Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases of Campylobacter jejuni and Their Impact on Bacterial Physiology and Pathogenesis

• Published in: International journal of molecular sciences Vol. 22; no. 24; p. 13451
• Main Authors: Banaś, Anna M, Bocian-Ostrzycka, Katarzyna M, Dunin-Horkawicz, Stanisław, Ludwiczak, Jan, Wilk, Piotr, Orlikowska, Marta, Wyszyńska, Agnieszka, Dąbrowska, Maria, Plichta, Maciej, Spodzieja, Marta, Polańska, Marta A, Malinowska, Agata, Jagusztyn-Krynicka, Elżbieta Katarzyna
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 15.12.2021; MDPI
• Subjects: Amino Acid Sequence; Amino acids; Antiinfectives and antibacterials; Bacteria; Bacterial Physiological Phenomena; Bacterial Proteins - metabolism; Campylobacter; Campylobacter jejuni; Campylobacter jejuni - pathogenicity; Campylobacter jejuni - physiology; Chemical bonds; Cooperation; crystal structure; disulfide bond; Disulfides - metabolism; Dsb proteins; E coli; Gram-positive bacteria; Guillain-Barre syndrome; Homology; Intestine; Microorganisms; Oxidation; Oxidation-Reduction; Oxidoreductases - genetics; Oxidoreductases - metabolism; Pathogenesis; Periplasm - metabolism; Periplasmic Proteins - genetics; Periplasmic Proteins - metabolism; Protein Disulfide-Isomerases - genetics; Protein Disulfide-Isomerases - metabolism; Protein transport; Proteins; Proteomics; Sequence Homology, Amino Acid; substrates; Surface charge; thiol oxidoreductase; Virulence; Dsb proteins; crystal structure; substrates; thiol oxidoreductase; disulfide bond; Campylobacter jejuni
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms222413451

The bacterial proteins of the Dsb family catalyze the formation of disulfide bridges between cysteine residues that stabilize protein structures and ensure their proper functioning. Here, we report the detailed analysis of the Dsb pathway of . The oxidizing Dsb system of this pathogen is unique because it consists of two monomeric DsbAs (DsbA1 and DsbA2) and one dimeric bifunctional protein (C8J_1298). Previously, we showed that DsbA1 and C8J_1298 are redundant. Here, we unraveled the interaction between the two monomeric DsbAs by in vitro and in vivo experiments and by solving their structures and found that both monomeric DsbAs are dispensable proteins. Their structures confirmed that they are homologs of EcDsbL. The slight differences seen in the surface charge of the proteins do not affect the interaction with their redox partner. Comparative proteomics showed that several respiratory proteins, as well as periplasmic transport proteins, are targets of the Dsb system. Some of these, both donors and electron acceptors, are essential elements of the respiratory process under oxygen-limiting conditions in the host intestine. The data presented provide detailed information on the function of the Dsb system, identifying it as a potential target for novel antibacterial molecules.