Analysis of a collagen-binding trimeric autotransporter adhesin from Mannheimia haemolytica A1
A locus that codes for a high-molecular-weight adhesin was previously isolated from Mannheimia haemolytica A1. In this study, we showed that this locus, named ahs, codes for two proteins (AhsA and AhsB) that exhibit characteristics of a trimeric autotransporter adhesin. Sequence analysis of AhsA sho...
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| Veröffentlicht in: | FEMS microbiology letters 2009-11, Vol.300 (2), p.242-248 |
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| creator | Daigneault, Michelle C Lo, Reggie Y.C |
| description | A locus that codes for a high-molecular-weight adhesin was previously isolated from Mannheimia haemolytica A1. In this study, we showed that this locus, named ahs, codes for two proteins (AhsA and AhsB) that exhibit characteristics of a trimeric autotransporter adhesin. Sequence analysis of AhsA showed the presence of 21 collagen-binding motifs in the protein. Collagen-binding assays showed that M. haemolytica A1 binds to collagen in a dose-dependent manner. This binding activity is trypsin sensitive and can be inhibited by anti-AhsA antibody. AhsB is the cognate transporter for AhsA. The C-terminal of AhsB showed highly conserved amino acids typical of trimeric autotransporters. Experimental data showed that the C-terminal 120 amino acids of AhsB could indeed form trimeric molecules. Western immunoblots showed the presence of anti-AhsA antibodies in the sera of calves that had been challenged with M. haemolytica A1, suggesting that AhsA is expressed and immunogenic in cattle. |
| doi_str_mv | 10.1111/j.1574-6968.2009.01786.x |
| format | Article |
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In this study, we showed that this locus, named ahs, codes for two proteins (AhsA and AhsB) that exhibit characteristics of a trimeric autotransporter adhesin. Sequence analysis of AhsA showed the presence of 21 collagen-binding motifs in the protein. Collagen-binding assays showed that M. haemolytica A1 binds to collagen in a dose-dependent manner. This binding activity is trypsin sensitive and can be inhibited by anti-AhsA antibody. AhsB is the cognate transporter for AhsA. The C-terminal of AhsB showed highly conserved amino acids typical of trimeric autotransporters. Experimental data showed that the C-terminal 120 amino acids of AhsB could indeed form trimeric molecules. Western immunoblots showed the presence of anti-AhsA antibodies in the sera of calves that had been challenged with M. haemolytica A1, suggesting that AhsA is expressed and immunogenic in cattle.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2009.01786.x</identifier><identifier>PMID: 19796136</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Oxford, UK : Blackwell Publishing Ltd</publisher><subject>adhesin ; Adhesins, Bacterial - genetics ; Adhesins, Bacterial - immunology ; Adhesins, Bacterial - metabolism ; Amino acids ; Animals ; Antibodies ; Antibodies, Bacterial - blood ; autotransporter ; Bacteriology ; Binding ; Binding Sites ; Biological and medical sciences ; Calves ; Cattle ; Collagen ; Collagen - metabolism ; collagen binding ; Conserved Sequence ; Fundamental and applied biological sciences. Psychology ; Immunogenicity ; Loci ; Mannheimia haemolytica ; Mannheimia haemolytica - genetics ; Mannheimia haemolytica - immunology ; Mannheimia haemolytica - metabolism ; Membrane Transport Proteins - genetics ; Membrane Transport Proteins - metabolism ; Microbiology ; Pasteurellaceae Infections - immunology ; Pasteurellaceae Infections - veterinary ; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains ; Protein Binding ; Protein Multimerization ; Proteins ; Sequence Analysis, DNA ; Trypsin</subject><ispartof>FEMS microbiology letters, 2009-11, Vol.300 (2), p.242-248</ispartof><rights>2009 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved 2009</rights><rights>2009 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5256-cd8fcf540348341ff362efa947f6740f96593a603aac5f9dfd6a08e6223ab5f33</citedby><cites>FETCH-LOGICAL-c5256-cd8fcf540348341ff362efa947f6740f96593a603aac5f9dfd6a08e6223ab5f33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.2009.01786.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2009.01786.