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Infection and Immunity, December 2003, p. 6784-6792, Vol. 71, No. 12
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.12.6784-6792.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Identification of Dimethyl Sulfoxide Reductase in Actinobacillus pleuropneumoniae and Its Role in Infection

Department of Infectious Diseases, Institute for Microbiology,¹ Clinic for Pigs and Small Ruminants,² Institute for Pathology, Veterinary School of Hannover, 30173 Hannover, Germany³

Received 3 April 2003/ Returned for modification 24 June 2003/ Accepted 3 September 2003

Actinobacillus pleuropneumoniae, the causative agent of porcine pleuropneumonia, is capable of persisting in oxygen-deprived surroundings, namely, tonsils and sequestered necrotic lung tissue. Utilization of alternative terminal electron acceptors in the absence of oxygen is a common strategy in bacteria under anaerobic growth conditions. In an experiment aimed at identification of genes expressed in vivo, the putative catalytic subunit DmsA of anaerobic dimethyl sulfoxide reductase was identified in an A. pleuropneumoniae serotype 7 strain. The 90-kDa protein exhibits 85% identity to the putative DmsA protein of Haemophilus influenzae, and its expression was found to be upregulated under anaerobic conditions. Analysis of the unfinished A. pleuropneumoniae genome sequence revealed putative open reading frames (ORFs) encoding DmsB and DmsC proteins situated downstream of the dmsA ORF. In order to investigate the role of the A. pleuropneumoniae DmsA protein in virulence, an isogenic deletion mutant, A. pleuropneumoniae dmsA, was constructed and examined in an aerosol infection model. A. pleuropneumoniae dmsA was attenuated in acute disease, which suggests that genes involved in oxidative metabolism under anaerobic conditions might contribute significantly to A. pleuropneumoniae virulence.

Editor: B. B. Finlay

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