The evolutionary origin of host association in the Rickettsiales

ME Schön, J Martijn, J Vosseberg, S Köstlbacher… - Nature …, 2022 - nature.com
The evolution of obligate host-association of bacterial symbionts and pathogens remains
poorly understood. The Rickettsiales are an alphaproteobacterial order of obligate …

Four structural subclasses of the antivirulence drug target disulfide oxidoreductase DsbA provide a platform for design of subclass-specific inhibitors

RM McMahon, L Premkumar, JL Martin - Biochimica et Biophysica Acta …, 2014 - Elsevier
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 …

Life inside and out: making and breaking protein disulfide bonds in Chlamydia

S Christensen, RM McMahon, JL Martin… - Critical reviews in …, 2019 - Taylor & Francis
Disulphide bonds are widely used among all domains of life to provide structural stability to
proteins and to regulate enzyme activity. Chlamydia spp. are obligate intracellular bacteria …

The Scs disulfide reductase system cooperates with the metallochaperone CueP in Salmonella copper resistance

P Subedi, JJ Paxman, G Wang, AA Ukuwela… - Journal of Biological …, 2019 - ASBMB
The human pathogen Salmonella enterica serovar Typhimurium (S. Typhimurium) contains
a complex disulfide bond (Dsb) catalytic machinery. This machinery encompasses multiple …

Disulfide isomerase activity of the dynamic, trimeric Proteus mirabilis ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB

EJ Furlong, HG Choudhury, F Kurth, AP Duff… - Journal of Biological …, 2018 - ASBMB
Correct disulfide bond formation is essential for proper folding of many proteins, including
bacterial virulence factors. The suppressor of copper sensitivity (Scs) proteins have roles in …

Structural and Biochemical Characterization of Chlamydia trachomatis DsbA Reveals a Cysteine-Rich and Weakly Oxidising Oxidoreductase

S Christensen, MK Grøftehauge, K Byriel, WM Huston… - PLoS …, 2016 - journals.plos.org
The Gram negative bacteria Chlamydia trachomatis is an obligate intracellular human
pathogen that can cause pelvic inflammatory disease, infertility and blinding trachoma. C …

Oxidoreductase disulfide bond proteins DsbA and DsbB form an active redox pair in Chlamydia trachomatis, a bacterium with disulfide dependent infection and …

S Christensen, MA Halili, N Strange, GA Petit… - PLoS …, 2019 - journals.plos.org
Chlamydia trachomatis is an obligate intracellular bacterium with a distinctive biphasic
developmental cycle that alternates between two distinct cell types; the extracellular …

The evolutionary origin of host association in an ancient bacterial clade

ME Schön, J Martijn, J Vosseberg, S Köstlbacher… - bioRxiv, 2021 - biorxiv.org
The evolution of obligate host-association of bacterial symbionts and pathogens remains
poorly understood. The Rickettsiales represent an order of obligate alphaproteobacterial …

Engineering of the Dsb (disulfide bond) proteins–contribution towards understanding their mechanism of action and their applications in biotechnology and medicine

AM Banaś, KM Bocian-Ostrzycka… - Critical reviews in …, 2019 - Taylor & Francis
The Dsb protein family in prokaryotes catalyzes the generation of disulfide bonds between
thiol groups of cysteine residues in nascent proteins, ensuring their proper three …

[PDF][PDF] The atypical thiol–disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase

PM Walden, AE Whitten, L Premkumar… - … Section D: Structural …, 2019 - journals.iucr.org
Disulfide-bond-forming (DSB) oxidative folding enzymes are master regulators of virulence
that are localized to the periplasm of many Gram-negative bacteria. The archetypal DSB …