity and is required for full bacterial virulence.</ArticleTitle><Pagination><MedlinePgn>1126-35</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/jobm.201300342</ELocationID><Abstract><AbstractText>Lonsdalea quercina N-5-1 is a bacterial pathogen that causes poplar bark cankers. It has been isolated from the branch of Populus × euramericana cv. "74/76" in Henan, China. Previous studies have revealed that the Type III secretion system (T3SS) acts as an essential pathogenic factor in L. quercina N-5-1. HrpW is a putative effector of T3SS in strain N-5-1, which has a typical harpin domain at the amino terminal and a pectate lyase (Pel) domain at its carboxyl terminal. Genetic evidence had shown that, compared to the wild-type and the complementary strain, the hrpW mutation causes a small but significant reduction in virulence when inoculated on the poplar branches. The amino terminal domain of HrpW was found to trigger tobacco hypersensitive response, but the carboxyl terminal domain of HrpW was not. Unlike most HrpW homologs in other bacteria, the carboxyl terminal domain of HrpW of strain N-5-1 exhibited detectable pectate lyase activity. Site-direction mutations (W104A, W171M) further demonstrated that two tryptophan residues were essential to its pectate lyase activity. The results of the present work suggest that HrpW in L. quercina N-5-1 possesses pectate lyase activity and acts as a nonessential but important pathogenic factor in poplar bark canker disease.</AbstractText><CopyrightInformation>© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Li</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>The Key Laboratory for Silviculture and Conservation of Ministry of Education, Beijing Forestry University, Beijing, 100083, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Xu</LastName><ForeName>Bochao</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>He</LastName><ForeName>Wei</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Liqun</ForeName><Initials>L</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>01</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>J Basic Microbiol</MedlineTA><NlmUniqueID>8503885</NlmUniqueID><ISSNLinking>0233-111X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.2.-</RegistryNumber><NameOfSubstance UI="D011133">Polysaccharide-Lyases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.2.2</RegistryNumber><NameOfSubstance UI="C023911">pectate lyase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002681" MajorTopicYN="N" Type="Geographic">China</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004755" MajorTopicYN="N">Enterobacteriaceae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005798" MajorTopicYN="N">Genes, Bacterial</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011133" MajorTopicYN="N">Polysaccharide-Lyases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014774" MajorTopicYN="N">Virulence</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Bark canker</Keyword><Keyword MajorTopicYN="N">Harpin</Keyword><Keyword MajorTopicYN="N">T3SS</Keyword><Keyword MajorTopicYN="N">hrpW</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>04</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>11</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>1</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>1</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>6</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24395334</ArticleId><ArticleId IdType="doi">10.1002/jobm.201300342</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><noCountry><name sortKey="He, Wei" sort="He, Wei" uniqKey="He W" first="Wei" last="He">Wei He</name><name sortKey="Xu, Bochao" sort="Xu, Bochao" uniqKey="Xu B" first="Bochao" last="Xu">Bochao Xu</name><name sortKey="Zhang, Liqun" sort="Zhang, Liqun" uniqKey="Zhang L" first="Liqun" last="Zhang">Liqun Zhang</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Yang, Li" sort="Yang, Li" uniqKey="Yang L" first="Li" last="Yang">Li Yang</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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