Evidence for a system of general protein glycosylation in Campylobacter jejuni
A genetic locus from Campylobacter jejuni 81‐176 (O:23, 36) has been characterized that appears to be involved in glycosylation of multiple proteins, including flagellin. The lipopolysaccharide (LPS) core of Escherichia coli DH5α containing some of these genes is modified such that it becomes immuno...
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| Veröffentlicht in: | Molecular microbiology 1999-06, Vol.32 (5), p.1022-1030 |
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| creator | Szymanski, Christine M. Yao, Ruijin Ewing, Cheryl P. Trust, Trevor J. Guerry, Patricia |
| description | A genetic locus from Campylobacter jejuni 81‐176 (O:23, 36) has been characterized that appears to be involved in glycosylation of multiple proteins, including flagellin. The lipopolysaccharide (LPS) core of Escherichia coli DH5α containing some of these genes is modified such that it becomes immunoreactive with O:23 and O:36 antisera and loses reactivity with the lectin wheat germ agglutinin (WGA). Site‐specific mutation of one of these genes in the E. coli host causes loss of O:23 and O:36 antibody reactivity and restores reactivity with WGA. However, site‐specific mutation of each of the seven genes in 81‐176 failed to show any detectable changes in LPS. Multiple proteins from various cellular fractions of each mutant showed altered reactivity by Western blot analyses using O:23 and O:36 antisera. The changes in protein antigenicity could be restored in one of the mutants by the presence of the corresponding wild‐type allele in trans on a shuttle vector. Flagellin, which is known to be a glycoprotein, was one of the proteins that showed altered reactivity with O:23 and O:36 antiserum in the mutants. Chemical deglycosylation of protein fractions from the 81‐176 wild type suggests that the other proteins with altered antigenicity in the mutants are also glycosylated. |
| doi_str_mv | 10.1046/j.1365-2958.1999.01415.x |
| format | Article |
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The lipopolysaccharide (LPS) core of Escherichia coli DH5α containing some of these genes is modified such that it becomes immunoreactive with O:23 and O:36 antisera and loses reactivity with the lectin wheat germ agglutinin (WGA). Site‐specific mutation of one of these genes in the E. coli host causes loss of O:23 and O:36 antibody reactivity and restores reactivity with WGA. However, site‐specific mutation of each of the seven genes in 81‐176 failed to show any detectable changes in LPS. Multiple proteins from various cellular fractions of each mutant showed altered reactivity by Western blot analyses using O:23 and O:36 antisera. The changes in protein antigenicity could be restored in one of the mutants by the presence of the corresponding wild‐type allele in trans on a shuttle vector. Flagellin, which is known to be a glycoprotein, was one of the proteins that showed altered reactivity with O:23 and O:36 antiserum in the mutants. Chemical deglycosylation of protein fractions from the 81‐176 wild type suggests that the other proteins with altered antigenicity in the mutants are also glycosylated.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1046/j.1365-2958.1999.01415.x</identifier><identifier>PMID: 10361304</identifier><language>eng</language><publisher>Oxford BSL: Blackwell Science Ltd</publisher><subject>Antigens, Bacterial - immunology ; Bacterial Proteins - genetics ; Bacterial Proteins - immunology ; Bacterial Proteins - metabolism ; Campylobacter jejuni ; Campylobacter jejuni - genetics ; Campylobacter jejuni - immunology ; Campylobacter jejuni - metabolism ; DNA, Bacterial - chemistry ; DNA, Bacterial - genetics ; Enzyme-Linked Immunosorbent Assay ; Escherichia coli ; Flagellin - genetics ; Flagellin - metabolism ; Genes, Bacterial ; Glycosylation ; Immunoblotting ; Lipopolysaccharides - immunology ; Lipopolysaccharides - isolation & purification ; Lipopolysaccharides - metabolism ; Membrane Proteins - genetics ; Membrane Proteins - immunology ; Membrane Proteins - metabolism ; Molecular Sequence Data ; Mutation ; Plasmids - genetics ; Reverse Transcriptase Polymerase Chain Reaction - methods ; Sequence Analysis, DNA ; Wheat Germ Agglutinins - metabolism</subject><ispartof>Molecular microbiology, 1999-06, Vol.32 (5), p.1022-1030</ispartof><rights>Blackwell Science Ltd, Oxford</rights><rights>Copyright Blackwell Scientific Publications Ltd. 