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,778,782,1414,27911,27912,45561,45562</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22069521$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19796136$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Daigneault, Michelle C</creatorcontrib><creatorcontrib>Lo, Reggie Y.C</creatorcontrib><title>Analysis of a collagen-binding trimeric autotransporter adhesin from Mannheimia haemolytica A1</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>A locus that codes for a high-molecular-weight adhesin was previously isolated from Mannheimia haemolytica A1. In this study, we showed that this locus, named ahs, codes for two proteins (AhsA and AhsB) that exhibit characteristics of a trimeric autotransporter adhesin. Sequence analysis of AhsA showed the presence of 21 collagen-binding motifs in the protein. Collagen-binding assays showed that M. haemolytica A1 binds to collagen in a dose-dependent manner. This binding activity is trypsin sensitive and can be inhibited by anti-AhsA antibody. AhsB is the cognate transporter for AhsA. The C-terminal of AhsB showed highly conserved amino acids typical of trimeric autotransporters. Experimental data showed that the C-terminal 120 amino acids of AhsB could indeed form trimeric molecules. Western immunoblots showed the presence of anti-AhsA antibodies in the sera of calves that had been challenged with M. haemolytica A1, suggesting that AhsA is expressed and immunogenic in cattle.</description><subject>adhesin</subject><subject>Adhesins, Bacterial - genetics</subject><subject>Adhesins, Bacterial - immunology</subject><subject>Adhesins, Bacterial - metabolism</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antibodies, Bacterial - blood</subject><subject>autotransporter</subject><subject>Bacteriology</subject><subject>Binding</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Calves</subject><subject>Cattle</subject><subject>Collagen</subject><subject>Collagen - metabolism</subject><subject>collagen binding</subject><subject>Conserved Sequence</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Immunogenicity</subject><subject>Loci</subject><subject>Mannheimia haemolytica</subject><subject>Mannheimia haemolytica - genetics</subject><subject>Mannheimia haemolytica - immunology</subject><subject>Mannheimia haemolytica - metabolism</subject><subject>Membrane Transport Proteins - genetics</subject><subject>Membrane Transport Proteins - metabolism</subject><subject>Microbiology</subject><subject>Pasteurellaceae Infections - immunology</subject><subject>Pasteurellaceae Infections - veterinary</subject><subject>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</subject><subject>Protein Binding</subject><subject>Protein Multimerization</subject><subject>Proteins</subject><subject>Sequence Analysis, DNA</subject><subject>Trypsin</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</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>eNqNkc2O0zAUhS0EYkrhFcASAlYp_omdeDGLasQAUkcsYLZYt47dukriYidi-vY4pBokBAhvbMnf8T0-ByFMyYrm9fawoqIqC6lkvWKEqBWhVS1Xdw_Q4v7iIVoQXtUFJaq6QE9SOhBCSkbkY3RBVaUk5XKBvq57aE_JJxwcBmxC28LO9sXW943vd3iIvrPRGwzjEIYIfTqGONiIodnb5HvsYujwDfT93vrOA96D7UJ7GrwBvKZP0SMHbbLPzvsS3V6_-3L1odh8ev_xar0pjGBCFqapnXGiJLyseUmd45JZB6qsnKxK4pQUioMkHMAIpxrXSCC1lYxx2ArH-RK9md89xvBttGnQnU_G5s_0NoxJV5xLIkQlMvn6nySjTFKSxy3Ry9_AQxhjTisznEgmiOI0U_VMmRhSitbpY04M4klToqeu9EFPleipEj11pX92pe-y9Pl5wLjtbPNLeC4nA6_OACQDrcvpG5_uOZa7VIJNHi5n7rtv7em_Dejrm810yno-68N4_Iu6-JP9F7PKQdCwi9nZ7WdGKCdUKl4Lzn8AiDjHTw</recordid><startdate>200911</startdate><enddate>200911</enddate><creator>Daigneault, Michelle C</creator><creator>Lo, Reggie Y.C</creator><general>Oxford, UK : Blackwell Publishing Ltd</general><general>Blackwell Publishing Ltd</general><general>Wiley-Blackwell</general><general>Oxford University Press</general><scope>FBQ</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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</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>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7ST</scope><scope>SOI</scope><scope>7X8</scope></search><sort><creationdate>200911</creationdate><title>Analysis of a collagen-binding trimeric autotransporter adhesin from Mannheimia haemolytica A1</title><author>Daigneault, Michelle C ; Lo, Reggie Y.C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5256-cd8fcf540348341ff362efa947f6740f96593a603aac5f9dfd6a08e6223ab5f33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>adhesin</topic><topic>Adhesins, Bacterial - genetics</topic><topic>Adhesins, Bacterial - immunology</topic><topic>Adhesins, Bacterial - metabolism</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Antibodies, Bacterial - blood</topic><topic>autotransporter</topic><topic>Bacteriology</topic><topic>Binding</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Calves</topic><topic>Cattle</topic><topic>Collagen</topic><topic>Collagen - metabolism</topic><topic>collagen binding</topic><topic>Conserved Sequence</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Immunogenicity</topic><topic>Loci</topic><topic>Mannheimia haemolytica</topic><topic>Mannheimia haemolytica - genetics</topic><topic>Mannheimia haemolytica - immunology</topic><topic>Mannheimia haemolytica - metabolism</topic><topic>Membrane Transport Proteins - genetics</topic><topic>Membrane Transport Proteins - metabolism</topic><topic>Microbiology</topic><topic>Pasteurellaceae Infections - immunology</topic><topic>Pasteurellaceae Infections - veterinary</topic><topic>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</topic><topic>Protein Binding</topic><topic>Protein Multimerization</topic><topic>Proteins</topic><topic>Sequence Analysis, DNA</topic><topic>Trypsin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Daigneault, Michelle C</creatorcontrib><creatorcontrib>Lo, Reggie Y.C</creatorcontrib><collection>AGRIS</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>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</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>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</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>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Daigneault, Michelle C</au><au>Lo, Reggie Y.C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of a collagen-binding trimeric autotransporter adhesin from Mannheimia haemolytica A1</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2009-11</date><risdate>2009</risdate><volume>300</volume><issue>2</issue><spage>242</spage><epage>248</epage><pages>242-248</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>A locus that codes for a high-molecular-weight adhesin was previously isolated from Mannheimia haemolytica A1. In this study, we showed that this locus, named ahs, codes for two proteins (AhsA and AhsB) that exhibit characteristics of a trimeric autotransporter adhesin. Sequence analysis of AhsA showed the presence of 21 collagen-binding motifs in the protein. Collagen-binding assays showed that M. haemolytica A1 binds to collagen in a dose-dependent manner. This binding activity is trypsin sensitive and can be inhibited by anti-AhsA antibody. AhsB is the cognate transporter for AhsA. The C-terminal of AhsB showed highly conserved amino acids typical of trimeric autotransporters. Experimental data showed that the C-terminal 120 amino acids of AhsB could indeed form trimeric molecules. Western immunoblots showed the presence of anti-AhsA antibodies in the sera of calves that had been challenged with M. haemolytica A1, suggesting that AhsA is expressed and immunogenic in cattle.</abstract><cop>Oxford, UK</cop><pub>Oxford, UK : Blackwell Publishing Ltd</pub><pmid>19796136</pmid><doi>10.1111/j.1574-6968.2009.01786.x</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 2009-11, Vol.300 (2), p.242-248 |
| issn | 0378-1097 1574-6968 |
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| subjects | adhesin Adhesins, Bacterial - genetics Adhesins, Bacterial - immunology Adhesins, Bacterial - metabolism Amino acids Animals Antibodies Antibodies, Bacterial - blood autotransporter Bacteriology Binding Binding Sites Biological and medical sciences Calves Cattle Collagen Collagen - metabolism collagen binding Conserved Sequence Fundamental and applied biological sciences. Psychology Immunogenicity Loci Mannheimia haemolytica Mannheimia haemolytica - genetics Mannheimia haemolytica - immunology Mannheimia haemolytica - metabolism Membrane Transport Proteins - genetics Membrane Transport Proteins - metabolism Microbiology Pasteurellaceae Infections - immunology Pasteurellaceae Infections - veterinary Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Protein Binding Protein Multimerization Proteins Sequence Analysis, DNA Trypsin |
| title | Analysis of a collagen-binding trimeric autotransporter adhesin from Mannheimia haemolytica A1 |
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