Blocking of iron uptake by monoclonal antibodies specific for the Neisseria meningitidis transferrin-binding protein 2
Departamento de Microbiología, Facultad de Farmacia, Universidad de Santiago de Compostela, Spain * Centre for Applied Microbiology and Research, Porton Down, Salisbury, Wiltshire Corresponding author: Professor C. M. Ferreirós. Received January 9, 1996 Accepted February 22, 1996 The existence of ep...
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Veröffentlicht in: | Journal of medical microbiology 1996-10, Vol.45 (4), p.252-257 |
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creator | Pintor, Mar Ferron, Lucia Gomez, J. A Gorringe, A Criado, M. Teresa Ferreiros, C. M |
description | Departamento de Microbiología, Facultad de Farmacia, Universidad de Santiago de Compostela, Spain
* Centre for Applied Microbiology and Research, Porton Down, Salisbury, Wiltshire
Corresponding author: Professor C. M. Ferreirós.
Received January 9, 1996
Accepted February 22, 1996
The existence of epitopes common to different strains in the Neisseria meningitidis transferrin (Tf)-binding protein 2 (TBP2), combined with the ability of polyclonal anti-TBP2 antibodies to inhibit Tf binding and block iron uptake in this species, led to this study on the effect of anti-TBP1+2 monoclonal antibodies (MAbs) to determine the presence of epitopes inside the Tf-binding region. All MAbs used reacted exclusively with the homologous strain when tested by dot-blots of outer membrane vesicles, with the reaction being specific for TBP2 after SDS-PAGE and electroblotting. In contrast, ELISA and iron-uptake blocking assays were also positive with heterologous strains belonging to Rokbi's group II (high mol.wt TBP2). The results confirmed the two group classification proposed by Rokbi and, in contrast to other studies, indicated the existence of epitopes in the Tf-binding region that are common only to strains of Rokbi's group II. These epitopes may become denatured after drying for dot-blot assays or after SDS-PAGE and electroblotting. |
doi_str_mv | 10.1099/00222615-45-4-252 |
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* Centre for Applied Microbiology and Research, Porton Down, Salisbury, Wiltshire
Corresponding author: Professor C. M. Ferreirós.
Received January 9, 1996
Accepted February 22, 1996
The existence of epitopes common to different strains in the Neisseria meningitidis transferrin (Tf)-binding protein 2 (TBP2), combined with the ability of polyclonal anti-TBP2 antibodies to inhibit Tf binding and block iron uptake in this species, led to this study on the effect of anti-TBP1+2 monoclonal antibodies (MAbs) to determine the presence of epitopes inside the Tf-binding region. All MAbs used reacted exclusively with the homologous strain when tested by dot-blots of outer membrane vesicles, with the reaction being specific for TBP2 after SDS-PAGE and electroblotting. In contrast, ELISA and iron-uptake blocking assays were also positive with heterologous strains belonging to Rokbi's group II (high mol.wt TBP2). The results confirmed the two group classification proposed by Rokbi and, in contrast to other studies, indicated the existence of epitopes in the Tf-binding region that are common only to strains of Rokbi's group II. These epitopes may become denatured after drying for dot-blot assays or after SDS-PAGE and electroblotting.</description><identifier>ISSN: 0022-2615</identifier><identifier>EISSN: 1473-5644</identifier><identifier>DOI: 10.1099/00222615-45-4-252</identifier><identifier>PMID: 8849698</identifier><identifier>CODEN: JMMIAV</identifier><language>eng</language><publisher>Reading: Soc General Microbiol</publisher><subject>Animals ; Antibodies, Monoclonal - immunology ; Antigenic determinants, haptens, artificial antigens ; Antigens ; Bacterial Outer Membrane Proteins - immunology ; Bacterial Outer Membrane Proteins - metabolism ; Biological and medical sciences ; Blotting, Western ; Carrier Proteins - immunology ; Carrier Proteins - metabolism ; Cross Reactions ; Enzyme-Linked Immunosorbent Assay ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Humans ; Immune Sera - immunology ; Immunoblotting ; Iron - metabolism ; Iron-Binding Proteins ; Male ; Molecular immunology ; Neisseria meningitidis ; Neisseria meningitidis - immunology ; Neisseria meningitidis - metabolism ; Rabbits ; Transferrin-Binding Protein B ; Transferrin-Binding Proteins</subject><ispartof>Journal of medical microbiology, 1996-10, Vol.45 (4), p.252-257</ispartof><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c431t-e102177c20455f529ea26e118a43db3bd98baf0034cc9e4416a3c981988d9e993</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,3744,3745,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3221224$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8849698$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pintor, Mar</creatorcontrib><creatorcontrib>Ferron, Lucia</creatorcontrib><creatorcontrib>Gomez, J. A</creatorcontrib><creatorcontrib>Gorringe, A</creatorcontrib><creatorcontrib>Criado, M. Teresa</creatorcontrib><creatorcontrib>Ferreiros, C. M</creatorcontrib><title>Blocking of iron uptake by monoclonal antibodies specific for the Neisseria meningitidis transferrin-binding protein 2</title><title>Journal of medical microbiology</title><addtitle>J Med Microbiol</addtitle><description>Departamento de Microbiología, Facultad de Farmacia, Universidad de Santiago de Compostela, Spain
* Centre for Applied Microbiology and Research, Porton Down, Salisbury, Wiltshire
Corresponding author: Professor C. M. Ferreirós.
