By catalyzing oxidative protein folding, the bacterial disulfide bond protein A (DsbA) plays an
essential role in the assembly of many virulence factors. Predictably, DsbA disruption affects …

One approach to address antibiotic resistance is to develop drugs that interfere with
bacterial virulence. A master regulator of virulence in Gram-negative bacteria is the oxidative …

The disulfide bond (DSB) forming system and in particular DsbA, is a key bacterial oxidative
folding catalyst. Due to its role in promoting the correct assembly of a wide range of …

Abstract Aims: The intracellular pathogen Burkholderia pseudomallei causes the disease
melioidosis, a major source of morbidity and mortality in southeast Asia and northern …

Vibrio cholerae, the causative agent of the severe diarrheal disease cholera, has evolved
signal transduction systems to control co‐ordinately the expression of virulence …

The dramatic increase in the number of protein sequences and structures deposited in
biological databases has led to the development of many bioinformatics tools and programs …

The DsbA: DsbB redox machinery catalyzes disulfide bond formation in secreted proteins
and is required for bacterial virulence factor assembly. Both enzymes have been identified …

Background Bacterial D is ulfide b ond forming (Dsb) proteins facilitate proper folding and
disulfide bond formation of periplasmic and secreted proteins. Previously, we have shown …

Bacterial DsbA enzymes catalyze oxidative folding of virulence factors, and have been
identified as targets for antivirulence drugs. However, DsbA enzymes characterized to date …

In bacteria the formation of disulphide bonds is facilitated by a family of enzymes known as
the disulphide bond forming (Dsb) proteins, which, despite low sequence homology, belong …