Type IV pilin is glycosylated in Pseudomonas syringae pv. tabaci 6605 and is required for surface motility and virulence
SUMMARY Type IV pilin (PilA) is a major constituent of pilus and is required for bacterial biofilm formation, surface motility and virulence. It is known that mature PilA is produced by cleavage of the short leader sequence of the pilin precursor, followed by methylation of N‐terminal phenylalanine....
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| Veröffentlicht in: | Molecular plant pathology 2012-09, Vol.13 (7), p.764-774 |
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| creator | NGUYEN, LINH CHI TAGUCHI, FUMIKO TRAN, QUANG MINH NAITO, KANA YAMAMOTO, MASANOBU OHNISHI-KAMEYAMA, MAYUMI ONO, HIROSHI YOSHIDA, MITSURU CHIKU, KAZUHIRO ISHII, TADASHI INAGAKI, YOSHISHIGE TOYODA, KAZUHIRO SHIRAISHI, TOMONORI ICHINOSE, YUKI |
| description | SUMMARY
Type IV pilin (PilA) is a major constituent of pilus and is required for bacterial biofilm formation, surface motility and virulence. It is known that mature PilA is produced by cleavage of the short leader sequence of the pilin precursor, followed by methylation of N‐terminal phenylalanine. The molecular mass of the PilA mature protein from the tobacco bacterial pathogen Pseudomonas syringae pv. tabaci 6605 (Pta 6605) has been predicted to be 12 329 Da from its deduced amino acid sequence. Previously, we have detected PilA as an approximately 13‐kDa protein by immunoblot analysis with anti‐PilA‐specific antibody. In addition, we found the putative oligosaccharide‐transferase gene tfpO downstream of pilA. These findings suggest that PilA in Pta 6605 is glycosylated. The defective mutant of tfpO (ΔtfpO) shows reductions in pilin molecular mass, surface motility and virulence towards host tobacco plants. Thus, pilin glycan plays important roles in bacterial motility and virulence. The genetic region around pilA was compared among P. syringae pathovars. The tfpO gene exists in some strains of pathovars tabaci, syringae, lachrymans, mori, actinidiae, maculicola and P. savastanoi pv. savastanoi. However, some strains of pathovars tabaci, syringae, glycinea, tomato, aesculi and oryzae do not possess tfpO, and the existence of tfpO is independent of the classification of pathovars/strains in P. syringae. Interestingly, the PilA amino acid sequences in tfpO‐possessing strains show higher homology with each other than with tfpO‐nonpossessing strains. These results suggest that tfpO and pilA might co‐evolve in certain specific bacterial strains. |
| doi_str_mv | 10.1111/j.1364-3703.2012.00789.x |
| format | Article |
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Type IV pilin (PilA) is a major constituent of pilus and is required for bacterial biofilm formation, surface motility and virulence. It is known that mature PilA is produced by cleavage of the short leader sequence of the pilin precursor, followed by methylation of N‐terminal phenylalanine. The molecular mass of the PilA mature protein from the tobacco bacterial pathogen Pseudomonas syringae pv. tabaci 6605 (Pta 6605) has been predicted to be 12 329 Da from its deduced amino acid sequence. Previously, we have detected PilA as an approximately 13‐kDa protein by immunoblot analysis with anti‐PilA‐specific antibody. In addition, we found the putative oligosaccharide‐transferase gene tfpO downstream of pilA. These findings suggest that PilA in Pta 6605 is glycosylated. The defective mutant of tfpO (ΔtfpO) shows reductions in pilin molecular mass, surface motility and virulence towards host tobacco plants. Thus, pilin glycan plays important roles in bacterial motility and virulence. The genetic region around pilA was compared among P. syringae pathovars. The tfpO gene