Antigenic cross-reactivity and sequence homology between Actinobacillus actinomycetemcomitans GroEL protein and human fibronectin
The immunologic cross‐reactivity between human fibronectin and Actinobacillus actinomycetemcomitans GroEL was examined. Analyses by SDS‐PAGE/Western immunoblotting and ELISA showed that a polyclonal antibody directed against the purified GroEL protein of A. actinomycetemcomitans, but not against the...
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description | The immunologic cross‐reactivity between human fibronectin and Actinobacillus actinomycetemcomitans GroEL was examined. Analyses by SDS‐PAGE/Western immunoblotting and ELISA showed that a polyclonal antibody directed against the purified GroEL protein of A. actinomycetemcomitans, but not against the Escherichia coli GroEL, cross‐reacts with human fibronectin. No antigenic cross‐reactivity was observed between anti‐A. actinomycetemcomitans GroEL antibody and type IV collagen, another important constituent of the basement membrane. A comparative analysis of the amino acid sequences of A. actinomycetemcomitans GroEL and human fibronectin revealed eight instances of four‐amino acid sequence homology between the two proteins. Six of these tetrapeptide sequences were also shared with E. coli GroEL, suggesting that the remaining two tetrapeptides, GQLI (Glycine‐Glutamine‐Leucine‐Isoleucine) and TGLE (Threonine‐Glycine‐Leucine‐Glutamic acid), may be associated with the epitope that the anti‐A. actinomycetemcomitans GroEL antibody specifically recognizes. Reactivity between TGLE, but not GQLI, with anti‐A. actinomycetemcomitans GroEL antibody was confirmed by a biospecific interaction analysis using a biosensor technology. Although additional investigations are required, the observed phenomenon may lead to an autoimmune response and thus contribute to tissue destruction during periodontitis. |
doi_str_mv | 10.1111/j.0902-0055.2003.00125.x |
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Analyses by SDS‐PAGE/Western immunoblotting and ELISA showed that a polyclonal antibody directed against the purified GroEL protein of A. actinomycetemcomitans, but not against the Escherichia coli GroEL, cross‐reacts with human fibronectin. No antigenic cross‐reactivity was observed between anti‐A. actinomycetemcomitans GroEL antibody and type IV collagen, another important constituent of the basement membrane. A comparative analysis of the amino acid sequences of A. actinomycetemcomitans GroEL and human fibronectin revealed eight instances of four‐amino acid sequence homology between the two proteins. Six of these tetrapeptide sequences were also shared with E. coli GroEL, suggesting that the remaining two tetrapeptides, GQLI (Glycine‐Glutamine‐Leucine‐Isoleucine) and TGLE (Threonine‐Glycine‐Leucine‐Glutamic acid), may be associated with the epitope that the anti‐A. actinomycetemcomitans GroEL antibody specifically recognizes. Reactivity between TGLE, but not GQLI, with anti‐A. actinomycetemcomitans GroEL antibody was confirmed by a biospecific interaction analysis using a biosensor technology. Although additional investigations are required, the observed phenomenon may lead to an autoimmune response and thus contribute to tissue destruction during periodontitis.</description><identifier>ISSN: 0902-0055</identifier><identifier>EISSN: 1399-302X</identifier><identifier>DOI: 10.1111/j.0902-0055.2003.00125.x</identifier><identifier>PMID: 14871354</identifier><identifier>CODEN: OMIMEE</identifier><language>eng</language><publisher>Oxford UK: Munksgaard International Publishers</publisher><subject>Actinobacillus actinomycetemcomitans ; Aggregatibacter actinomycetemcomitans - immunology ; Antibodies, Bacterial - immunology ; Antibodies, Bispecific - immunology ; Antibody Specificity - immunology ; Antigens, Bacterial - immunology ; Bacteriology ; Biological and medical sciences ; Chaperonin 60 - analysis ; Chaperonin 60 - immunology ; Collagen Type IV - immunology ; Cross Reactions - immunology ; Dentistry ; Epitopes - immunology ; Escherichia coli ; Escherichia coli - immunology ; fibronectin ; Fibronectins - immunology ; Fundamental and applied biological sciences. Psychology ; Glutamic Acid - analysis ; Glutamine - analysis ; Glycine - analysis ; GroEL ; heat shock protein ; Humans ; Isoleucine - analysis ; Leucine - analysis ; Microbiology ; Miscellaneous ; periodontitis ; Sequence Homology, Amino Acid ; Threonine - analysis</subject><ispartof>Oral microbiology and immunology, 2004-04, Vol.19 (2), p.124-128</ispartof><rights>2004 INIST-CNRS</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4635-7cc929a76286539a67c43fcb32541f840e692e39b5886e658625a315ecc9dda23</citedby><cites>FETCH-LOGICAL-c4635-7cc929a76286539a67c43fcb32541f840e692e39b5886e658625a315ecc9dda23</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.0902-0055.2003.00125.