Factor H-binding protein is a 27-kDa lipoprotein of Neisseria meningitidis discovered while screening the bacterial genome for vaccine candidates. In addition to being an important component of a vaccine against meningococcus in late stage of development, the protein is essential for pathogenesis because it allows the bacterium to survive and grow in human blood by binding the human complement factor H. We recently reported the solution structure of the C-terminal domain of factor H-binding protein, which contains the immunodominant epitopes. In the present study, we report the structure of the full-length molecule, determined by nuclear magnetic resonance spectroscopy. The protein is composed of two independent barrels connected by a short link. Mapping the residues recognized by monoclonal antibodies with bactericidal or factor H binding inhibition properties allowed us to predict the sites involved in the function of the protein. The structure therefore provides the basis for designing improved vaccine molecules. © 2009 by The American Society for Biochemistry and Molecular Biology, Inc.

Solution structure of the factor H binding protein, a survival factor and protective antigen of neisseria meningitidis / F.Cantini; D.Veggi; S.Dragonetti; S.Savino; M.Scarselli; G.Romagnoli; M.Pizza; L.Banci; R.Rappuoli. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - STAMPA. - 284:(2009), pp. 9022-9026. [10.1074/jbc.C800214200]

Solution structure of the factor H binding protein, a survival factor and protective antigen of neisseria meningitidis

CANTINI, FRANCESCA;DRAGONETTI, SARA;BANCI, LUCIA;
2009

Abstract

Factor H-binding protein is a 27-kDa lipoprotein of Neisseria meningitidis discovered while screening the bacterial genome for vaccine candidates. In addition to being an important component of a vaccine against meningococcus in late stage of development, the protein is essential for pathogenesis because it allows the bacterium to survive and grow in human blood by binding the human complement factor H. We recently reported the solution structure of the C-terminal domain of factor H-binding protein, which contains the immunodominant epitopes. In the present study, we report the structure of the full-length molecule, determined by nuclear magnetic resonance spectroscopy. The protein is composed of two independent barrels connected by a short link. Mapping the residues recognized by monoclonal antibodies with bactericidal or factor H binding inhibition properties allowed us to predict the sites involved in the function of the protein. The structure therefore provides the basis for designing improved vaccine molecules. © 2009 by The American Society for Biochemistry and Molecular Biology, Inc.
284
9022
9026
F.Cantini; D.Veggi; S.Dragonetti; S.Savino; M.Scarselli; G.Romagnoli; M.Pizza; L.Banci; R.Rappuoli
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in FLORE sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2158/372303
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 53
  • ???jsp.display-item.citation.isi??? 55
social impact