exists in some strains of pathovars tabaci, syringae, lachrymans, mori, actinidiae, maculicola and P. savastanoi pv. savastanoi. However, some strains of pathovars tabaci, syringae, glycinea, tomato, aesculi and oryzae do not possess tfpO, and the existence of tfpO is independent of the classification of pathovars/strains in P. syringae. Interestingly, the PilA amino acid sequences in tfpO‐possessing strains show higher homology with each other than with tfpO‐nonpossessing strains. These results suggest that tfpO and pilA might co‐evolve in certain specific bacterial strains.</description><identifier>ISSN: 1464-6722</identifier><identifier>EISSN: 1364-3703</identifier><identifier>DOI: 10.1111/j.1364-3703.2012.00789.x</identifier><identifier>PMID: 22353307</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino acid sequence ; Antibodies ; Bacterial Adhesion ; Bacterial plant pathogens ; Bacterial Proteins - metabolism ; Biofilms ; Biological and medical sciences ; Defective mutant ; Fimbriae Proteins - chemistry ; Fimbriae Proteins - genetics ; Fimbriae Proteins - metabolism ; Flagellin - metabolism ; Fundamental and applied biological sciences. Psychology ; Genes, Bacterial - genetics ; Glycosylation ; Homology ; Host plants ; Lycopersicon esculentum ; Methylation ; Molecular Sequence Data ; Motility ; Movement ; Mutation - genetics ; Nicotiana - virology ; Open Reading Frames - genetics ; Original ; Pathogens ; Phenylalanine ; Phylogeny ; Phytopathology. Animal pests. Plant and forest protection ; PilA protein ; pilin ; Polysaccharides ; Pseudomonas syringae ; Pseudomonas syringae - genetics ; Pseudomonas syringae - metabolism ; Pseudomonas syringae - pathogenicity ; Pseudomonas syringae - physiology ; Tobacco ; Virulence</subject><ispartof>Molecular plant pathology, 2012-09, Vol.13 (7), p.764-774</ispartof><rights>2012 The Authors. Molecular Plant Pathology © 2012 BSPP and Blackwell Publishing Ltd</rights><rights>2015 INIST-CNRS</rights><rights>2012 The Authors. Molecular Plant Pathology © 2012 BSPP and Blackwell Publishing Ltd.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6409-f64f1144f5b9ee84db2d1c96430db3813bbeb4ced35556ac7ec38468a2f56c473</citedby><cites>FETCH-LOGICAL-c6409-f64f1144f5b9ee84db2d1c96430db3813bbeb4ced35556ac7ec38468a2f56c473</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/PMC6638785/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6638785/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,724,777,781,882,1412,11543,27905,27906,45555,45556,46033,46457,53772,53774</link.rule.ids><linktorsrc>$$Uhttps://onlinelibrary.wiley.com/doi/abs/10.1111%2Fj.1364-3703.2012.00789.x$$EView_record_in_Wiley-Blackwell$$FView_record_in_$$GWiley-Blackwell</linktorsrc><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=26239245$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22353307$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>NGUYEN, LINH CHI</creatorcontrib><creatorcontrib>TAGUCHI, FUMIKO</creatorcontrib><creatorcontrib>TRAN, QUANG MINH</creatorcontrib><creatorcontrib>NAITO, KANA</creatorcontrib><creatorcontrib>YAMAMOTO, MASANOBU</creatorcontrib><creatorcontrib>OHNISHI-KAMEYAMA, MAYUMI</creatorcontrib><creatorcontrib>ONO, HIROSHI</creatorcontrib><creatorcontrib>YOSHIDA, MITSURU</creatorcontrib><creatorcontrib>CHIKU, KAZUHIRO</creatorcontrib><creatorcontrib>ISHII, TADASHI</creatorcontrib><creatorcontrib>INAGAKI, YOSHISHIGE</creatorcontrib><creatorcontrib>TOYODA, KAZUHIRO</creatorcontrib><creatorcontrib>SHIRAISHI, TOMONORI</creatorcontrib><creatorcontrib>ICHINOSE, YUKI</creatorcontrib><title>Type IV pilin is glycosylated in Pseudomonas syringae pv. tabaci 6605 and is required for surface motility and virulence</title><title>Molecular plant pathology</title><addtitle>Mol Plant Pathol</addtitle><description>SUMMARY
