title: Erysipelothrix rhusiopathiae YS-1 as a live vaccine vehicle for heterologous protein expression and intranasal immunization of pigs.
abstract: We have developed a system in which a foreign antigen is delivered and expressed on the surface of an attenuated strain of Erysipelothrix rhusiopathiae YS-1 and have examined the ability of a such recombinant E. rhusiopathiae strain to function as a mucosal vaccine vector. The C-terminal portion, including two repeat regions, R1 and R2, of the P97 adhesin of Mycoplasma hyopneumoniae strain E-1 was successfully translocated and expressed on the E. rhusiopathiae YS-1 cell surface after it was fused to SpaA.1, a cell surface protective antigen of E. rhusiopathiae. BALB/c mice subcutaneously immunized with the E. rhusiopathiae recombinant strains developed specific antibodies against SpaA.1 protein and were protected from lethal challenge with the highly virulent homologous E. rhusiopathiae Fujisawa-SmR strain, showing the efficacy of this heterologous-antigen expression system as a vaccine against E. rhusiopathiae infection. To determine whether protective immune responses are induced in target species, newborn, specific-pathogen-free piglets were immunized intranasally with a recombinant strain designated YS-19. The immunized piglets developed specific anti-SpaA.1 immunoglobulin G (IgG) antibodies in their serum and were protected from death by erysipelas, showing that mucosal vaccination of piglets with YS-19 induces systemic immune responses. Furthermore, YS-19-immunized piglets showed higher levels of P97-specific IgA antibodies in the respiratory tract than did YS-1-immunized piglets. Thus, E. rhusiopathiae YS-1 appears to be a promising vaccine vector for mucosal delivery that can induce local and systemic immune responses.
authors.affiliation: National Institute of Animal Health, Tsukuba, Ibaraki 305-0856, Japan. shimoji@affrc.go.jp
authors.forename: Yoshihiro
authors.initials: Y
authors.lastname: Shimoji
authors.forename: Eiji
authors.initials: E
authors.lastname: Oishi
authors.forename: Takashi
authors.initials: T
authors.lastname: Kitajima
authors.forename: Yoshihiro
authors.initials: Y
authors.lastname: Muneta
authors.forename: Shinya
authors.initials: S
authors.lastname: Shimizu
authors.forename: Yasuyuki
authors.initials: Y
authors.lastname: Mori
mesh_terms: D018829:Adhesins, Bacterial / Q000235:genetics* / Q000276:immunology; D000281:Administration, Intranasal; D000818:Animals; D000907:Antibodies, Bacterial / Q000276:immunology; D001428:Bacterial Vaccines / Q000235:genetics* / Q000276:immunology; D002462:Cell Membrane / Q000378:metabolism; D004888:Erysipelothrix / Q000235:genetics* / Q000276:immunology / Q000472:pathogenicity; D004889:Erysipelothrix Infections / Q000517:prevention & control; D005260:Female; D015870:Gene Expression; D005822:Genetic Vectors / Q000235:genetics* / Q000276:immunology; D007070:Immunoglobulin A / Q000276:immunology; D051379:Mice; D008807:Mice, Inbred BALB C; D011995:Recombination, Genetic; D012137:Respiratory System / Q000276:immunology; D013552:Swine; D014611:Vaccination; D014613:Vaccines, Attenuated; D014614:Vaccines, Synthetic / Q000235:genetics* / Q000276:immunology; D014774:Virulence
chemical_list: D018829:Adhesins, Bacterial; D000907:Antibodies, Bacterial; D001428:Bacterial Vaccines; D007070:Immunoglobulin A; C092236:P97 protein, Mycoplasma; D014613:Vaccines, Attenuated; D014614:Vaccines, Synthetic