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Beta-lactamase inhibitors derived from single-domain antibody fragments elicited in the camelidae
Publication Type:
Journal ArticleSource:
Volume 45, Issue 10, p.2807 - 2812 (2001)URL:
PM:11557473Keywords:
Amino Acid Sequence; Ampicillin; pharmacology; Animals; Antibody Specificity; Bacterial Proteins; Camels; immunology; Escherichia coli; drug effects; enzymology; Immunoglobulin Fragments; isolation & purification; Male; Molecular Sequence Data; PenicillinAbstract:
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
Notes:
DA - 20010914
IS - 0066-4804 (Print)
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
RN - 0 (Bacterial Proteins)
RN - 0 (Immunoglobulin Fragments)
RN - 0 (Penicillins)
RN - 0 (beta-lactamase-inhibitor protein, Streptomyces)
RN - 0 (immunoglobulin Fv)
RN - 69-53-4 (Ampicillin)
RN - EC 3.5.2.6 (beta-Lactamases)
SB - IM