Screening and characterization of high-affinity ssDNA aptamers against anthrax protective antigen

  • Choi J
  • Kim S
  • Lahousse M
 et al. 
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The protective antigen (PA) of Bacillus anthracis is a secreted protein that functions as a critical virulence factor. Protective antigen has been selected as a biomarker in detecting bacterial infection. The in vitro selection method, systematic evolution of ligands by exponential enrichment (SELEX), was used to find single-stranded DNAs that were tightly bound to PA. After 8 rounds of the SELEX process with PA, 4 different oligonucleotides (referred to as aptamers) that contain a 30-residue ssDNA sequence were identified. Dissociation constant (K(d)) values with Cy3-attached aptamers were determined via fluorophotometry to be within a nanomolar range. The authors attempted to visualize the detection of PA using an aptamer-based enzyme-linked immunosorbent assay method, which has proven to be successful within a nanomolar K(d) value range. Furthermore, 2 of the 4 aptamers exhibited specificity to PA against bovine serum albumin and bovine serum. The results of this study demonstrate the analytical potential of an oligonucleotide-based biosensor for a wide variety of applications, particularly in diagnosing disease through specific protein biomarkers.

Author-supplied keywords

  • Bacillus anthracis
  • anthrax
  • aptamer
  • protective antigen

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  • Ji Sun Choi

  • Sang Gon Kim

  • Mieke Lahousse

  • Hye Yeon Park

  • Hae Chul Park

  • Byeongmoon Jeong

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