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

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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)
Year published
2012
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Show full item recordAbstract
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 ...
View more >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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View more >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.
View less >
Journal Title
Biochemistry
Volume
51
Issue
46
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