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The lipopolysaccharide (LPS) core of Escherichia coli DH5α containing some of these genes is modified such that it becomes immunoreactive with O:23 and O:36 antisera and loses reactivity with the lectin wheat germ agglutinin (WGA). Site‐specific mutation of one of these genes in the E. coli host causes loss of O:23 and O:36 antibody reactivity and restores reactivity with WGA. However, site‐specific mutation of each of the seven genes in 81‐176 failed to show any detectable changes in LPS. Multiple proteins from various cellular fractions of each mutant showed altered reactivity by Western blot analyses using O:23 and O:36 antisera. The changes in protein antigenicity could be restored in one of the mutants by the presence of the corresponding wild‐type allele in trans on a shuttle vector. Flagellin, which is known to be a glycoprotein, was one of the proteins that showed altered reactivity with O:23 and O:36 antiserum in the mutants. Chemical deglycosylation of protein fractions from the 81‐176 wild type suggests that the other proteins with altered antigenicity in the mutants are also glycosylated.</description><subject>Antigens, Bacterial - immunology</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - immunology</subject><subject>Bacterial Proteins - metabolism</subject><subject>Campylobacter jejuni</subject><subject>Campylobacter jejuni - genetics</subject><subject>Campylobacter jejuni - immunology</subject><subject>Campylobacter jejuni - metabolism</subject><subject>DNA, Bacterial - chemistry</subject><subject>DNA, Bacterial - genetics</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Escherichia coli</subject><subject>Flagellin - genetics</subject><subject>Flagellin - metabolism</subject><subject>Genes, Bacterial</subject><subject>Glycosylation</subject><subject>Immunoblotting</subject><subject>Lipopolysaccharides - immunology</subject><subject>Lipopolysaccharides - isolation & purification</subject><subject>Lipopolysaccharides - metabolism</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - immunology</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Plasmids - genetics</subject><subject>Reverse Transcriptase Polymerase Chain Reaction - methods</subject><subject>Sequence Analysis, DNA</subject><subject>Wheat Germ Agglutinins - metabolism</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkcFO3DAQhq2qVdlCXwFZPfSW1GPHTnzgUK2AIgG9gMTNcpIJSpTEi50Aefs6LKoqLuXk0fibXzP6CKHAUmCZ-tGlIJRMuJZFClrrlEEGMn3-QDZ_Pz6SDdOSJaLgdwfkSwgdYyCYEp_JATChYp1tyPXpY1vjWCFtnKeWhiVMOFDX0Hsc0due7rybsB3pfb9ULiy9nVo30tjY2mG39K601YSedtjNY3tEPjW2D_j19T0kt2enN9tfyeXv84vtz8ukygotk1KWDWJhGWOYi9piUYPiBfDYs01d1axWObeWlzVgbktVirhxJgGwQqFzcUi-73Pjdg8zhskMbaiw7-2Ibg5G6RjGxP9ByHkmC80j-O0N2LnZj_EIA1pJkMBFhIo9VHkXgsfG7Hw7WL8YYGY1YzqzCjCrALOaMS9mzHMcPX7Nn8sB638G9yoicLIHntoel3cHm6uri7USfwBuG50F</recordid><startdate>199906</startdate><enddate>199906</enddate><creator>Szymanski, Christine M.</creator><creator>Yao, Ruijin</creator><creator>Ewing, Cheryl P.</creator><creator>Trust, Trevor J.</creator><creator>Guerry, Patricia</creator><general>Blackwell Science Ltd</general><general>Blackwell Publishing Ltd</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>199906</creationdate><title>Evidence for a system of general protein glycosylation in Campylobacter jejuni</title><author>Szymanski, Christine M. ; Yao, Ruijin ; Ewing, Cheryl P. ; Trust, Trevor J. ; Guerry, Patricia</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4895-b5bfee8a000e73dae8d162812e8aafdcd0d672aa2bd1e7ab6b30364511ece3973</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Antigens, Bacterial - immunology</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - immunology</topic><topic>Bacterial Proteins - metabolism</topic><topic>Campylobacter jejuni</topic><topic>Campylobacter jejuni - genetics</topic><topic>Campylobacter jejuni - immunology</topic><topic>Campylobacter jejuni - metabolism</topic><topic>DNA, Bacterial - chemistry</topic><topic>DNA, Bacterial - genetics</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Escherichia coli</topic><topic>Flagellin - genetics</topic><topic>Flagellin - metabolism</topic><topic>Genes, Bacterial</topic><topic>Glycosylation</topic><topic>Immunoblotting</topic><topic>Lipopolysaccharides - immunology</topic><topic>Lipopolysaccharides - isolation & purification</topic><topic>Lipopolysaccharides - metabolism</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - immunology</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Plasmids - genetics</topic><topic>Reverse Transcriptase Polymerase Chain Reaction - methods</topic><topic>Sequence Analysis, DNA</topic><topic>Wheat Germ Agglutinins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Szymanski, Christine M.</creatorcontrib><creatorcontrib>Yao, Ruijin</creatorcontrib><creatorcontrib>Ewing, Cheryl P.</creatorcontrib><creatorcontrib>Trust, Trevor J.</creatorcontrib><creatorcontrib>Guerry, Patricia</creatorcontrib><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>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Szymanski, Christine M.</au><au>Yao, Ruijin</au><au>Ewing, Cheryl P.</au><au>Trust, Trevor J.</au><au>Guerry, Patricia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence for a system of general protein glycosylation in Campylobacter jejuni</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>1999-06</date><risdate>1999</risdate><volume>32</volume><issue>5</issue><spage>1022</spage><epage>1030</epage><pages>1022-1030</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>A genetic locus from Campylobacter jejuni 81‐176 (O:23, 36) has been characterized that appears to be involved in glycosylation of multiple proteins, including flagellin. The lipopolysaccharide (LPS) core of Escherichia coli DH5α containing some of these genes is modified such that it becomes immunoreactive with O:23 and O:36 antisera and loses reactivity with the lectin wheat germ agglutinin (WGA). Site‐specific mutation of one of these genes in the E. coli host causes loss of O:23 and O:36 antibody reactivity and restores reactivity with WGA. However, site‐specific mutation of each of the seven genes in 81‐176 failed to show any detectable changes in LPS. Multiple proteins from various cellular fractions of each mutant showed altered reactivity by Western blot analyses using O:23 and O:36 antisera. The changes in protein antigenicity could be restored in one of the mutants by the presence of the corresponding wild‐type allele in trans on a shuttle vector. Flagellin, which is known to be a glycoprotein, was one of the proteins that showed altered reactivity with O:23 and O:36 antiserum in the mutants. Chemical deglycosylation of protein fractions from the 81‐176 wild type suggests that the other proteins with altered antigenicity in the mutants are also glycosylated.</abstract><cop>Oxford BSL</cop><pub>Blackwell Science Ltd</pub><pmid>10361304</pmid><doi>10.1046/j.1365-2958.1999.01415.x</doi><tpages>9</tpages></addata></record> |
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| ispartof | Molecular microbiology, 1999-06, Vol.32 (5), p.1022-1030 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Free Content; Free Full-Text Journals in Chemistry |
| subjects | Antigens, Bacterial - immunology Bacterial Proteins - genetics Bacterial Proteins - immunology Bacterial Proteins - metabolism Campylobacter jejuni Campylobacter jejuni - genetics Campylobacter jejuni - immunology Campylobacter jejuni - metabolism DNA, Bacterial - chemistry DNA, Bacterial - genetics Enzyme-Linked Immunosorbent Assay Escherichia coli Flagellin - genetics Flagellin - metabolism Genes, Bacterial Glycosylation Immunoblotting Lipopolysaccharides - immunology Lipopolysaccharides - isolation & purification Lipopolysaccharides - metabolism Membrane Proteins - genetics Membrane Proteins - immunology Membrane Proteins - metabolism Molecular Sequence Data Mutation Plasmids - genetics Reverse Transcriptase Polymerase Chain Reaction - methods Sequence Analysis, DNA Wheat Germ Agglutinins - metabolism |
| title | Evidence for a system of general protein glycosylation in Campylobacter jejuni |
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