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β-Lactamase Inhibitors Derived from Single-Domain Antibody Fragments Elicited in the Camelidae
Open accessAbstract
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 β-lactamases has lead to the isolation of such single-domain antibody fragments specifically recognizing and inhibiting those β-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 β-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 β-lactamases.
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Naturally occurring antibodies devoid of light chains
Hamers-Casterman, C., Atarhouch, T., Muyldermans, S., Robinson, G., Hammers, C., Songa, E. B., Bendahman, N., & Hammers, R. (1993) · Nature · doi:10.1038/363446a0 · Cited by 3,241
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Nanobodies: natural single-domain antibodies
Muyldermans, S. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-063011-092449 · Cited by 2,304
Self-citationThree Decades of β-Lactamase Inhibitors
Drawz, S. M., & Bonomo, R. A. (2010) · Clinical Microbiology Reviews · doi:10.1128/cmr.00037-09 · Cited by 1,709
Activation and allosteric modulation of a muscarinic acetylcholine receptor
Kruse, A. C., Ring, A. M., Manglik, A., Hu, J., Hu, K., Eitel, K., Hübner, H., Pardon, E., Valant, C., Sexton, P. M., et al. (2013) · Nature · doi:10.1038/nature12735 · Cited by 893
Properties, production, and applications of camelid single-domain antibody fragments
Harmsen, M. M., & De Haard, H. J. (2007) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-007-1142-2 · Cited by 809
“However, antigen binding by the C-terminal VHH in such fusions can be compromised (Conrath et al. 2001b) presumably because of steric hindrance by the N-terminal VHH.”
BackgroundMolecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies
De Genst, E., Silence, K., Decanniere, K., Conrath, K., Loris, R., Kinne, J., Muyldermans, S., & Wyns, L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505379103 · Cited by 676
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Metadata
- Authors
- Conrath, K. E., Lauwereys, M., Galleni, M., Matagne, A., Frère, J.-M., Kinne, J., Wyns, L., & Muyldermans, S.
- Venue
- Antimicrobial Agents and Chemotherapy
- Publisher
- American Society for Microbiology
- Published
- 2001-10
- Volume
- 45
- Issue
- 10
- Pages
- 2807-2812
- ISSN
- 0066-4804 (ISSN-L)
- 1098-6596
- OpenAlex
- W2161709523
- Cited by
- 347
- References
- 1
- FWCI
- 3.93
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Conrath, K. E., Lauwereys, M., Galleni, M., Matagne, A., Frère, J.-M., Kinne, J., Wyns, L., & Muyldermans, S. (2001). β-Lactamase Inhibitors Derived from Single-Domain Antibody Fragments Elicited in the Camelidae. Antimicrobial Agents and Chemotherapy. https://doi.org/10.1128/aac.45.10.2807-2812.2001
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