title: The N-terminal domain of RTX toxin ApxI of Actinobacillus pleuropneumoniae elicits protective immunity in mice.
abstract: 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.
authors.affiliation: Laboratory of Animal Health Biotechnology, Temasek Life Sciences Laboratory, The National University of Singapore, Singapore 117604, Singapore.
authors.forename: J N
authors.initials: JN
authors.lastname: Seah
authors.forename: J
authors.initials: J
authors.lastname: Frey
authors.forename: J
authors.initials: J
authors.lastname: Kwang
mesh_terms: 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
chemical_list: D001426:Bacterial Proteins; D001428:Bacterial Vaccines; D006460:Hemolysin Proteins; D010446:Peptide Fragments; D011994:Recombinant Proteins; C087744:ApxI toxin, Bacteria