Received January 9, 1996
Accepted February 22, 1996
The existence of epitopes common to different strains in the Neisseria meningitidis transferrin (Tf)-binding protein 2 (TBP2), combined with the ability of polyclonal anti-TBP2 antibodies to inhibit Tf binding and block iron uptake in this species, led to this study on the effect of anti-TBP1+2 monoclonal antibodies (MAbs) to determine the presence of epitopes inside the Tf-binding region. All MAbs used reacted exclusively with the homologous strain when tested by dot-blots of outer membrane vesicles, with the reaction being specific for TBP2 after SDS-PAGE and electroblotting. In contrast, ELISA and iron-uptake blocking assays were also positive with heterologous strains belonging to Rokbi's group II (high mol.wt TBP2). The results confirmed the two group classification proposed by Rokbi and, in contrast to other studies, indicated the existence of epitopes in the Tf-binding region that are common only to strains of Rokbi's group II. These epitopes may become denatured after drying for dot-blot assays or after SDS-PAGE and electroblotting.</description><subject>Animals</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antigenic determinants, haptens, artificial antigens</subject><subject>Antigens</subject><subject>Bacterial Outer Membrane Proteins - immunology</subject><subject>Bacterial Outer Membrane Proteins - metabolism</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Carrier Proteins - immunology</subject><subject>Carrier Proteins - metabolism</subject><subject>Cross Reactions</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Humans</subject><subject>Immune Sera - immunology</subject><subject>Immunoblotting</subject><subject>Iron - metabolism</subject><subject>Iron-Binding Proteins</subject><subject>Male</subject><subject>Molecular immunology</subject><subject>Neisseria meningitidis</subject><subject>Neisseria meningitidis - immunology</subject><subject>Neisseria meningitidis - metabolism</subject><subject>Rabbits</subject><subject>Transferrin-Binding Protein B</subject><subject>Transferrin-Binding Proteins</subject><issn>0022-2615</issn><issn>1473-5644</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtvFDEQhC0ECpvAD-CA5AMipyF-zYx9JBEvKUoucLY8nvZuJzP2Ys-C8u_j1S57RWrJh_q6quUi5B1nnzgz5ooxIUTH20bVaUQrXpAVV71s2k6pl2S115s98Jqcl_LAGO-lNGfkTGtlOqNX5M_1lPwjxjVNgWJOke62i3sEOjzROcXkpxTdRF1ccEgjQqFlCx4DehpSpssG6B1gKZDR0RlidcIFRyx0yS6WADljbAaM4z5jm9MCGKl4Q14FNxV4e3wvyK-vX37efG9u77_9uPl823gl-dIAZ4L3vRdMtW1ohQEnOuBcOyXHQQ6j0YMLjEnlvQGleOekN5obrUcDxsgL8vHgW5N_76AsdsbiYZpchLQrttfSdJrJ_4K87duuU6yC_AD6nErJEOw24-zyk-XM7kux_0qxqo6tpdSd90fz3TDDeNo4tlD1D0fdFe-mUH_OYzlhUgguhKrY5QHb4HrzFzPYNcQZ6yEDJvswz6fAZ2O_ouE</recordid><startdate>19961001</startdate><enddate>19961001</enddate><creator>Pintor, Mar</creator><creator>Ferron, Lucia</creator><creator>Gomez, J. A</creator><creator>Gorringe, A</creator><creator>Criado, M. Teresa</creator><creator>Ferreiros, C. M</creator><general>Soc General Microbiol</general><general>Society for General Microbiology</general><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>19961001</creationdate><title>Blocking of iron uptake by monoclonal antibodies specific for the Neisseria meningitidis transferrin-binding protein 2</title><author>Pintor, Mar ; Ferron, Lucia ; Gomez, J. A ; Gorringe, A ; Criado, M. Teresa ; Ferreiros, C. M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c431t-e102177c20455f529ea26e118a43db3bd98baf0034cc9e4416a3c981988d9e993</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Animals</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antigenic determinants, haptens, artificial antigens</topic><topic>Antigens</topic><topic>Bacterial Outer Membrane Proteins - immunology</topic><topic>Bacterial Outer Membrane Proteins - metabolism</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Carrier Proteins - immunology</topic><topic>Carrier Proteins - metabolism</topic><topic>Cross