ArticleClinical and vaccine immunology : CVI2007
Genetic and antigenic diversity of the surface protective antigen proteins of Erysipelothrix rhusiopathiae.
Article in Clinical and vaccine immunology : CVI, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 67 citations in OpenAlex.
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- Serotypes, Antibiotic Susceptibility, Genotypic Virulence Profiles and SpaA Variants ofPathogens (Basel, Switzerland) · 2023Article
- Population Structure and Genomic Characteristics of AustralianMicroorganisms · 2023Article
- Pathology, microbiology, and genetic diversity associated withFrontiers in microbiology · 2023Article
- The Swine Erysipelas Vaccine SER-ME Effectively Protects Pigs against Challenge with theVeterinary sciences · 2022Article
- Screening immune adjuvants for an inactivated vaccine againstFrontiers in veterinary science · 2022Article
- Comparative genomics of a novel clade shed light on the evolution of the genus Erysipelothrix and characterise an emerging species.Scientific reports · 2021Article
- Serovars and SpaA Types of Erysipelothrix rhusiopathiae Isolated from Pigs in Japan from 2012 to 2019.Current microbiology · 2021Article
- Draft genome sequence data and comparative analysis of3 Biotech · 2020Article
- Review
- Genomic and Immunogenic Protein Diversity ofFrontiers in microbiology · 2020Article
- Disassociation of Spa type and serovar of an Erysipelothrix rhusiopathiae serovar 6 strain isolated from a diseased pig.Journal of veterinary diagnostic investigation : official publication of the American Association of Veterinary Laboratory Diagnosticians, Inc · 2019Article
- Article
- Microcrystalline Cellulose for Delivery of Recombinant Protein-Based Antigen against Erysipelas in Mice.BioMed research international · 2018Article
- Isolation and Detection ofIranian journal of medical sciences · 2017Article
- Pathogenic characterization of Erysipelothrix rhusiopathiae Met-203 type SpaA strains from chronic and subacute swine erysipelas in Japan.The Journal of veterinary medical science · 2017Article
- Article
- A combinational approach of multilocus sequence typing and other molecular typing methods in unravelling the epidemiology of Erysipelothrix rhusiopathiae strains from poultry and mammals.Veterinary research · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The surface protective antigen (Spa) protein of Erysipelothrix rhusiopathiae has been shown to be highly immunogenic and is a potential candidate for a new vaccine against erysipelas. In this study, we cloned and sequenced spa genes from all E. rhusiopathiae serovar reference strains as well as from a serovar 18 strain which was not classified as any species in the genus Erysipelothrix. Sequence analysis revealed that the Spa proteins could be classified into three molecular species, including SpaA, which was previously found in serovars 1a and 2, and the newly designated SpaB and SpaC proteins. The SpaA protein is produced by E. rhusiopathiae serovars 1a, 1b, 2, 5, 8, 9, 12, 15, 16, 17, and N, the SpaB protein is produced by E. rhusiopathiae serovars 4, 6, 11, 19, and 21, and the SpaC protein is produced only by serovar 18. The amino acid sequence similarity was high among members of each Spa type (96 to 99%) but low between different Spa types ( approximately 60%). The greatest diversity in Spa proteins was found in the N-terminal half of the molecule (50 to 57% similarity), which was shown to be involved in immunoprotection. Coinciding with this, immunoblot analysis revealed that rabbit antisera specific to each Spa reacted strongly with the homologous Spa protein but weakly with heterologous Spa proteins. A mouse cross-protection study showed that the three recombinant Spa (rSpa) proteins elicited complete protection against challenge with homologous strains but that the level of protection against challenge with heterologous strains varied depending on the rSpa protein used for immunization. Our study is the first to demonstrate sequence and antigenic diversity in Spa proteins and to indicate that rSpaC may be the most promising antigen for use as a vaccine component because of its broad cross-protectiveness.
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