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Updated: Aug 6, 2026

Immunization of Alpacas (Lama pacos) with Protein Antigens and Production of Antigen-specific Single Domain Antibodies
Published on: January 26, 2019
Structural basis for the inhibition of Trypanosoma brucei enolase by a camelid single-domain antibody
Zeng Li1, Natalia Smiejkowska2, Julie Vansevenant2
1Laboratory of Cellular and Immunology, Brussels Center for Immunology (BCIM), Department of Bioengineering Sciences, Vrije Universiteit Brussel, Brussels B-1050, Belgium; Laboratory of Medical Biochemistry (LMB) and the Infla-Med Center of Excellence, Department of Pharmaceutical Sciences, Universiteit of Antwerp, Wilrijk B-2610, Belgium.
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.
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