Mutation in the LPS outer core biosynthesis gene, galU, affects LPS interaction with the RTX toxins ApxI and ApxII and cytolytic activity of Actinobacillus pleuropneumoniae serotype 1: Mol.Microbiol.

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TypeArticle
Journal titleMol.Microbiol.
Volume70
Issue1
Pages221235; # of pages: 15
SubjectActinobacillus; Actinobacillus Infections; Actinobacillus pleuropneumoniae; Affect; Animals; assay; Bacteria; bacterial; Bacterial Proteins; binding; biosynthesis; Canada; Carrier Proteins; Cloning,Molecular; core oligosaccharide; Cytotoxins; DIFFERENCE; Enzyme-Linked Immunosorbent Assay; EXPRESSION; GENE; Gene Expression; Genes,Bacterial; genetics; Hemolysin Proteins; interaction; LIPOPOLYSACCHARIDE; Lipopolysaccharides; LPS; Macrophages; Macrophages,Alveolar; metabolism; Microbiology; MOLECULE; MUTANT; Mutation; oligosaccharide; pathogenicity; PIGS; Pleuropneumoniae; protein; Protein Interaction Domains and Motifs; Proteins; RESIDUES; RESONANCE; Reverse Transcriptase Polymerase Chain Reaction; Rna; RNA,Bacterial; secretion; SEROTYPE; surface; Surface Plasmon Resonance; Swine; Swine Diseases; TRISACCHARIDE; veterinary; Virulence; Virulence Factors
AbstractLipopolysaccharides (LPS) and Apx toxins are major virulence factors of Actinobacillus pleuropneumoniae, a pathogen of the respiratory tract of pigs. Here, we evaluated the effect of LPS core truncation in haemolytic and cytotoxic activities of this microorganism. We previously generated a highly attenuated galU mutant of A. pleuropneumoniae serotype 1 that has an LPS molecule lacking the GalNAc-Gal II-Gal I outer core residues. Our results demonstrate that this mutant exhibits wild-type haemolytic activity but is significantly less cytotoxic to porcine alveolar macrophages. However, no differences were found in gene expression and secretion of the haemolytic and cytotoxic toxins ApxI and ApxII, both secreted by A. pleuropneumoniae serotype 1. This suggests that the outer core truncation mediated by the galU mutation affects the toxins in their cytotoxic activities. Using both ELISA and surface plasmon resonance binding assays, we demonstrate a novel interaction between LPS and the ApxI and ApxII toxins via the core oligosaccharide. Our results indicate that the GalNAc-Gal II-Gal I trisaccharide of the outer core is fundamental to mediating LPS/Apx interactions. The present study suggests that a lack of binding between LPS and ApxI/II affects the cytotoxicity and virulence of A. pleuropneumoniae
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberRAMJEET2008
NPARC number9379186
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Record identifier72c6620f-7c5f-4ad4-9656-6ba24d45b300
Record created2009-07-10
Record modified2016-05-09
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