Surface antigen analysis of group B Neisseria meningitidis outer membrane by monoclonal antibodies: identification of bactericidal antibodies to class 5 protein

Twenty-four monoclonal antibodies (mAbs) against group B Neisseria meningitidis surface antigens were analyzed by immunoenzymatic assays and by a bactericidal test. Two mAbs were specific to polysaccharide B and one to lipopolysaccharide. The others were directed against outer membrane proteins rang...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Current microbiology 1995-09, Vol.31 (3), p.146-151
Hauptverfasser: DANELLI, M. D. G. M, BATOREU, N. M, LACERDA, M. D, FERREIRA, C. R. B, CARDOSO, J. D, PERALTA, J. M, FRASCH, C. E
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 151
container_issue 3
container_start_page 146
container_title Current microbiology
container_volume 31
creator DANELLI, M. D. G. M
BATOREU, N. M
LACERDA, M. D
FERREIRA, C. R. B
CARDOSO, J. D
PERALTA, J. M
FRASCH, C. E
description Twenty-four monoclonal antibodies (mAbs) against group B Neisseria meningitidis surface antigens were analyzed by immunoenzymatic assays and by a bactericidal test. Two mAbs were specific to polysaccharide B and one to lipopolysaccharide. The others were directed against outer membrane proteins ranging in molecular mass from 25 to 200 kDa. The outer membrane protein epitopes recognized by the mAbs were not conformational and were located on the outer surface of the microorganism. Linear epitopes on the class 5 protein, exposed on the surface of the membrane, were able to induce bactericidal antibodies to the homologous strain. The susceptibility of Neisseria meningitidis to these antibodies was unchanged when this organism was cultivated under conditions of iron depletion. These results demonstrate that peptides derived from class 5 proteins are potentially important in synthetic peptide or in recombinant protein vaccines containing linear bactericidal epitopes.
doi_str_mv 10.1007/BF00293545
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_16840015</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>16840015</sourcerecordid><originalsourceid>FETCH-LOGICAL-c325t-34b0d7eefb8a82562357fb915f613821c52ea1b3120cf3bbbd1ba54bb307cabf3</originalsourceid><addsrcrecordid>eNpVkc1OHDEMgCNUJJaFC0-QQ8Wh0rT5mcxPb4CgIKFyoD2PkoyzcjUz2cYzh32bPmqz7KqoJ8vW58-yzdiVFJ-lEPWX2wchVKtNaU7YSpZaFaJt5Qe2ErrURVMZecbOiX4JIVUr5Ir9eV1SsB64nWbcwJSjHXaExGPgmxSXLb_l3wGJIKHlI0w4bXDGfk8sM6RcGl2yE3C342Ocoh9iVrz5XOwR6CvHHnIW0NsZ47Q3O-tzL3rs_0P5HLkfLBE3fJviDDhdsNNgB4LLY1yznw_3P-4ei-eXb093N8-F18rMhS6d6GuA4BrbKFMpbergWmlCJXWjpDcKrHRaKuGDds710llTOqdF7a0Les2uD9489_cCNHcjkodhyKvFhTpZNWW-msngpwPoUyRKELptwtGmXSdFt39C9_6EDH88Wi15O4R8KI_0r0NXStR1rf8Cc1uKPQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16840015</pqid></control><display><type>article</type><title>Surface antigen analysis of group B Neisseria meningitidis outer membrane by monoclonal antibodies: identification of bactericidal antibodies to class 5 protein</title><source>SpringerNature Journals</source><creator>DANELLI, M. D. G. M ; BATOREU, N. M ; LACERDA, M. D ; FERREIRA, C. R. B ; CARDOSO, J. D ; PERALTA, J. M ; FRASCH, C. E</creator><creatorcontrib>DANELLI, M. D. G. M ; BATOREU, N. M ; LACERDA, M. D ; FERREIRA, C. R. B ; CARDOSO, J. D ; PERALTA, J. M ; FRASCH, C. E</creatorcontrib><description>Twenty-four monoclonal antibodies (mAbs) against group B Neisseria meningitidis surface antigens were analyzed by immunoenzymatic assays and by a bactericidal test. Two mAbs were specific to polysaccharide B and one to lipopolysaccharide. The others were directed against outer membrane proteins ranging in molecular mass from 25 to 200 kDa. The outer membrane protein epitopes recognized by the mAbs were not conformational and were located on the outer surface of the microorganism. Linear epitopes on the class 5 protein, exposed on the surface of the membrane, were able to induce bactericidal antibodies to the homologous strain. The susceptibility of Neisseria meningitidis to these antibodies was unchanged when this organism was cultivated under conditions of iron depletion. These results demonstrate that peptides derived from class 5 proteins are potentially important in synthetic peptide or in recombinant protein vaccines containing linear bactericidal epitopes.