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Updated: Aug 26, 2026
Double Labeling Immunofluorescence using Antibodies from the Same Species to Study Host-Pathogen Interactions
Published on: July 10, 2021
Correlation between conformation and antibody binding: NMR structure of cross-reactive peptides from T. cruzi, human
M R Soares1, P M Bisch, A C Campos de Carvalho
1Instituto de Biofísica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, 21941-590 Rio de Janeiro, RJ, Brazil.
Abstract:
The structure of peptides corresponding to the C-terminal residues from Trypanosoma cruzi (R13), human (H13) and Leishmania braziliensis (A13) ribosomal proteins were determined using nuclear magnetic resonance. Although there is only one amino acid difference between them, the peptides present distinct structures in solution: R13 adopts a random coil conformation while H13 and A13 form a bend. Interaction of these peptides with polyclonal antibodies from chronic Chagas' disease patients and a monoclonal antibody raised against T. cruzi ribosomal P2beta protein was probed by transferred NOE. The results show that the flexibility of R13 is fundamental for the binding to the antibody.
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