5O0W

Crystal structure of the complex between Nb474 and Trypanosoma congolense fructose-1,6-bisphosphate aldolase

Summary for 5O0W

• Entry DOI: 10.2210/pdb5o0w/pdb
• Descriptor: Fructose-bisphosphate aldolase, Nb474, GLYCEROL, ... (4 entities in total)
• Functional Keywords: complex, nanobody, aldolase, diagnosis, lyase
• Biological source: Trypanosoma congolense (strain IL3000); More
• Total number of polymer chains: 8
• Total formula weight: 234587.39

Authors

Pinto, J.,Magez, S.,Sterckx, Y. (deposition date: 2017-05-17, release date: 2017-09-27, Last modification date: 2024-10-09)

Primary citation

Pinto, J.,Odongo, S.,Lee, F.,Gaspariunaite, V.,Muyldermans, S.,Magez, S.,Sterckx, Y.G.
Structural basis for the high specificity of a Trypanosoma congolense immunoassay targeting glycosomal aldolase.
PLoS Negl Trop Dis, 11:e0005932-e0005932, 2017

PubMed Abstract: Animal African trypanosomosis (AAT) is a neglected tropical disease which imposes a heavy burden on the livestock industry in Sub-Saharan Africa. Its causative agents are Trypanosoma parasites, with T. congolense and T. vivax being responsible for the majority of the cases. Recently, we identified a Nanobody (Nb474) that was employed to develop a homologous sandwich ELISA targeting T. congolense fructose-1,6-bisphosphate aldolase (TcoALD). Despite the high sequence identity between trypanosomatid aldolases, the Nb474-based immunoassay is highly specific for T. congolense detection. The results presented in this paper yield insights into the molecular principles underlying the assay's high specificity.

PubMed: 28915239
DOI: 10.1371/journal.pntd.0005932

Experimental method

X-RAY DIFFRACTION (2.57 Å)