</description><identifier>ISSN: 0343-8651</identifier><identifier>EISSN: 1432-0991</identifier><identifier>DOI: 10.1007/BF00293545</identifier><identifier>CODEN: CUMIDD</identifier><language>eng</language><publisher>New York, NY: Springer</publisher><subject>Bacteriology ; Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Microbiology ; Morphology, structure, chemical composition ; Neisseria meningitidis</subject><ispartof>Current microbiology, 1995-09, Vol.31 (3), p.146-151</ispartof><rights>1995 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c325t-34b0d7eefb8a82562357fb915f613821c52ea1b3120cf3bbbd1ba54bb307cabf3</citedby><cites>FETCH-LOGICAL-c325t-34b0d7eefb8a82562357fb915f613821c52ea1b3120cf3bbbd1ba54bb307cabf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27928,27929</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=3620777$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>DANELLI, M. D. G. M</creatorcontrib><creatorcontrib>BATOREU, N. M</creatorcontrib><creatorcontrib>LACERDA, M. D</creatorcontrib><creatorcontrib>FERREIRA, C. R. B</creatorcontrib><creatorcontrib>CARDOSO, J. D</creatorcontrib><creatorcontrib>PERALTA, J. M</creatorcontrib><creatorcontrib>FRASCH, C. E</creatorcontrib><title>Surface antigen analysis of group B Neisseria meningitidis outer membrane by monoclonal antibodies: identification of bactericidal antibodies to class 5 protein</title><title>Current microbiology</title><description>Twenty-four monoclonal antibodies (mAbs) against group B Neisseria meningitidis surface antigens were analyzed by immunoenzymatic assays and by a bactericidal test. Two mAbs were specific to polysaccharide B and one to lipopolysaccharide. The others were directed against outer membrane proteins ranging in molecular mass from 25 to 200 kDa. The outer membrane protein epitopes recognized by the mAbs were not conformational and were located on the outer surface of the microorganism. Linear epitopes on the class 5 protein, exposed on the surface of the membrane, were able to induce bactericidal antibodies to the homologous strain. The susceptibility of Neisseria meningitidis to these antibodies was unchanged when this organism was cultivated under conditions of iron depletion. These results demonstrate that peptides derived from class 5 proteins are potentially important in synthetic peptide or in recombinant protein vaccines containing linear bactericidal epitopes.</description><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Microbiology</subject><subject>Morphology, structure, chemical composition</subject><subject>Neisseria meningitidis</subject><issn>0343-8651</issn><issn>1432-0991</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNpVkc1OHDEMgCNUJJaFC0-QQ8Wh0rT5mcxPb4CgIKFyoD2PkoyzcjUz2cYzh32bPmqz7KqoJ8vW58-yzdiVFJ-lEPWX2wchVKtNaU7YSpZaFaJt5Qe2ErrURVMZecbOiX4JIVUr5Ir9eV1SsB64nWbcwJSjHXaExGPgmxSXLb_l3wGJIKHlI0w4bXDGfk8sM6RcGl2yE3C342Ocoh9iVrz5XOwR6CvHHnIW0NsZ47Q3O-tzL3rs_0P5HLkfLBE3fJviDDhdsNNgB4LLY1yznw_3P-4ei-eXb093N8-F18rMhS6d6GuA4BrbKFMpbergWmlCJXWjpDcKrHRaKuGDds710llTOqdF7a0Les2uD9489_cCNHcjkodhyKvFhTpZNWW-msngpwPoUyRKELptwtGmXSdFt39C9_6EDH88Wi15O4R8KI_0r0NXStR1rf8Cc1uKPQ</recordid><startdate>19950901</startdate><enddate>19950901</enddate><creator>DANELLI, M. D. G. M</creator><creator>BATOREU, N. M</creator><creator>LACERDA, M. D</creator><creator>FERREIRA, C. R. B</creator><creator>CARDOSO, J. D</creator><creator>PERALTA, J. M</creator><creator>FRASCH, C. E</creator><general>Springer</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7T5</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope></search><sort><creationdate>19950901</creationdate><title>Surface antigen analysis of group B Neisseria meningitidis outer membrane by monoclonal antibodies: