Reference : Beta-lactamase inhibitors derived from single-domain antibody fragments elicited in t...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Beta-lactamase inhibitors derived from single-domain antibody fragments elicited in the camelidae.
Conrath, K. E. [Vrije Universiteit Brussel - VUB > Ultrastructure > > >]
Lauwereys, M. [> > > >]
Galleni, Moreno mailto [Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques, Centre d'Ingénierie des Protéines > >]
Matagne, André mailto [Université de Liège - ULiège > Département des sciences de la vie > Enzymologie, Centre d'Ingénierie des Protéines > >]
Frère, Jean-Marie mailto [Université de Liège - ULiège > > Centre d'ingénierie des protéines >]
Kinne, J. [> > > >]
Wyns, L. [> > > >]
Muyldermans, S. [Vrije Universiteit Brussel - VUB > Ultrastructure > > >]
Antimicrobial Agents and Chemotherapy
American Society for Microbiology (ASM)
Yes (verified by ORBi)
[en] Amino Acid Sequence ; Ampicillin/pharmacology ; Animals ; Antibody Specificity ; Bacterial Proteins/pharmacology ; Camels/immunology ; Escherichia coli/drug effects/enzymology ; Immunoglobulin Fragments/isolation & purification/pharmacology ; Male ; Molecular Sequence Data ; Penicillin Resistance ; Penicillins/pharmacology ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid ; beta-Lactamases/antagonists & inhibitors/immunology
[en] Small, soluble single-domain fragments derived from the unique variable region of dromedary heavy-chain antibodies (VHHs) against enzymes are known to be potent inhibitors. The immunization of dromedaries with the TEM-1 and BcII beta-lactamases has lead to the isolation of such single-domain antibody fragments specifically recognizing and inhibiting those beta-lactamases. Two VHHs were isolated that inhibit TEM-1 and one BcII inhibiting VHH was identified. All inhibitory VHHs were tight-binding inhibitors. The 50% inhibitory concentrations were determined for all inhibitors and they were all in the same range as the enzyme concentration used in the assay. Addition of the VHHs to the TEM-1 beta-lactamase, expressed on the surface of bacteria, leads to a higher ampicillin sensitivity of the bacteria. This innovative strategy could generate multiple potent inhibitors for all types of beta-lactamases.

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