title: Truncated surface protective antigen (SpaA) of Erysipelothrix rhusiopathiae serotype 1a elicits protection against challenge with serotypes 1a and 2b in pigs.
abstract: Erysipelothrix rhusiopathiae is a causal agent of swine erysipelas, which is of economic importance in the swine industry by virtue of causing acute septicemia, chronic arthritis, and endocarditis. However, little is known about the genetic properties of its protective antigens. Recently, a surface protective antigen (SpaA) gene was identified from serotype 2 in a mouse model. We cloned spaA from virulent strain Fujisawa (serotype 1a) and determined that the N-terminal 342 amino acids without C-terminal repeats of 20 amino acids have the ability to elicit protection in mice. Fusions of 342 amino acids of Fujisawa SpaA and histidine hexamer (HisSpa1.0) protected pigs against challenge with both serotype 1 and serotype 2, the most important serotypes in the swine industry. Pigs immunized with HisSpa1.0 reacted well with both HisSpa1.0 and intact SpaA by enzyme-linked immunosorbent assay and immunoblotting. Serum collected at the time of challenge from a pig immunized with HisSpa1. 0 markedly enhanced the in vitro phagocytic and killing activity of pig neutrophils against the bacteria. DNA sequences of protective regions of spaA genes from five strains of serotypes 1 and 2 were almost identical. The full DNA sequences also seemed to be conserved among strains of all 12 serotype reference strains harboring the spaA gene by restriction fragment length polymorphism analysis of PCR products. These results indicates that SpaA is a common protective antigen of serotypes 1 and 2 of E. rhusiopathiae in swine and will be a useful tool for development of new types of vaccines and diagnostic tools for effective control of the disease.
authors.affiliation: National Institute of Animal Health, Tsukuba, Ibaraki 305-0856, Japan. yumima@niah.affrc.go.jp
authors.forename: Y
authors.initials: Y
authors.lastname: Imada
authors.forename: N
authors.initials: N
authors.lastname: Goji
authors.forename: H
authors.initials: H
authors.lastname: Ishikawa
authors.forename: M
authors.initials: M
authors.lastname: Kishima
authors.forename: T
authors.initials: T
authors.lastname: Sekizaki
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000942:Antigens, Bacterial / Q000235:genetics / Q000276:immunology*; D000954:Antigens, Surface / Q000235:genetics / Q000276:immunology*; D001426:Bacterial Proteins; D001428:Bacterial Vaccines / Q000235:genetics / Q000276:immunology*; D001483:Base Sequence; D002846:Chromatography, Affinity; D004269:DNA, Bacterial; D004888:Erysipelothrix / Q000235:genetics / Q000276:immunology* / Q000302:isolation & purification; D004889:Erysipelothrix Infections / Q000517:prevention & control*; D005260:Female; D006639:Histidine / Q000276:immunology; D016056:Immunodominant Epitopes / Q000235:genetics / Q000276:immunology; D051379:Mice; D008969:Molecular Sequence Data; D009000:Monocytes / Q000276:immunology / Q000382:microbiology; D009504:Neutrophils / Q000276:immunology / Q000382:microbiology; D010587:Phagocytosis; D011817:Rabbits; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000276:immunology; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D012703:Serotyping; D013552:Swine; D014614:Vaccines, Synthetic / Q000235:genetics / Q000276:immunology*
chemical_list: D000942:Antigens, Bacterial; D000954:Antigens, Surface; D001426:Bacterial Proteins; D001428:Bacterial Vaccines; D004269:DNA, Bacterial; D016056:Immunodominant Epitopes; D011993:Recombinant Fusion Proteins; C114457:SpaA protein, Erysipelothrix rhusiopathiae; D014614:Vaccines, Synthetic; D006639:Histidine