Type IV pilin (PilA) is a major constituent of pilus and is required for bacterial biofilm formation, surface motility and virulence. It is known that mature PilA is produced by cleavage of the short leader sequence of the pilin precursor, followed by methylation of N‐terminal phenylalanine. The molecular mass of the PilA mature protein from the tobacco bacterial pathogen Pseudomonas syringae pv. tabaci 6605 (Pta 6605) has been predicted to be 12 329 Da from its deduced amino acid sequence. Previously, we have detected PilA as an approximately 13‐kDa protein by immunoblot analysis with anti‐PilA‐specific antibody. In addition, we found the putative oligosaccharide‐transferase gene tfpO downstream of pilA. These findings suggest that PilA in Pta 6605 is glycosylated. The defective mutant of tfpO (ΔtfpO) shows reductions in pilin molecular mass, surface motility and virulence towards host tobacco plants. Thus, pilin glycan plays important roles in bacterial motility and virulence. The genetic region around pilA was compared among P. syringae pathovars. The tfpO gene exists in some strains of pathovars tabaci, syringae, lachrymans, mori, actinidiae, maculicola and P. savastanoi pv. savastanoi. However, some strains of pathovars tabaci, syringae, glycinea, tomato, aesculi and oryzae do not possess tfpO, and the existence of tfpO is independent of the classification of pathovars/strains in P. syringae. Interestingly, the PilA amino acid sequences in tfpO‐possessing strains show higher homology with each other than with tfpO‐nonpossessing strains. These results suggest that tfpO and pilA might co‐evolve in certain specific bacterial strains.</description><subject>Amino acid sequence</subject><subject>Antibodies</subject><subject>Bacterial Adhesion</subject><subject>Bacterial plant pathogens</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biofilms</subject><subject>Biological and medical sciences</subject><subject>Defective mutant</subject><subject>Fimbriae Proteins - chemistry</subject><subject>Fimbriae Proteins - genetics</subject><subject>Fimbriae Proteins - metabolism</subject><subject>Flagellin - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Bacterial - genetics</subject><subject>Glycosylation</subject><subject>Homology</subject><subject>Host plants</subject><subject>Lycopersicon esculentum</subject><subject>Methylation</subject><subject>Molecular Sequence Data</subject><subject>Motility</subject><subject>Movement</subject><subject>Mutation - genetics</subject><subject>Nicotiana - virology</subject><subject>Open Reading Frames - genetics</subject><subject>Original</subject><subject>Pathogens</subject><subject>Phenylalanine</subject><subject>Phylogeny</subject><subject>Phytopathology. Animal pests. Plant and forest protection</subject><subject>PilA protein</subject><subject>pilin</subject><subject>Polysaccharides</subject><subject>Pseudomonas syringae</subject><subject>Pseudomonas syringae - genetics</subject><subject>Pseudomonas syringae - metabolism</subject><subject>Pseudomonas syringae - pathogenicity</subject><subject>Pseudomonas syringae - physiology</subject><subject>Tobacco</subject><subject>Virulence</subject><issn>1464-6722</issn><issn>1364-3703</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUtv1DAUhSMEog_4C8gbJDYJfsV2JISEWhiKWphFgaXlODeDh0yS2sl08u9xOsMAO7zxle_5jo90kgQRnJF4Xq8zwgRPmcQso5jQDGOpimz3KDk9Lh7HmcdZSEpPkrMQ1hgTWdD8aXJCKcsZw_I02d1OPaCrb6h3jWuRC2jVTLYLU2MGqFB8WgYYq27TtSagMHnXrgygfpuhwZTGOiQEzpFpq5n1cDc6H7m68yiMvjYW0KYbovcwPYi2zo8NtBaeJU9q0wR4frjPk68f3t9efEyvvyyuLt5dp1ZwXKS14DUhnNd5WQAoXpW0IrYQnOGqZIqwsoSSW6hYnufCWAmWKS6UoXUuLJfsPHm79-3HcgOVhXbwptG9dxvjJ90Zp__dtO6HXnVbLQRTUuXR4NXBwHd3I4RBb1yw0DSmhW4MmmCmBJGMsihVe6n1XQge6uM3BOu5OL3Wcz967kfPxemH4vQuoi_-jnkEfzcVBS8PAhOsaWpvWuvCH52grKB8jvtmr7t3DUz_HUDfLJdxiHi6x10YYHfEjf-phWQy198_LyJ9c7kolNSf2C_vdsSk</recordid><startdate>201209</startdate><enddate>201209</enddate><creator>NGUYEN, LINH