identification of bactericidal antibodies to class 5 protein</title><author>DANELLI, M. D. G. M ; BATOREU, N. M ; LACERDA, M. D ; FERREIRA, C. R. B ; CARDOSO, J. D ; PERALTA, J. M ; FRASCH, C. E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c325t-34b0d7eefb8a82562357fb915f613821c52ea1b3120cf3bbbd1ba54bb307cabf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Microbiology</topic><topic>Morphology, structure, chemical composition</topic><topic>Neisseria meningitidis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>DANELLI, M. D. G. M</creatorcontrib><creatorcontrib>BATOREU, N. M</creatorcontrib><creatorcontrib>LACERDA, M. D</creatorcontrib><creatorcontrib>FERREIRA, C. R. B</creatorcontrib><creatorcontrib>CARDOSO, J. D</creatorcontrib><creatorcontrib>PERALTA, J. M</creatorcontrib><creatorcontrib>FRASCH, C. E</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Immunology 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>Biotechnology and BioEngineering Abstracts</collection><jtitle>Current microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>DANELLI, M. D. G. M</au><au>BATOREU, N. M</au><au>LACERDA, M. D</au><au>FERREIRA, C. R. B</au><au>CARDOSO, J. D</au><au>PERALTA, J. M</au><au>FRASCH, C. E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Surface antigen analysis of group B Neisseria meningitidis outer membrane by monoclonal antibodies: identification of bactericidal antibodies to class 5 protein</atitle><jtitle>Current microbiology</jtitle><date>1995-09-01</date><risdate>1995</risdate><volume>31</volume><issue>3</issue><spage>146</spage><epage>151</epage><pages>146-151</pages><issn>0343-8651</issn><eissn>1432-0991</eissn><coden>CUMIDD</coden><abstract>Twenty-four monoclonal antibodies (mAbs) against group B Neisseria meningitidis surface antigens were analyzed by immunoenzymatic assays and by a bactericidal test. Two mAbs were specific to polysaccharide B and one to lipopolysaccharide. The others were directed against outer membrane proteins ranging in molecular mass from 25 to 200 kDa. The outer membrane protein epitopes recognized by the mAbs were not conformational and were located on the outer surface of the microorganism. Linear epitopes on the class 5 protein, exposed on the surface of the membrane, were able to induce bactericidal antibodies to the homologous strain. The susceptibility of Neisseria meningitidis to these antibodies was unchanged when this organism was cultivated under conditions of iron depletion. These results demonstrate that peptides derived from class 5 proteins are potentially important in synthetic peptide or in recombinant protein vaccines containing linear bactericidal epitopes.</abstract><cop>New York, NY</cop><pub>Springer</pub><doi>10.1007/BF00293545</doi><tpages>6</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0343-8651
ispartof Current microbiology, 1995-09, Vol.31 (3), p.146-151
issn 0343-8651
1432-0991
language eng
recordid cdi_proquest_miscellaneous_16840015
source SpringerNature Journals
subjects Bacteriology
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Microbiology
Morphology, structure, chemical composition
Neisseria meningitidis
title Surface antigen analysis of group B Neisseria meningitidis outer membrane by monoclonal antibodies: identification of bactericidal antibodies to class 5 protein
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-16T23%3A27%3A25IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Surface%20antigen%20analysis%20of%20group%20B%20Neisseria%20meningitidis%20outer%20membrane%20by%20monoclonal%20antibodies:%20identification%20of%20bactericidal%20antibodies%20to%20class%205%20protein&rft.jtitle=Current%20microbiology&rft.au=DANELLI,%20M.%20D.%20G.%20M&rft.date=1995-09-01&rft.volume=31&rft.issue=3&rft.spage=146&rft.epage=151&rft.pages=146-151&rft.issn=0343-8651&rft.eissn=1432-0991&rft.coden=CUMIDD&rft_id=info:doi/10.1007/BF00293545&rft_dat=%3Cproquest_cross%3E16840015%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=16840015&rft_id=info:pmid/&rfr_iscdi=true