title: Both the full-length and the N-terminal domain of the meningococcal transferrin-binding protein B discriminate between human iron-loaded and apo-transferrin.
abstract: We have readdressed the ability of the transferrin-binding protein B (TbpB) from Neisseria meningitidis to discriminate between the iron-loaded and the iron-free human transferrin (hTf) by using the BIAcore technology, a powerful experimental technique for the observation of direct interactions between a receptor and its ligands, without the use of labels. Recombinant full-length TbpB from five N. meningitidis strains were produced and purified from Escherichia coli as fusion proteins. They showed a preference for the binding to iron-loaded hTf. As for the full-length molecule, we have demonstrated that the minimal N-terminal hTf binding domain of meningococcal TbpB from B16B6 and M982 strains was able to discriminate between both hTf forms.
authors.affiliation: Pasteur Mérieux Connaught, Marcy l'Etoile, France. grenauld@fr.pmc-vacc.com
authors.forename: G
authors.initials: G
authors.lastname: Renauld-Mongénie
authors.forename: M
authors.initials: M
authors.lastname: Latour
authors.forename: D
authors.initials: D
authors.lastname: Poncet
authors.forename: S
authors.initials: S
authors.lastname: Naville
authors.forename: M J
authors.initials: MJ
authors.lastname: Quentin-Millet
mesh_terms: D001059:Apoproteins / Q000378:metabolism*; D015374:Biosensing Techniques; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D033862:Iron-Binding Proteins; D009345:Neisseria meningitidis; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D014168:Transferrin / Q000378:metabolism*; D033882:Transferrin-Binding Protein B; D033863:Transferrin-Binding Proteins
chemical_list: D001059:Apoproteins; D002352:Carrier Proteins; D033862:Iron-Binding Proteins; D011993:Recombinant Fusion Proteins; D014168:Transferrin; D033882:Transferrin-Binding Protein B; D033863:Transferrin-Binding Proteins; C028284:apotransferrin