The N-terminal domain of RTX toxin ApxI of Actinobacillus pleuropneumoniae elicits protective immunity in mice.
We expressed three Actinobacillus pleuropneumoniae ApxI deletion derivatives to map the domain that could induce protective immunity. Antiserum to ApxI N-terminal covered by residues 40 to 380 was found to neutralize ApxI hemolytic activity but not ApxIII cytotoxicity. When used as a subunit vaccine in mice, this recombinant N-terminal fragment elicited protection against lethal infection with heterologous A. pleuropneumoniae serovars.
Seah
J N
JN
Laboratory of Animal Health Biotechnology, Temasek Life Sciences Laboratory, The National University of Singapore, Singapore 117604, Singapore.
Frey
J
J
Kwang
J
J
D016977:Actinobacillus pleuropneumoniae / Q000276:immunology* / Q000472:pathogenicity; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000276:immunology*; D001428:Bacterial Vaccines / Q000276:immunology*; D006168:Guinea Pigs; D006460:Hemolysin Proteins; D007114:Immunization; D051379:Mice; D010446:Peptide Fragments / Q000276:immunology*; D011994:Recombinant Proteins / Q000276:immunology; D013552:Swine
D001426:Bacterial Proteins; D001428:Bacterial Vaccines; D006460:Hemolysin Proteins; D010446:Peptide Fragments; D011994:Recombinant Proteins; C087744:ApxI toxin, Bacteria