Journal article
Fragment library screening identifies hits that bind to the non-catalytic surface of Pseudomonas aeruginosa DsbA1
B Mohanty, K Rimmer, RM McMahon, SJ Headey, M Vazirani, SR Shouldice, M Coinçon, S Tay, CJ Morton, JS Simpson, JL Martin, MJ Scanlon
Plos One | PUBLIC LIBRARY SCIENCE | Published : 2017
Open access
Abstract
At a time when the antibiotic drug discovery pipeline has stalled, antibiotic resistance is accelerating with catastrophic implications for our ability to treat bacterial infections. Globally we face the prospect of a future when common infections can once again kill. Anti-virulence approaches that target the capacity of the bacterium to cause disease rather than the growth or survival of the bacterium itself offer a tantalizing prospect of novel antimicrobials. They may also reduce the propensity to induce resistance by removing the strong selection pressure imparted by bactericidal or bacteriostatic agents. In the human pathogen Pseudomonas aeruginosa, disulfide bond protein A (PaDsbA1) pl..
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Awarded by National Health and Medical Research Council
Funding Acknowledgements
The study was funded through a Linkage Grant from the Australian Research Council (arc.gov.au) (LP0990166), which was supported by an Industry Partner - Biota Holdings Ltd. JLM was supported by an Australian Research Council (arc.gov.au) Australian Laureate Fellowship during this research (FL0992138). RMM, MC and ST were supported by the same Laureate Award. RMM and BM were supported in part by a National Health and Medical Research Council (nhmrc.gov.au) Project Grant (1061241). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.