Journal article
Trehalose 6-phosphate phosphatases of Pseudomonas aeruginosa
M Cross, S Biberacher, SY Park, S Rajan, P Korhonen, RB Gasser, JS Kim, MJ Coster, A Hofmann
FASEB Journal | Published : 2018
Abstract
The opportunistic bacteriumPseudomonas aeruginosa has been recognized as an important pathogen of clinical relevance and is a leading cause of hospital-acquired infections. The presence of a glycolytic enzyme in Pseudomonas,whichisknowntobe inhibitedbytrehalose 6-phosphate (T6P) inother organisms, suggests that these bacteria may be vulnerable to the detrimental effects of intracellular T6P accumulation. In the present study, we explored the structural and functional properties of trehalose 6-phosphate phosphatase (TPP) in P. aeruginosa in support of future target-baseddrug discovery.Asurvey of genomes revealedthe existence of 2TPPgeneswitheither chromosomal or extrachromosomal location. Bot..
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Awarded by Australian Research Council
Funding Acknowledgements
Research in the investigators' laboratories was funded by the Australian Research Council (to A.H. and R.B.G.), the Rebecca L. Cooper Medical Research Foundation (to A.H.), and the Chonnam National University (2015-0597, to J.-S.K.). The Equity Trustees Ph.D. Scholarship and the Australian Government Research Training Program Scholarship (to M.C.), as well as support by the German Academic Exchange Service through DAAD RISE and PROMOS scholarships (to S.B.) are gratefully acknowledged. Mass spectrometric analysis was undertaken at the Australian Proteome Analysis Facility, and the infrastructure was provided by the Australian Government through the National Collaborative Research Infrastructure Strategy. The authors declare no conflicts of interest.