CHI</creator><creator>TAGUCHI, FUMIKO</creator><creator>TRAN, QUANG MINH</creator><creator>NAITO, KANA</creator><creator>YAMAMOTO, MASANOBU</creator><creator>OHNISHI-KAMEYAMA, MAYUMI</creator><creator>ONO, HIROSHI</creator><creator>YOSHIDA, MITSURU</creator><creator>CHIKU, KAZUHIRO</creator><creator>ISHII, TADASHI</creator><creator>INAGAKI, YOSHISHIGE</creator><creator>TOYODA, KAZUHIRO</creator><creator>SHIRAISHI, TOMONORI</creator><creator>ICHINOSE, YUKI</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>BSCLL</scope><scope>IQODW</scope><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>7QL</scope><scope>C1K</scope><scope>5PM</scope></search><sort><creationdate>201209</creationdate><title>Type IV pilin is glycosylated in Pseudomonas syringae pv. tabaci 6605 and is required for surface motility and virulence</title><author>NGUYEN, LINH CHI ; TAGUCHI, FUMIKO ; TRAN, QUANG MINH ; NAITO, KANA ; YAMAMOTO, MASANOBU ; OHNISHI-KAMEYAMA, MAYUMI ; ONO, HIROSHI ; YOSHIDA, MITSURU ; CHIKU, KAZUHIRO ; ISHII, TADASHI ; INAGAKI, YOSHISHIGE ; TOYODA, KAZUHIRO ; SHIRAISHI, TOMONORI ; ICHINOSE, YUKI</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6409-f64f1144f5b9ee84db2d1c96430db3813bbeb4ced35556ac7ec38468a2f56c473</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amino acid sequence</topic><topic>Antibodies</topic><topic>Bacterial Adhesion</topic><topic>Bacterial plant pathogens</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biofilms</topic><topic>Biological and medical sciences</topic><topic>Defective mutant</topic><topic>Fimbriae Proteins - chemistry</topic><topic>Fimbriae Proteins - genetics</topic><topic>Fimbriae Proteins - metabolism</topic><topic>Flagellin - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, Bacterial - genetics</topic><topic>Glycosylation</topic><topic>Homology</topic><topic>Host plants</topic><topic>Lycopersicon esculentum</topic><topic>Methylation</topic><topic>Molecular Sequence Data</topic><topic>Motility</topic><topic>Movement</topic><topic>Mutation - genetics</topic><topic>Nicotiana - virology</topic><topic>Open Reading Frames - genetics</topic><topic>Original</topic><topic>Pathogens</topic><topic>Phenylalanine</topic><topic>Phylogeny</topic><topic>Phytopathology. Animal pests. Plant and forest protection</topic><topic>PilA protein</topic><topic>pilin</topic><topic>Polysaccharides</topic><topic>Pseudomonas syringae</topic><topic>Pseudomonas syringae - genetics</topic><topic>Pseudomonas syringae - metabolism</topic><topic>Pseudomonas syringae - pathogenicity</topic><topic>Pseudomonas syringae - physiology</topic><topic>Tobacco</topic><topic>Virulence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>NGUYEN, LINH CHI</creatorcontrib><creatorcontrib>TAGUCHI, FUMIKO</creatorcontrib><creatorcontrib>TRAN, QUANG MINH</creatorcontrib><creatorcontrib>NAITO, KANA</creatorcontrib><creatorcontrib>YAMAMOTO, MASANOBU</creatorcontrib><creatorcontrib>OHNISHI-KAMEYAMA, MAYUMI</creatorcontrib><creatorcontrib>ONO, HIROSHI</creatorcontrib><creatorcontrib>YOSHIDA, MITSURU</creatorcontrib><creatorcontrib>CHIKU, KAZUHIRO</creatorcontrib><creatorcontrib>ISHII, TADASHI</creatorcontrib><creatorcontrib>INAGAKI, YOSHISHIGE</creatorcontrib><creatorcontrib>TOYODA, KAZUHIRO</creatorcontrib><creatorcontrib>SHIRAISHI, TOMONORI</creatorcontrib><creatorcontrib>ICHINOSE, YUKI</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular plant pathology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>NGUYEN, LINH CHI</au><au>TAGUCHI, FUMIKO</au><au>TRAN, QUANG