Inhibition of anthrax lethal factor by ssDNA aptamers.

Anthrax is caused by Bacillus anthracis, a bacterium that is able to secrete the toxins protective antigen, edema factor and lethal factor. Due to the high level of secretion from the bacteria and its severe virulence, lethal factor (LF) has been sought as a biomarker for detecting bacterial infection and as an effective target to neutralize toxicity. In this study, we found three aptamers, and binding affinity was determined by fluorescently labeled aptamers.

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

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.

A mechanistic explanation for pH-dependent ambient aquatic toxicity of Prymnesium parvum carter.

The harmful algal bloom species Prymnesium parvum has caused millions of dollars in damage to fisheries around the world. These fish kills have been attributed to P. parvum releasing a mixture of toxins in the water.