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Infection and Immunity, January 2004, p. 260-268, Vol. 72, No. 1
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.1.260-268.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

L-Serine Catabolism via an Oxygen-Labile L-Serine Dehydratase Is Essential for Colonization of the Avian Gut by Campylobacter jejuni

Jyoti Velayudhan,1,{dagger} Michael A. Jones,2 Paul A. Barrow,2 and David J. Kelly1*

Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN,1 Institute for Animal Health, Compton, Berkshire, RG20 7NN, United Kingdom2

Received 3 June 2003/ Returned for modification 4 September 2003/ Accepted 15 October 2003

Campylobacter jejuni is a microaerophilic, asaccharolytic bacterium. The identity of the carbon and energy sources used by C. jejuni in vivo is unknown, but the genome sequence of strain NCTC11168 indicates the presence of genes for catabolism of a limited range of amino acids, including serine. Specific omission of L-serine from a defined medium containing a mixture of amino acids led to a dramatic decrease in cell yields. As C. jejuni does not have a biosynthetic serine requirement, this supports earlier suggestions that L-serine is a preferentially catabolized amino acid. Serine transport was found to be mediated by at least two systems in strain 11168; a high-capacity, low-affinity L-serine-specific system encoded by Cj1625c (sdaC) and a higher-affinity L-serine/L-threonine system responsible for residual L-serine transport in an sdaC mutant. Catabolism of L-serine to pyruvate and ammonia is carried out by SdaA (encoded by Cj1624c), which was overexpressed, purified, and shown to be an oxygen-labile iron-sulfur enzyme. L-Serine dehydratase activity in an sdaA mutant was reduced 10-fold compared to that in the wild type, but the residual activity (due to the anabolic L-threonine dehydratase) could not support either growth on or utilization of L-serine in defined media. However, although sdaA mutants showed no obvious growth defect in complex media, they completely failed to colonize 3-week-old chickens as assayed both by cloacal swabs taken over a 6-week period and by cecal colony counts postmortem. In contrast, the isogenic parent strain colonized chickens to high levels within 1 week of inoculation. The results show that an active SdaA is essential for colonization of the avian gut by C. jejuni and imply that catabolism of L-serine is crucially important for the growth of this bacterium in vivo.

* Corresponding author. Mailing address: Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Ct., Western Bank, Sheffield S10 2TN, United Kingdom. Phone: 44 (0)114 222 4414. Fax: 44 (0)114 272 8697. E-mail: d.kelly{at}sheffield.ac.uk.

Editor: J. T. Barbieri

{dagger} Present address: University of Washington, School of Medicine, Seattle, WA 98195-7242.

Infection and Immunity, January 2004, p. 260-268, Vol. 72, No. 1
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.1.260-268.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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