Journal article

The multifunctional enzyme S-adenosylhomocysteine/methylthioadenosine nucleosidase is a key metabolic enzyme in the virulence of Salmonella enterica var Typhimurium

Asma U Husna, Nancy Wang, Jonathan J Wilksch, Hayley J Newton, Dianna M Hocking, Iain D Hay, Simon A Cobbold, Mark R Davies, Malcolm J McConville, Trevor Lithgow, Richard A Strugnell

Biochemical Journal | PORTLAND PRESS LTD | Published : 2019

Abstract

Key physiological differences between bacterial and mammalian metabolism provide opportunities for the development of novel antimicrobials. We examined the role of the multifunctional enzyme S-adenosylhomocysteine/Methylthioadenosine (SAH/MTA) nucleosidase (Pfs) in the virulence of S. enterica var Typhimurium (S. Typhimurium) in mice, using a defined Pfs deletion mutant (i.e. Δpfs). Pfs was essential for growth of S. Typhimurium in M9 minimal medium, in tissue cultured cells, and in mice. Studies to resolve which of the three known functions of Pfs were key to murine virulence suggested that downstream production of autoinducer-2, spermidine and methylthioribose were non-essential for Salmon..

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Grants

Awarded by National Health and Medical Research Council


Awarded by Australian Research Council Laureate Fellowship


Funding Acknowledgements

The authors acknowledge the support of the National Health and Medical Research Council in providing a Program Grant to TL and RAS (APP1092262) and an Australian Research Council Laureate Fellowship in support of TL (FL130100038).