[en] In presence of β-lactamines, some strains of B. licheniformis secret a β-lactamase that hydrolyses the antibiotic, making the bacteria resistant to penicillin. Staphylococcus aureus possesses a very similar system, allowing the expression of a β-lactamase in response to the presence of antibiotic outside the cell . In both strains, cells are able to sense the antibiotic in the medium through a membrane penicillin receptor BlaR1. Up to now, the 3D structure addressing the receptor in its entire form is not available, mainly due to low production yields and degradation. Here we show production, purification and reconstitution of the entire membrane protein in a lipid bilayer and a first AFM study of intra-molecular forces involved in the activation process of BlaR1.
Research Center/Unit :
CIP - Centre d'Ingénierie des Protéines - ULiège Nanochemistry and Molecular Systems - University of Liege
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Mescola, Andrea ; Université de Liège > Département de chimie (sciences) > Nanochimie et systèmes moléculaires
Dauvin, Marjorie ; Université de Liège > Département des sciences de la vie > Physiologie et génétique bactériennes
Language :
English
Title :
AFM study of the penicillin receptor BlaR1 of Bacillus licheniformis
Alternative titles :
[en] Etude AFM du récepteur à la pénicilline BlaR1 de Bacillus licheniformis