Structural and biochemical insights into the disulfide reductase mechanism of DsbD, an essential enzyme for neisserial pathogens
Roxanne P Smith, Biswaranjan Mohanty, Shakeel Mowlaboccus, Jason J Paxman, Martin L Williams, Stephen J Headey, Geqing Wang, Pramod Subedi, Bradley C Doak, Charlene M Kahler, Martin J Scanlon, Begona Heras
JOURNAL OF BIOLOGICAL CHEMISTRY | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2018
The worldwide incidence of neisserial infections, particularly gonococcal infections, is increasingly associated with antibiotic-resistant strains. In particular, extensively drug-resistant Neisseria gonorrhoeae strains that are resistant to third-generation cephalosporins are a major public health concern. There is a pressing clinical need to identify new targets for the development of antibiotics effective against Neisseria-specific processes. In this study, we report that the bacterial disulfide reductase DsbD is highly prevalent and conserved among Neisseria spp. and that this enzyme is essential for survival of N. gonorrhoeae DsbD is a membrane-bound protein that consists of two peripla..View full abstract
Awarded by Australian Research Council
Awarded by National Health and Medical Research Council
Awarded by Australian Research Council Future Fellowship
This work was supported by Australian Research Council Project Grant DP150102287 and National Health and Medical Research Council Project Grant APP1099151. The authors declare that they have no conflicts of interest with the contents of this article.Supported by National Health and Medical Research Council Grant APP546003.Supported by Australian Research Council Future Fellowship FT130100580.