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  • The Factor H Binding Protein of Neisseria meningitidis Interacts with Xenosiderophores in Vitro

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    Accepted Manuscript (AM)
    Author(s)
    Veggi, Daniele
    Gentile, Maria A
    Cantini, Francesca
    Lo Surdo, Paola
    Nardi-Dei, Vincenzo
    Seib, Kate L
    Pizza, Mariagrazia
    Rappuoli, Rino
    Banci, Lucia
    Savino, Silvana
    Scarselli, Maria
    Griffith University Author(s)
    Seib, Kate
    Year published
    2012
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    Abstract
    The factor H binding protein (fHbp) is a key virulence factor of Neisseria meningitidis that confers to the bacterium the ability to resist killing by human serum. The determination of its three-dimensional structure revealed that the carboxyl terminus of the protein folds into an eight-stranded ߠbarrel. The structural similarity of this part of the protein to lipocalins provided the rationale for exploring the ability of fHbp to bind siderophores. We found that fHbp was able to bind in vitro siderophores belonging to the cathecolate family and mapped the interaction site by nuclear magnetic resonance. Our results indicated ...
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    The factor H binding protein (fHbp) is a key virulence factor of Neisseria meningitidis that confers to the bacterium the ability to resist killing by human serum. The determination of its three-dimensional structure revealed that the carboxyl terminus of the protein folds into an eight-stranded ߠbarrel. The structural similarity of this part of the protein to lipocalins provided the rationale for exploring the ability of fHbp to bind siderophores. We found that fHbp was able to bind in vitro siderophores belonging to the cathecolate family and mapped the interaction site by nuclear magnetic resonance. Our results indicated that the enterobactin binding site was distinct from the site involved in binding to human factor H and stimulates new hypotheses about possible multiple activities of fHbp.
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    Journal Title
    Biochemistry
    Volume
    51
    Issue
    46
    DOI
    https://doi.org/10.1021/bi301161w
    Copyright Statement
    © 2012 American Chemical Society. This document is the Postprint: Accepted Manuscript version of a Published Work that appeared in final form in Biochemistry, after peer review and technical editing by the publisher. To access the final edited and published work see 10.1021/bi301161w
    Subject
    Medicinal and biomolecular chemistry
    Biochemistry and cell biology
    Structural biology (incl. macromolecular modelling)
    Bacteriology
    Medical biochemistry and metabolomics
    Publication URI
    http://hdl.handle.net/10072/51642
    Collection
    • Journal articles

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