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.0902-0055.2003.00125.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15513771$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14871354$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yoshioka, M.</creatorcontrib><creatorcontrib>Grenier, D.</creatorcontrib><creatorcontrib>Hinode, D.</creatorcontrib><creatorcontrib>Fukui, M.</creatorcontrib><creatorcontrib>Mayrand, D.</creatorcontrib><title>Antigenic cross-reactivity and sequence homology between Actinobacillus actinomycetemcomitans GroEL protein and human fibronectin</title><title>Oral microbiology and immunology</title><addtitle>Oral Microbiol Immunol</addtitle><description>The immunologic cross‐reactivity between human fibronectin and Actinobacillus actinomycetemcomitans GroEL was examined. Analyses by SDS‐PAGE/Western immunoblotting and ELISA showed that a polyclonal antibody directed against the purified GroEL protein of A. actinomycetemcomitans, but not against the Escherichia coli GroEL, cross‐reacts with human fibronectin. No antigenic cross‐reactivity was observed between anti‐A. actinomycetemcomitans GroEL antibody and type IV collagen, another important constituent of the basement membrane. A comparative analysis of the amino acid sequences of A. actinomycetemcomitans GroEL and human fibronectin revealed eight instances of four‐amino acid sequence homology between the two proteins. Six of these tetrapeptide sequences were also shared with E. coli GroEL, suggesting that the remaining two tetrapeptides, GQLI (Glycine‐Glutamine‐Leucine‐Isoleucine) and TGLE (Threonine‐Glycine‐Leucine‐Glutamic acid), may be associated with the epitope that the anti‐A. actinomycetemcomitans GroEL antibody specifically recognizes. Reactivity between TGLE, but not GQLI, with anti‐A. actinomycetemcomitans GroEL antibody was confirmed by a biospecific interaction analysis using a biosensor technology. Although additional investigations are required, the observed phenomenon may lead to an autoimmune response and thus contribute to tissue destruction during periodontitis.</description><subject>Actinobacillus actinomycetemcomitans</subject><subject>Aggregatibacter actinomycetemcomitans - immunology</subject><subject>Antibodies, Bacterial - immunology</subject><subject>Antibodies, Bispecific - immunology</subject><subject>Antibody Specificity - immunology</subject><subject>Antigens, Bacterial - immunology</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Chaperonin 60 - analysis</subject><subject>Chaperonin 60 - immunology</subject><subject>Collagen Type IV - immunology</subject><subject>Cross Reactions - immunology</subject><subject>Dentistry</subject><subject>Epitopes - immunology</subject><subject>Escherichia coli</subject><subject>Escherichia coli - immunology</subject><subject>fibronectin</subject><subject>Fibronectins - immunology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glutamic Acid - analysis</subject><subject>Glutamine - analysis</subject><subject>Glycine - analysis</subject><subject>GroEL</subject><subject>heat shock protein</subject><subject>Humans</subject><subject>Isoleucine - analysis</subject><subject>Leucine - analysis</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>periodontitis</subject><subject>Sequence Homology, Amino Acid</subject><subject>Threonine - analysis</subject><issn>0902-0055</issn><issn>1399-302X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkV1v0zAUhi0EYmXwF5Bv4C7F34klbqpqlEmFITE-7izHPdlcEmeLE9Zc7p_PaavtEnzjY-l5jo_9IoQpmdO0PmznRBOWESLlnBHC54RQJue7Z2hGudYZJ-z3czR7hE7Qqxi3JJVK65fohIoip1yKGbpfhN5fQfAOu66NMevAut7_9f2IbdjgCLcDBAf4um3aur0acQn9HUDAi4SFtrTO1_UQsd0fm9FBD41rG9_bEPGqa8_W-KZre_Bh3_B6aGzAlS-7NsDkvEYvKltHeHPcT9GPT2eXy8_Z-mJ1vlysMycUl1nunGba5ooVSnJtVe4Er1zJmRS0KgQBpRlwXcqiUKBkoZi0nEpI3mZjGT9F7w990zTpTbE3jY8O6toGaIdoCkIl4YL-E6S5JFookcDiAO5_roPK3HS-sd1oKDFTTmZrpgjMFIGZcjL7nMwuqW-PdwxlA5sn8RhMAt4dARudravOBufjEycl5Xk-DfvxwN35Gsb_HsBcfDlPRdKzg-5jD7tH3XZ_jMp5Ls2vryuT_7wU9Pu3pWH8AeLjvx4</recordid><startdate>200404</startdate><enddate>200404</enddate><creator>Yoshioka, M.</creator><creator>Grenier, D.</creator><creator>Hinode, D.</creator><creator>Fukui, M.</creator><creator>Mayrand, D.