9SLQ

Trypanosome brucei enolase in complex with a camelid single-domain antibody

Summary for 9SLQ

• Entry DOI: 10.2210/pdb9slq/pdb
• Descriptor: phosphopyruvate hydratase, sdAbR1-10, GLYCEROL, ... (7 entities in total)
• Functional Keywords: enolase;single-domain antibody, cytosolic protein
• Biological source: Trypanosoma brucei; More
• Total number of polymer chains: 8
• Total formula weight: 255603.82

Authors

Sterckx, Y.G.-J. (deposition date: 2025-09-04, release date: 2026-08-05)

Primary citation

Li, Z.,Smiejkowska, N.,Vansevenant, J.,Mertens, J.,Van Wielendaele, P.,Pinto Torres, J.E.,Magez, S.,Sterckx, Y.G.
Structural basis for the inhibition of Trypanosoma brucei enolase by a camelid single-domain antibody.
Mol.Biochem.Parasitol., 267:111763-111763, 2026

PubMed Abstract: Trypanosoma 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.

PubMed: 42486369
DOI: 10.1016/j.molbiopara.2026.111763

Experimental method

X-RAY DIFFRACTION (2.33 Å)