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Expression of a poliovirus neutralization epitope at the surface of recombinant bacteria: first immunization results.

Expression of a poliovirus neutralization epitope at the surface of recombinant bacteria: first immunization results. Research Abstract Details 

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  • Expression of a poliovirus neutralization epitope at the surface of recombinant bacteria: first immunization results. Abstract Text:

    a charbitA Charbit,s van der werfS Van der Werf,v mimicV Mimic,j c boulainJ C Boulain,m girardM Girard,m hofnungM Hofnung,

    We devised a procedure to construct strains of Escherichia coli which expose at their surface a foreign antigen genetically inserted into LamB, an outer membrane protein. In particular, we showed that amino acid residues 93-103 of poliovirus type 1 capsid polypeptide VP1, which correspond to the C3 neutralization epitope, when inserted into two different external loops of LamB (after residues 153 and 374 of the mature protein), yielded the synthesis of stable hybrid proteins named, respectively, 153-C3 and 374-C3. The poliovirus epitope was accessible to monoclonal antibody C3 at the cell surface. In the present work, these two hybrid proteins were injected into rabbits by the intravenous route in the form of live recombinant bacteria, and the humoral response to the poliovirus epitope was studied. With construction 153-C3, the subcutaneous route was also assayed using solubilized hybrid protein. The C3 viral sequence inserted in the two different regions of LamB were found to be immunogenic. Different types of antibodies specific to the C3 peptide were raised with the two construction: anti-peptide and antiviral particle antibodies. These first results indicate that the LamB presentation vector system constitutes a mode of peptide coupling which may lead to the elaboration of a new type of live vaccine.

    Expression of a poliovirus neutralization epitope at the surface of recombinant bacteria: first immunization results. Publishing Authors By Initials

    a charbitA Charbit,s van der werfS Van der Werf,v mimicV Mimic,jc boulainJC Boulain,m girardM Girard,m hofnungM Hofnung,

    For similar proteins: recombinant proteins research abstracts see: proteins: recombinant proteins research

    PUBMED ID PMID:

    MEDLINE DATE: 1988 Jan-Feb

    Expression of a poliovirus neutralization epitope at the surface of recombinant bacteria: first immunization results. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Annales de l'Institut Pasteur. Microbiology

    VOLUME: 139

    Page Numbers: 45-58

    Journal Abbreviation: Ann. Inst. Pasteur Microbiol.

    ISSN: 0769-2609

    DAY: 27

    MONTH: 11

    YEAR: 2007

    Expression of a poliovirus neutralization epitope at the surface of recombinant bacteria: first immunization results. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 8701984

    Expression of a poliovirus neutralization epitope at the surface of recombinant bacteria: first immunization results. Keywords Mesh Terms:

    KEYWORDS: Recombinant Proteins

    MESH TERMS: immunology

    Chemical & Substance for Abstract: Expression of a poliovirus neutralization epitope at the surface of recombinant bacteria: first immunization results. Information

    Substance Name: maltoporins

    Registry Number: 0

    Grant and Affiliation Information for Expression of a poliovirus neutralization epitope at the surface of recombinant bacteria: first immunization results.

    AFFILIATION: Unité de Programmation Moléculaire et Toxicologie Génétique (CNRS UA271, INSERM U163), Institut Pasteur, Paris, France.

    Country: FRANCE

    FRANCE Research PublicationFRANCE Research Publication

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    MEDLINETA: Ann Inst Pasteur Microbiol

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