Utilization of host‐derived cysteine‐containing peptides overcomes the restricted sulphur metabolism of Campylobacter jejuni. Issue 6 (25th August 2014)

• Record Type: Journal Article
• Authors: Vorwerk, Hanne; Mohr, Juliane; Huber, Claudia; Wensel, Olga; Schmidt‐Hohagen, Kerstin; Gripp, Eugenia; Josenhans, Christine; Schomburg, Dietmar; Eisenreich, Wolfgang; Hofreuter, Dirk
• Is Part Of: Molecular microbiology. Volume 93:Issue 6(2014)
• Page Start: 1224
• Page End: 1245
• Publication Date: 2014-08-25
• Subjects: Molecular microbiology -- Periodicals; 572.829
• DOI: 10.1111/mmi.12732
• Languages: English
• ISSNs: 0950-382X

Abstract

<abstract abstract-type="main"> <title>Summary</title> <p>The non‐glycolytic food‐borne pathogen <italic>C</italic><italic>ampylobacter jejuni</italic> successfully colonizes the intestine of various hosts in spite of its restricted metabolic properties. While several amino acids are known to be used by <italic>C</italic><italic>. jejuni</italic> as energy sources, none of these have been found to be essential for growth. Here we demonstrated through phenotype microarray analysis that cysteine utilization increases the metabolic activity of <italic>C</italic><italic>. jejuni</italic>. Furthermore, cysteine was crucial for its growth as <italic>C</italic><italic>. jejuni</italic> was unable to synthesize it from sulphate or methionine. Our study showed that <italic>C</italic><italic>. jejuni</italic> compensates this limited anabolic capacity by utilizing sulphide, thiosulphate, glutathione and the dipeptides γGlu–Cys, Cys–Gly and Gly–Cys as sulphur sources and cysteine precursors. A panel of <italic>C</italic><italic>. jejuni</italic> mutants in putative peptidases and peptide transporters were generated and tested for their participation in the catabolism of the cysteine‐containing peptides, and the predicted transporter protein CJJ81176_0236 was discovered to facilitate the growth with the dipeptide Cys–Gly, Ile–Arg and Ile–Trp. It was named <italic>C</italic><italic>ampylobacter</italic> peptide transporter A (CptA) and is the first representative of the oligopeptide transporter OPT family demonstrated to participate in the glutathione‐derivative Cys–Gly catabolism in prokaryotes. Our study provides new insights into how host‐ and microbiota‐derived substrates like sulphide, thiosulphate and short peptides are used by <italic>C</italic><italic>. jejuni</italic> to compensate its restricted metabolic capacities.</p> </abstract>