Functional and evolutionary analyses of Helicobacter pylori HP0231 (DsbK) protein with strong oxidative and chaperone activity characterized by a highly diverged dimerization domain

Bocian-Ostrzycka, Katarzyna M.; Łasica, Anna M.; Dunin-Horkawicz, Stanisław; Grzeszczuk, Magdalena; Drabik, Karolina; Dobosz, Aneta M.; Godlewska, Renata; Nowak, Elżbieta; Collet, Jean-François; Jagusztyn-Krynicka, Elżbieta Katarzyna

doi:10.3389/fmicb.2015.01065

Cited by 15 publications

(40 citation statements)

References 65 publications

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“…However, this kind of designation should always be verified by in vitro or/and in vivo experiments. For instance, the Helicobacter pylori HP0231 dimeric oxidoreductase, which originally was classified as DsbG, turned out to possess both oxidation and isomerization activities [1,47,48,54]. Also, H. pylori thiol oxidoreductase HP0377 that is a CcmG protein responsible for cytochrome c biogenesis, was described as a DsbC homolog [70].…”

Section: Discussionmentioning

confidence: 99%

“…The DsbG/C-like family can be subdivided into two subgroups, one comprising Helicobacter proteins, including HP0231, which we and others have studied previously [47,48], and the other comprising C8J_1298 and its homologs from Campylobacter and Sulfurospirillum species. As mentioned above, most of the HP0231-like and C8J_1298-like proteins have the VcP cis-proline motif.…”

Section: C8j_1298 Genome Location and Phylogenetic Analysis Of Its Prmentioning

confidence: 97%

“…The protein was eluted with an imidazole gradient, using the NGC chromatography system (Bio-Rad). To obtain higher purity, proteins were next loaded onto The redox states of the analyzed C. jejuni proteins were visualized by alkylating the free cysteine residues using 4-acetamido-4'-maleimidylstilbene-2,2'-disulfonic acid (AMS, ThermoFisher Scientific) [1,47]. These agents can only modify covalently free thiols, resulting in a molecular mass increase of 490 Da (AMS).…”

Section: Protein Analysis and Biochemical Assaysmentioning

confidence: 99%

“…Reductase activity was assessed by an insulin precipitation assay [3,84] using human insulin solution (Sigma) Reactions (triplicate) were carried out in 200 μl of 100 mM sodium phosphate buffer, pH 7.0, 133 μM insulin, 1 mM dithiothreitol (DTT), 2 mM EDTA and 10 μM of C8J_1298 or EcDsbA or EcDsbC; reaction mixtures were incubated in a 96-well plate format at room temperature in a Sunrise™ (Tecan) plate reader [47]. Reactions were started by adding DTT to a final concentration of 1 mM.…”

Section: Insulin Reduction Assaymentioning

confidence: 99%

“…Oxidative folding of reduced RNaseA. In vitro oxidative folding of reduced, unfolded RNaseA (ruRNaseA) was performed with C8J_1298, EcDsbC and EcDsbA as described earlier [47]. Proteins were oxidized with 50 mM oxidized glutathione (GSSG) and incubated for 1 h at room temperature.…”

Section: Determination Of the Redox Potential Of C8j_1298 Proteinmentioning

confidence: 99%

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C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning

et al. 2020

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Posttranslational generation of disulfide bonds catalyzed by bacterial Dsb (disulfide bond) enzymes is essential for the oxidative folding of many proteins. Although we now have a good understanding of the Escherichia coli disulfide bond formation system, there are significant gaps in our knowledge concerning the Dsb systems of other bacteria, including Campylobacter jejuni, a food-borne, zoonotic pathogen. We attempted to gain a more complete understanding of the process by thorough analysis of C8J_1298 functioning in vitro and in vivo. C8J_1298 is a homodimeric thiol-oxidoreductase present in wild type (wt) cells, in both reduced and oxidized forms. The protein was previously described as a homolog of DsbC, and thus potentially should be active in rearrangement of disulfides. Indeed, biochemical studies with purified protein revealed that C8J_1298 shares many properties with EcDsbC. However, its activity in vivo is dependent on the genetic background, namely, the set of other Dsb proteins present in the periplasm that determine the redox conditions. In wt C. jejuni cells, C8J_1298 potentially works as a DsbG involved in the control of the cysteine sulfenylation level and protecting single cysteine residues from oxidation to sulfenic acid. A strain lacking only C8J_1298 is indistinguishable from the wild type strain by several assays recognized as the criteria to determine isomerization or oxidative Dsb pathways. Remarkably, in C. jejuni strain lacking DsbA1, the protein involved in generation of disulfides, C8J_1298 acts as an oxidase, similar to the homodimeric oxidoreductase of Helicobater pylori, HP0231. In E. coli, C8J_1298 acts as a bifunctional protein, also resembling HP0231. These findings are strongly supported by phylogenetic data. We also showed that CjDsbD (C8J_0565) is a C8J_1298 redox partner.

