Affiliation:
1. Department of Infectious Diseases, Institute for Microbiology
2. Clinic for Pigs and Small Ruminants
3. Institute for Pathology, Veterinary School of Hannover, 30173 Hannover, Germany
Abstract
ABSTRACT
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
Δ
dmsA
, was constructed and examined in an aerosol infection model.
A. pleuropneumoniae
Δ
dmsA
was attenuated in acute disease, which suggests that genes involved in oxidative metabolism under anaerobic conditions might contribute significantly to
A. pleuropneumoniae
virulence.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
Cited by
50 articles.
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