Selection of RNA aptamers against the M. tuberculosis EsxG protein using surface plasmon resonance-based SELEX

There are currently no molecular probes with high affinity and specificity to the EsxG protein that can be used to study it. Here we demonstrate the use of surface plasmon resonance-based systematic evolution of ligands by exponential enrichment (SELEX) to identify two aptamers, G43 and G78 that bind EsxG with high affinities, KD of 8.04 ± 1.90 nM and 78.85 ± 9.40 nM, respectively. Moreover, these aptamers preferentially bind EsxG over its homologue EsxA. Availability of such probes enables biological investigation of the role of this protein in mycobacteria and its potential as a biomarker for TB diagnosis.