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.
journal_name
Microbes Infectjournal_title
Microbes and infectionauthors
Kortekaas J,Müller SA,Ringler P,Gregorini M,Weynants VE,Rutten L,Bos MP,Tommassen Jdoi
10.1016/j.micinf.2006.04.011subject
Has Abstractpub_date
2006-07-01 00:00:00pages
2145-53issue
8eissn
1286-4579issn
1769-714Xpii
S1286-4579(06)00174-2journal_volume
8pub_type
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