Solubilization and Characterization of a Protective Antigen of
            <i>Erysipelothrix rhusiopathiae</i>

White, R. R.; Verwey, W. F.

doi:10.1128/iai.1.4.387-393.1970

Cited by 18 publications

(12 citation statements)

References 5 publications

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“…It has been reported that the protective antigen of E. rhusiopathiae is also present in the culture supernatant of the organism and that antiserum against the culture supernatant fluids is protective (8,9,15,16). Although we found that SpaA.1 is also present in the culture supernatant, we do not yet know the relationship between the bound SpaA.…”

Section: Discussioncontrasting

confidence: 74%

“…Although we found that SpaA.1 is also present in the culture supernatant, we do not yet know the relationship between the bound SpaA. the protective antigens found in the culture supernatant reported so far (8,9,15,16).…”

Section: Discussionmentioning

confidence: 56%

“…It has been reported that a 200-kDa glycolipoprotein complex in the culture supernatant is a protective antigen of E. rhusiopathiae (15,16). This antigen was able to adsorb passively protective antibodies from rabbit antiserum produced by immunization with whole culture, suggesting that this molecule is a major protective antigen of the organism.…”

mentioning

confidence: 93%

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Immunological Characterization of a Protective Antigen of Erysipelothrix rhusiopathiae: Identification of the Region Responsible for Protective Immunity

1999

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The gene encoding a protective protein antigen of the gram-positive bacterium Erysipelothrix rhusiopathiae, an important veterinary pathogen responsible for erysipelas in swine and a variety of diseases in animals, was cloned and sequenced. The gene encodes a polypeptide of 597 amino acids plus a putative signal sequence of 29 amino acids, resulting in a mature protein with a molecular mass of 69,017 Da. Sequence analysis of the gene product revealed a C-terminal region composed of nine tandem repeats of 20 amino acids and a total sequence that is nearly identical to that of the 64-kDa cell surface protein (SpaA) of the bacterium. Because of this similarity, the protein was designated SpaA.1. In this study, we examined whether the SpaA.1 protein could induce protective antibodies and whether we could identify the region involved in protective immunity. Both the mature SpaA.1 protein and its C-terminal repeat region, but not the N-terminal segment, were expressed in Escherichia coli and purified as a histidine-tagged fusion recombinant protein. Rabbit antiserum raised against the mature SpaA.1 protein passively protected mice from lethal challenge with a virulent homologous strain, Fujisawa-SmR, suggesting that protection is mediated by humoral antibodies. To determine which domain of the SpaA.1 protein is responsible for the observed protection, mice were actively immunized with either the mature SpaA.1 protein or the C-terminal repeat region and then challenged with Fujisawa-SmR. The result showed that mice immunized with the mature SpaA.1 protein, but not the Cterminal repeat region, were protected, suggesting that the protection-eliciting epitope(s) is located within the N-terminal two-thirds of the SpaA.1 molecule. This was confirmed by passive immunization experiments in which the protective activity of rabbit antiserum, raised against mature SpaA.1 protein, was not abolished by absorption with the purified recombinant C-terminal repeat region. In addition, antibodies specific for the C-terminal repeat region were unable to protect mice from lethal challenge. These results show that the N-terminal two-thirds of the SpaA.1 molecule may constitute a good vaccine candidate against erysipelas.

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Section: Discussioncontrasting

confidence: 74%

Section: Discussionmentioning

confidence: 56%

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Immunological Characterization of a Protective Antigen of Erysipelothrix rhusiopathiae: Identification of the Region Responsible for Protective Immunity

1999

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“…Although protective antisera for passive immunization have been available for many years, the identity of the protective antigen(s) has not been clearly established. White and Verwey (28,29) described a large-molecular-weight protective antigen in culture supernatants; more recently, Lachmann and Deicher (12) have described smaller-molecular-weight antigenic components by immunoblotting.…”

mentioning

confidence: 99%

Cloning and expression in Escherichia coli of a protective antigen of Erysipelothrix rhusiopathiae

Galán

Timoney

1990

Infect Immun

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Erysipelothrix rhusiopathiae is a primary pathogen of swine and turkeys and sporadic cause of disease in a variety of other hosts, including humans. A genomic library of the highly virulent strain of E. rhusiopathiae E1-6P was constructed in the expression-cloning vector Xgtll and screened with serum from a pig convalescent from an E. rhusiopathiae experimental infection. Immunoreactive clones were screened for their ability to protectively immunized mice. Two clones, AgtlllersA and Agtll/ersB, were obtained that protected mice against challenge with E. rhusiopathiae E1-6P. Antisera against the recombinant clones reacted with polypeptides of molecular weights 66,000, 64,000, and 43,000 in detergent-solubilized surface antigen preparations and whole-cell lysates of E. rhusiopathiae. These polypeptides were also the major antigens recognized by convalescent pig serum when reacted with the same preparations. Western immunoblot and Southern blot analysis revealed that the cloned genes and gene products were present in all of the E. rhusiopathiae strains tested.

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“…Already in 1970 a protective antigen was described from an E. rhusiopathiae culture (86). In 1990, a 64 to 66-kDa protein in cell wall extracts was shown to be protective (125).…”

Section: Protective Antigensmentioning

confidence: 99%

Erysipelothrix Spp.: Past, Present, and Future Directions in Vaccine Research

2020

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Solubilization and Characterization of a Protective Antigen of Erysipelothrix rhusiopathiae

Cited by 18 publications

References 5 publications

Immunological Characterization of a Protective Antigen of Erysipelothrix rhusiopathiae: Identification of the Region Responsible for Protective Immunity

Immunological Characterization of a Protective Antigen of Erysipelothrix rhusiopathiae: Identification of the Region Responsible for Protective Immunity

Cloning and expression in Escherichia coli of a protective antigen of Erysipelothrix rhusiopathiae

Erysipelothrix Spp.: Past, Present, and Future Directions in Vaccine Research

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