Open AccessBoth the full‐length and the N‐terminal domain of the meningococcal transferrin‐binding protein B discriminate between human iron‐loaded and apo‐transferrin
Author(s) -
RenauldMongénie Geneviève,
Latour Mireille,
Poncet David,
Naville Sophie,
QuentinMillet MarieJosé
Publication year - 1998
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1998.tb13314.x
Subject(s) - transferrin , neisseria meningitidis , fusion protein , transferrin receptor , recombinant dna , chemistry , escherichia coli , meningococcal vaccine , neisseriaceae , biochemistry , biology , microbiology and biotechnology , bacteria , antibiotics , gene , genetics
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.