Immunogenicity and structural characterization of an in vitro folded meningococcal siderophore receptor (FrpB, FetA)

J.A. Kortekaas, S.A. Mueller, P. Ringler, M. Gregorini, V.E. Weynants, L. Rutten

    Research output: Contribution to journalArticleAcademicpeer-review

    21 Citations (Scopus)

    Abstract

    The iron-limitation-inducible protein FrpB of Neisseria meningitidis is an outer-membrane-localized siderophore receptor. Because of its abundance and its capacity to elicit bactericidal antibodies, it is considered a vaccine candidate. Bactericidal antibodies against FrpB are, however, type-specific. Hence, an FrpB-based vaccine should comprise several FrpB variants to be capable of providing broad protection. To facilitate the development of a meningococcal subunit vaccine, we have established a procedure to obtain large quantities of the protein in a native-like conformation. The protein was expressed without its signal sequence in Escherichia coli, where it accumulated in inclusion bodies. After in vitro folding, the protein was biochemically, biophysically and biologically characterised. Our results show that in vitro folded FrpB assembles into oligomers, presumably dimers, and that it induces high levels of bactericidal antibodies in laboratory animals.
    Original languageEnglish
    Pages (from-to)2145-2153
    JournalMicrobes and Infection
    Volume8
    Issue number8
    DOIs
    Publication statusPublished - 2006

    Keywords

    • outer-membrane protein
    • neisseria-meningitidis
    • escherichia-coli
    • enterobactin receptor
    • electron-microscopy
    • crystal-structure
    • iron transport
    • vaccine
    • fhua
    • pora

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