7pa5

Publication Abstract from PubMed

Three soluble single-domain fragments derived from the unique variable region of camelid heavy-chain antibodies (VHHs) against the CMY-2 beta-lactamase behaved as inhibitors. The structure of the complex VHH cAb(CMY-2)(254)/CMY-2 showed that the epitope is close to the active site and that the CDR3 of the VHH protrudes into the catalytic site. The beta-lactamase inhibition pattern followed a mixed profile with a predominant noncompetitive component. The three isolated VHHs recognized overlapping epitopes since they behaved as competitive binders. Our study identified a binding site that can be targeted by a new class of beta-lactamase inhibitors designed on the sequence of the paratope. Furthermore, the use of mono- or bivalent VHH and rabbit polyclonal anti-CMY-2 antibodies enables the development of the first generation of enzyme-linked immunosorbent assay (ELISA) for the detection of CMY-2 produced by CMY-2-expressing bacteria, irrespective of resistotype.

Development of Nanobodies as Theranostic Agents against CMY-2-Like Class C beta-Lactamases.,Cawez F, Mercuri PS, Morales-Yanez FJ, Maalouf R, Vandevenne M, Kerff F, Guerin V, Mainil J, Thiry D, Saulmont M, Vanderplasschen A, Lafaye P, Ayme G, Bogaerts P, Dumoulin M, Galleni M Antimicrob Agents Chemother. 2023 Apr 18;67(4):e0149922. doi: , 10.1128/aac.01499-22. Epub 2023 Mar 9. PMID:36892280^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.