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Section: Discussionmentioning

confidence: 99%

Section: C8j_1298 Genome Location and Phylogenetic Analysis Of Its Prmentioning

confidence: 97%

Section: Protein Analysis and Biochemical Assaysmentioning

confidence: 99%

Section: Insulin Reduction Assaymentioning

confidence: 99%

Section: Determination Of the Redox Potential Of C8j_1298 Proteinmentioning

confidence: 99%

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C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning

et al. 2020

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Helicobacter pylori in the post-antibiotics era: from virulence factors to new drug targets and therapeutic agents

Al-Fakhrany,

Elekhnawy

2023

Arch Microbiol

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Helicobacter pylori is considered one of the most prevalent human pathogenic microbes globally. It is the main cause of a number of gastrointestinal ailments, including peptic and duodenal ulcers, and gastric tumors with high mortality rates. Thus, eradication of H. pylori is necessary to prevent gastric cancer. Still, the rise in antibiotic resistance is the most important challenge for eradication strategies. Better consideration of H. pylori virulence factors, pathogenesis, and resistance is required for better eradication rates and, thus, prevention of gastrointestinal malignancy. This article is aimed to show the role of virulence factors of H. pylori. Some are involved in its survival in the harsh environment of the human gastric lumen, and others are related to pathogenesis and the infection process. Furthermore, this work has highlighted the recent advancement in H. pylori treatment, as well as antibiotic resistance as a main challenge in H. pylori eradication. Also, we tried to provide an updated summary of the evolving H. pylori control strategies and the potential alternative drugs to fight this lethal resistant pathogen. Recent studies have focused on evaluating the efficacy of alternative regimens (such as sequential, hybrid, concomitant treatment, vonoprazan (VPZ)-based triple therapy, high-dose PPI-amoxicillin dual therapy, probiotics augmented triple therapy, or in combination with BQT) in the effective eradication of H. pylori. Thus, innovating new anti-H. pylori drugs and establishing H. pylori databanks are upcoming necessities in the near future.

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Bacterial thiol oxidoreductases — from basic research to new antibacterial strategies

Bocian-Ostrzycka

Grzeszczuk

Banaś

et al. 2017

Appl Microbiol Biotechnol

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The recent, rapid increase in bacterial antimicrobial resistance has become a major public health concern. One approach to generate new classes of antibacterials is targeting virulence rather than the viability of bacteria. Proteins of the Dsb system, which play a key role in the virulence of many pathogenic microorganisms, represent potential new drug targets. The first part of the article presents current knowledge of how the Dsb system impacts function of various protein secretion systems that influence the virulence of many pathogenic bacteria. Next, the review describes methods used to study the structure, biochemistry, and microbiology of the Dsb proteins and shows how these experiments broaden our knowledge about their function. The lessons gained from basic research have led to a specific search for inhibitors blocking the Dsb networks.

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Functional and evolutionary analyses of Helicobacter pylori HP0231 (DsbK) protein with strong oxidative and chaperone activity characterized by a highly diverged dimerization domain

Cited by 15 publications

References 65 publications

C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning

C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning

Helicobacter pylori in the post-antibiotics era: from virulence factors to new drug targets and therapeutic agents

Bacterial thiol oxidoreductases — from basic research to new antibacterial strategies

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