MINH</au><au>NAITO, KANA</au><au>YAMAMOTO, MASANOBU</au><au>OHNISHI-KAMEYAMA, MAYUMI</au><au>ONO, HIROSHI</au><au>YOSHIDA, MITSURU</au><au>CHIKU, KAZUHIRO</au><au>ISHII, TADASHI</au><au>INAGAKI, YOSHISHIGE</au><au>TOYODA, KAZUHIRO</au><au>SHIRAISHI, TOMONORI</au><au>ICHINOSE, YUKI</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Type IV pilin is glycosylated in Pseudomonas syringae pv. tabaci 6605 and is required for surface motility and virulence</atitle><jtitle>Molecular plant pathology</jtitle><addtitle>Mol Plant Pathol</addtitle><date>2012-09</date><risdate>2012</risdate><volume>13</volume><issue>7</issue><spage>764</spage><epage>774</epage><pages>764-774</pages><issn>1464-6722</issn><eissn>1364-3703</eissn><abstract>SUMMARY
Type IV pilin (PilA) is a major constituent of pilus and is required for bacterial biofilm formation, surface motility and virulence. It is known that mature PilA is produced by cleavage of the short leader sequence of the pilin precursor, followed by methylation of N‐terminal phenylalanine. The molecular mass of the PilA mature protein from the tobacco bacterial pathogen Pseudomonas syringae pv. tabaci 6605 (Pta 6605) has been predicted to be 12 329 Da from its deduced amino acid sequence. Previously, we have detected PilA as an approximately 13‐kDa protein by immunoblot analysis with anti‐PilA‐specific antibody. In addition, we found the putative oligosaccharide‐transferase gene tfpO downstream of pilA. These findings suggest that PilA in Pta 6605 is glycosylated. The defective mutant of tfpO (ΔtfpO) shows reductions in pilin molecular mass, surface motility and virulence towards host tobacco plants. Thus, pilin glycan plays important roles in bacterial motility and virulence. The genetic region around pilA was compared among P. syringae pathovars. The tfpO gene exists in some strains of pathovars tabaci, syringae, lachrymans, mori, actinidiae, maculicola and P. savastanoi pv. savastanoi. However, some strains of pathovars tabaci, syringae, glycinea, tomato, aesculi and oryzae do not possess tfpO, and the existence of tfpO is independent of the classification of pathovars/strains in P. syringae. Interestingly, the PilA amino acid sequences in tfpO‐possessing strains show higher homology with each other than with tfpO‐nonpossessing strains. These results suggest that tfpO and pilA might co‐evolve in certain specific bacterial strains.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>22353307</pmid><doi>10.1111/j.1364-3703.2012.00789.x</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Molecular plant pathology, 2012-09, Vol.13 (7), p.764-774 |
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| subjects | Amino acid sequence Antibodies Bacterial Adhesion Bacterial plant pathogens Bacterial Proteins - metabolism Biofilms Biological and medical sciences Defective mutant Fimbriae Proteins - chemistry Fimbriae Proteins - genetics Fimbriae Proteins - metabolism Flagellin - metabolism Fundamental and applied biological sciences. Psychology Genes, Bacterial - genetics Glycosylation Homology Host plants Lycopersicon esculentum Methylation Molecular Sequence Data Motility Movement Mutation - genetics Nicotiana - virology Open Reading Frames - genetics Original Pathogens Phenylalanine Phylogeny Phytopathology. Animal pests. Plant and forest protection PilA protein pilin Polysaccharides Pseudomonas syringae Pseudomonas syringae - genetics Pseudomonas syringae - metabolism Pseudomonas syringae - pathogenicity Pseudomonas syringae - physiology Tobacco Virulence |
| title | Type IV pilin is glycosylated in Pseudomonas syringae pv. tabaci 6605 and is required for surface motility and virulence |
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