1. Fhua and HgbA, outer membrane proteins of Actinobacillus pleuropneumoniae: their role as virulence determinants.
- Author
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Shakarji L, Mikael LG, Srikumar R, Kobisch M, Coulton JW, and Jacques M
- Subjects
- Actinobacillus pleuropneumoniae classification, Actinobacillus pleuropneumoniae pathogenicity, Bacterial Outer Membrane Proteins metabolism, Bacterial Outer Membrane Proteins physiology, Bacterial Proteins genetics, Bacterial Proteins metabolism, Bacterial Proteins physiology, Carrier Proteins genetics, Carrier Proteins metabolism, Carrier Proteins physiology, Ferrichrome metabolism, Gene Expression Regulation, Bacterial, Hemoglobins metabolism, Iron metabolism, Mutation, Phylogeny, Serotyping, Siderophores metabolism, Substrate Specificity, Virulence genetics, Virulence Factors metabolism, Virulence Factors physiology, Actinobacillus pleuropneumoniae genetics, Bacterial Outer Membrane Proteins genetics, Virulence Factors genetics
- Abstract
For the recently described serotype 15 of biotype I and serotypes 13 and 14 of biotype II of Actinobacillus pleuropneumoniae, fhuA and hgbA were detected by polymerase chain reaction and DNA sequencing. To determine the substrate specificity of the iron receptors FhuA and HgbA and to study their role in the virulence of A. pleuropneumoniae, we used two isogenic A. pleuropneumoniae serotype 1 deletion mutants of fhuA and hgbA. Different sources of iron and siderophores were tested in growth promotion assays. FhuA and HgbA are specific for their ligands ferrichrome and hemoglobin, respectively. The virulence of the two deletion mutant strains was evaluated in experimental infections using specific pathogen-free piglets. While the fhuA mutant (DG02) was as highly virulent as the parental strain S4074, the virulence of the hgbA mutant (DeltahgbA) was reduced. Our data indicate that both FhuA and HgbA are conserved among all serotypes and biotypes of A. pleuropneumoniae and that HgbA, the receptor for porcine hemoglobin, may play a role in virulence.
- Published
- 2006
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