Reactions</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Humans</topic><topic>Immune Sera - immunology</topic><topic>Immunoblotting</topic><topic>Iron - metabolism</topic><topic>Iron-Binding Proteins</topic><topic>Male</topic><topic>Molecular immunology</topic><topic>Neisseria meningitidis</topic><topic>Neisseria meningitidis - immunology</topic><topic>Neisseria meningitidis - metabolism</topic><topic>Rabbits</topic><topic>Transferrin-Binding Protein B</topic><topic>Transferrin-Binding Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pintor, Mar</creatorcontrib><creatorcontrib>Ferron, Lucia</creatorcontrib><creatorcontrib>Gomez, J. A</creatorcontrib><creatorcontrib>Gorringe, A</creatorcontrib><creatorcontrib>Criado, M. Teresa</creatorcontrib><creatorcontrib>Ferreiros, C. M</creatorcontrib><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>Journal of medical microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pintor, Mar</au><au>Ferron, Lucia</au><au>Gomez, J. A</au><au>Gorringe, A</au><au>Criado, M. Teresa</au><au>Ferreiros, C. M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Blocking of iron uptake by monoclonal antibodies specific for the Neisseria meningitidis transferrin-binding protein 2</atitle><jtitle>Journal of medical microbiology</jtitle><addtitle>J Med Microbiol</addtitle><date>1996-10-01</date><risdate>1996</risdate><volume>45</volume><issue>4</issue><spage>252</spage><epage>257</epage><pages>252-257</pages><issn>0022-2615</issn><eissn>1473-5644</eissn><coden>JMMIAV</coden><abstract>Departamento de Microbiología, Facultad de Farmacia, Universidad de Santiago de Compostela, Spain
* Centre for Applied Microbiology and Research, Porton Down, Salisbury, Wiltshire
Corresponding author: Professor C. M. Ferreirós.
Received January 9, 1996
Accepted February 22, 1996
The existence of epitopes common to different strains in the Neisseria meningitidis transferrin (Tf)-binding protein 2 (TBP2), combined with the ability of polyclonal anti-TBP2 antibodies to inhibit Tf binding and block iron uptake in this species, led to this study on the effect of anti-TBP1+2 monoclonal antibodies (MAbs) to determine the presence of epitopes inside the Tf-binding region. All MAbs used reacted exclusively with the homologous strain when tested by dot-blots of outer membrane vesicles, with the reaction being specific for TBP2 after SDS-PAGE and electroblotting. In contrast, ELISA and iron-uptake blocking assays were also positive with heterologous strains belonging to Rokbi's group II (high mol.wt TBP2). The results confirmed the two group classification proposed by Rokbi and, in contrast to other studies, indicated the existence of epitopes in the Tf-binding region that are common only to strains of Rokbi's group II. These epitopes may become denatured after drying for dot-blot assays or after SDS-PAGE and electroblotting.</abstract><cop>Reading</cop><pub>Soc General Microbiol</pub><pmid>8849698</pmid><doi>10.1099/00222615-45-4-252</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; Microbiology Society; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
subjects | Animals Antibodies, Monoclonal - immunology Antigenic determinants, haptens, artificial antigens Antigens Bacterial Outer Membrane Proteins - immunology Bacterial Outer Membrane Proteins - metabolism Biological and medical sciences Blotting, Western Carrier Proteins - immunology Carrier Proteins - metabolism Cross Reactions Enzyme-Linked Immunosorbent Assay Fundamental and applied biological sciences. Psychology Fundamental immunology Humans Immune Sera - immunology Immunoblotting Iron - metabolism Iron-Binding Proteins Male Molecular immunology Neisseria meningitidis Neisseria meningitidis - immunology Neisseria meningitidis - metabolism Rabbits Transferrin-Binding Protein B Transferrin-Binding Proteins |
title | Blocking of iron uptake by monoclonal antibodies specific for the Neisseria meningitidis transferrin-binding protein 2 |
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