9slq | pdb_00009slq
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Trypanosome brucei enolase in complex with a camelid single-domain antibody
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Structural highlights
FunctionPublication Abstract from PubMedTrypanosoma brucei is an extracellular protozoan that causes neglected tropical diseases in both humans and livestock. The parasite has a bipartite life cycle involving an insect vector and a mammalian host. Within the latter, it mainly thrives as a blood-borne parasite that relies on glycolysis to support its energy metabolism. It is for this reason that trypanosomal glycolytic enzymes have been investigated as potential targets for the development of trypanosome-killing drugs. Recent work from our lab has shown that they are also interesting biomarkers for the detection of active trypanosome infections. T. brucei enolase (TbrENO) is a trypanosomal glycolytic enzyme that has gathered interest in both drug and diagnostics development. In this paper, we report the discovery of a camelid single domain antibody (sdAb aka nanobody) that specifically recognises and inhibits TbrENO. The sdAb's inhibitory mechanism is unraveled through a combination of protein biochemistry, biophysics, and structural biology. Structural basis for the inhibition of Trypanosoma brucei enolase by a camelid single-domain antibody.,Li Z, Smiejkowska N, Vansevenant J, Mertens J, Van Wielendaele P, Pinto Torres JE, Magez S, Sterckx YG Mol Biochem Parasitol. 2026 Jul 22;267:111763. doi: , 10.1016/j.molbiopara.2026.111763. PMID:42486369[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 07:17, 5 August 2026.