Both the full-length and the N-terminal domain of the meningococcal transferrin-binding protein B discriminate between human iron-loaded and apo-transferrin.
FEMS Microbiol Lett
; 169(1): 171-7, 1998 Dec 01.
Article
in En
| MEDLINE
| ID: mdl-9851049
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.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Apoproteins
/
Transferrin
/
Carrier Proteins
/
Neisseria meningitidis
Type of study:
Prognostic_studies
Limits:
Humans
Language:
En
Journal:
FEMS Microbiol Lett
Year:
1998
Document type:
Article
Affiliation country:
France