</creator><general>Munksgaard International Publishers</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>7X8</scope></search><sort><creationdate>200404</creationdate><title>Antigenic cross-reactivity and sequence homology between Actinobacillus actinomycetemcomitans GroEL protein and human fibronectin</title><author>Yoshioka, M. ; Grenier, D. ; Hinode, D. ; Fukui, M. ; Mayrand, D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4635-7cc929a76286539a67c43fcb32541f840e692e39b5886e658625a315ecc9dda23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Actinobacillus actinomycetemcomitans</topic><topic>Aggregatibacter actinomycetemcomitans - immunology</topic><topic>Antibodies, Bacterial - immunology</topic><topic>Antibodies, Bispecific - immunology</topic><topic>Antibody Specificity - immunology</topic><topic>Antigens, Bacterial - immunology</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Chaperonin 60 - analysis</topic><topic>Chaperonin 60 - immunology</topic><topic>Collagen Type IV - immunology</topic><topic>Cross Reactions - immunology</topic><topic>Dentistry</topic><topic>Epitopes - immunology</topic><topic>Escherichia coli</topic><topic>Escherichia coli - immunology</topic><topic>fibronectin</topic><topic>Fibronectins - immunology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glutamic Acid - analysis</topic><topic>Glutamine - analysis</topic><topic>Glycine - analysis</topic><topic>GroEL</topic><topic>heat shock protein</topic><topic>Humans</topic><topic>Isoleucine - analysis</topic><topic>Leucine - analysis</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>periodontitis</topic><topic>Sequence Homology, Amino Acid</topic><topic>Threonine - analysis</topic><toplevel>online_resources</toplevel><creatorcontrib>Yoshioka, M.</creatorcontrib><creatorcontrib>Grenier, D.</creatorcontrib><creatorcontrib>Hinode, D.</creatorcontrib><creatorcontrib>Fukui, M.</creatorcontrib><creatorcontrib>Mayrand, D.</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>MEDLINE - Academic</collection><jtitle>Oral microbiology and immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yoshioka, M.</au><au>Grenier, D.</au><au>Hinode, D.</au><au>Fukui, M.</au><au>Mayrand, D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Antigenic cross-reactivity and sequence homology between Actinobacillus actinomycetemcomitans GroEL protein and human fibronectin</atitle><jtitle>Oral microbiology and immunology</jtitle><addtitle>Oral Microbiol Immunol</addtitle><date>2004-04</date><risdate>2004</risdate><volume>19</volume><issue>2</issue><spage>124</spage><epage>128</epage><pages>124-128</pages><issn>0902-0055</issn><eissn>1399-302X</eissn><coden>OMIMEE</coden><abstract>The immunologic cross‐reactivity between human fibronectin and Actinobacillus actinomycetemcomitans GroEL was examined. Analyses by SDS‐PAGE/Western immunoblotting and ELISA showed that a polyclonal antibody directed against the purified GroEL protein of A. actinomycetemcomitans, but not against the Escherichia coli GroEL, cross‐reacts with human fibronectin. No antigenic cross‐reactivity was observed between anti‐A. actinomycetemcomitans GroEL antibody and type IV collagen, another important constituent of the basement membrane. A comparative analysis of the amino acid sequences of A. actinomycetemcomitans GroEL and human fibronectin revealed eight instances of four‐amino acid sequence homology between the two proteins. Six of these tetrapeptide sequences were also shared with E. coli GroEL, suggesting that the remaining two tetrapeptides, GQLI (Glycine‐Glutamine‐Leucine‐Isoleucine) and TGLE (Threonine‐Glycine‐Leucine‐Glutamic acid), may be associated with the epitope that the anti‐A. actinomycetemcomitans GroEL antibody specifically recognizes. Reactivity between TGLE, but not GQLI, with anti‐A. actinomycetemcomitans GroEL antibody was confirmed by a biospecific interaction analysis using a biosensor technology. Although additional investigations are required, the observed phenomenon may lead to an autoimmune response and thus contribute to tissue destruction during periodontitis.</abstract><cop>Oxford UK</cop><pub>Munksgaard International Publishers</pub><pmid>14871354</pmid><doi>10.1111/j.0902-0055.2003.00125.x</doi><tpages>5</tpages></addata></record> |
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subjects | Actinobacillus actinomycetemcomitans Aggregatibacter actinomycetemcomitans - immunology Antibodies, Bacterial - immunology Antibodies, Bispecific - immunology Antibody Specificity - immunology Antigens, Bacterial - immunology Bacteriology Biological and medical sciences Chaperonin 60 - analysis Chaperonin 60 - immunology Collagen Type IV - immunology Cross Reactions - immunology Dentistry Epitopes - immunology Escherichia coli Escherichia coli - immunology fibronectin Fibronectins - immunology Fundamental and applied biological sciences. Psychology Glutamic Acid - analysis Glutamine - analysis Glycine - analysis GroEL heat shock protein Humans Isoleucine - analysis Leucine - analysis Microbiology Miscellaneous periodontitis Sequence Homology, Amino Acid Threonine - analysis |
title | Antigenic cross-reactivity and sequence homology between Actinobacillus actinomycetemcomitans GroEL protein and human fibronectin |
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