edoc-vmtest

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

Kortekaas, Jeroen and Müller, Shirley A. and Ringler, Philippe and Gregorini, Marco and Weynants, Vincent E. and Rutten, Lucy and Bos, Martine P. and Tommassen, Jan. (2006) Immunogenicity and structural characterisation of an in vitro folded meningococcal siderophore receptor (FrpB, FetA). Microbes and infection, Vol. 8, H. 8. pp. 2145-2153.

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Official URL: http://edoc.unibas.ch/dok/A5262470

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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 biochem., biophys. and biol. characterized. Our results show that in vitro folded FrpB assembles into oligomers, presumably dimers, and that it induces high levels of bactericidal antibodies in lab. animals. [on SciFinder (R)]
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
UniBasel Contributors:Müller, Shirley and Ringler, Philippe and Engel, Andreas H
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Elsevier
ISSN:1286-4579
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:21
Deposited On:22 Mar 2012 13:24

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