- Structural basis of nanobody-mediated blocking of BtuF, the cognate substrate-binding protein of the Escherichia coli vitamin B12 transporter BtuCD.
Structural basis of nanobody-mediated blocking of BtuF, the cognate substrate-binding protein of the Escherichia coli vitamin B12 transporter BtuCD.
Scientific reports (2017-11-01)
S A Mireku, M M Sauer, R Glockshuber, K P Locher
PMID29084999
RÉSUMÉ
Bacterial ABC importers catalyze the uptake of essential nutrients including transition metals and metal-containing co-factors. Recently, an IgG antibody targeting the external binding protein of the Staphylococcus aureus Mn(II) ABC importer was reported to inhibit transport activity and reduce bacterial cell growth. We here explored the possibility of using alpaca-derived nanobodies to inhibit the vitamin B12 transporter of Escherichia coli, BtuCD-F, as a model system by generating nanobodies against the periplasmic binding protein BtuF. We isolated six nanobodies that competed with B12 for binding to BtuF, with inhibition constants between 10
MATÉRIAUX
Référence du produit
Marque
Description du produit
Sigma-Aldrich
Tubes ACCUSPIN™, stériles, d′une capacité de 50 ml, radiation sterilized tube fitted with a high density polyethylene barrier