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PubMed1994

Presence of a capsule in Erysipelothrix rhusiopathiae and its relationship to virulence for mice.

Three avirulent insertional mutants of Erysipelothrix rhusiopathiae were obtained by the technique of transposon mutagenesis with the self-conjugative transposon Tn916. The interactions between murine polymorphonuclear leukocytes and parent and mutant strains were studied in vitro. In the presence of normal serum, the virulent parent strain was resistant to phagocytosis, whereas the avirulent mutant strains were efficiently phagocytosed. In the presence of immune serum, the parent and the mutant strains were both efficiently phagocytosed. Electron microscopic examination of the parent strain demonstrated the presence of a structure resembling a capsule which was absent on the mutant strains, suggesting that a capsule may be involved in virulence. This was confirmed in studies in which an avirulent mutant strain reverted to virulence following acquisition of a capsule when the transposon was lost by spontaneous excision. These results strongly suggest that virulence of E. rhusiopathiae is associated, at least in part, with resistance to phagocytosis by polymorphonuclear leukocytes and that this antiphagocytic ability of the bacterium results from its possession of a capsule.

Animals↗

PubMed1998

Construction and vaccine potential of acapsular mutants of Erysipelothrix rhusiopathiae: use of excision of Tn916 to inactivate a target gene.

We previously showed that acapsular transposon Tn916 mutants of Erysipelothrix rhusiopathiae are avirulent for mice. In this study, we constructed nonreverting acapsular mutants and examined the vaccine potential of the mutants in mice. A representative acapsular transposon mutant, 33H6, was plated on selective agar containing autoclaved chlortetracycline and quinaldic acid, and two tetracycline-sensitive mutants were obtained. Sequence analysis of chromosomal regions of the mutants in which Tn916 had flanked revealed that Tn916 had spontaneously excised from the region and that the six new nucleotides, which were presumably inserted with Tn916 into 33H6 chromosome, substituted for those present at the insertion site. The mutants were confirmed to be devoid of capsular antigen by Western immunoblotting and were nonvirulent for mice (subcutaneous 50% lethal dose [LD50], >10(9) CFU). The safety and efficacy of acapsular mutants for live vaccines was further studied by using one mutant strain, named YS-1. The YS-1 bacteria were cleared from the skin sites of inoculation, livers, and spleens of the inoculated mice by 7 days after subcutaneous (s.c.) inoculation. Mice immunized s.c. with doses ranging from 2 x 10(4) to 2 x 10(8) CFU of strain YS-1 were completely protected against challenge with 100 LD50 of the homologous, highly virulent strain Fujisawa-SmR 21 days postimmunization, and protective immunity conferred by immunization with 2 x 10(8) CFU of the strain lasted for as long as the 3 months of the observation period. In passive immunization experiments, sera collected from mice immunized with strain YS-1 at days 14 and 21 postimmunization provided protection against challenge with Fujisawa-SmR, whereas sera collected at days 4 and 7 did not. Furthermore, specific spleen cell responses to E. rhusiopathiae antigens were observed in mice immunized with strain YS-1, and cross-protection against the antigenically heterologous bacterium Listeria monocytogenes was observed at 7 days after immunization in the mice, suggesting that cell-mediated immunity had been induced. These results suggest that E. rhusiopathiae YS-1 may be a suitable choice for further studies of vaccine efficacy in swine.

Animals↗

PubMed1999

Truncated surface protective antigen (SpaA) of Erysipelothrix rhusiopathiae serotype 1a elicits protection against challenge with serotypes 1a and 2b in pigs.

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.

Amino Acid Sequence↗

PubMed2002

Erysipelothrix rhusiopathiae YS-1 as a live vaccine vehicle for heterologous protein expression and intranasal immunization of pigs.

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.

Adhesins, Bacterial↗

PubMed2003

Adhesive surface proteins of Erysipelothrix rhusiopathiae bind to polystyrene, fibronectin, and type I and IV collagens.

Erysipelothrix rhusiopathiae is a gram-positive bacterium that causes erysipelas in animals and erysipeloid in humans. We found two adhesive surface proteins of E. rhusiopathiae and determined the nucleotide sequences of the genes, which were colocalized and designated rspA and rspB. The two genes were present in all of the serovars of E. rhusiopathiae strains examined. The deduced RspA and RspB proteins contain the C-terminal anchoring motif, LPXTG, which is preceded by repeats of consensus amino acid sequences. The consensus sequences are composed of 78 to 92 amino acids and repeat 16 and 3 times in RspA and RspB, respectively. Adhesive surface proteins of other gram-positive bacteria, including Listeria monocytogenes adhesin-like protein, Streptococcus pyogenes protein F2 and F2-like protein, Streptococcus dysgalactiae FnBB, and Staphylococcus aureus Cna, share the same consensus repeats. Furthermore, the N-terminal regions of RspA and RspB showed characteristics of the collagen-binding domain that was described for Cna. RspA and RspB were expressed in Escherichia coli as histidine-tagged fusion proteins and purified. The recombinant proteins showed a high degree of capacity to bind to polystyrene and inhibited the binding of E. rhusiopathiae onto the abiotic surface in a dose dependent manner. In a solid-phase binding assay, both of the recombinant proteins bound to fibronectin, type I and IV collagens, indicating broad spectrum of their binding ability. It was suggested that both RspA and RspB were exposed on the cell surface of E. rhusiopathiae, as were the bacterial cells agglutinated by the anti-RspA immunoglobulin G (IgG) and anti-RspB IgG. RspA and RspB were present both in surface-antigen extracts and the culture supernatants of E. rhusiopathiae Fujisawa-SmR (serovar 1a) and SE-9 (serovar 2). The recombinant RspA, but not RspB, elicited protection in mice against experimental challenge. These results suggest that RspA and RspB participate in initiation of biofilm formation through their binding abilities to abiotic and biotic surfaces.

Amino Acid Sequence↗

PubMed1969

Induction of experimental chronic arthritis in rabbits by cell-free fragments of Erysipelothrix.

A cell-free crude extract of Erysipelothrix rhusiopathiae injected by high pressure jet into the knee-joint of rabbits stimulated an acute, mild inflammatory reaction. Additional injections at 3-day intervals induced a chronic condition characterized by hyperplasia of the synovial cells and hypertrophy of the villi, due to infiltration by lymphocytes and plasma cells which formed aggregates resembling Allison-Ghormley bodies. There was also extensive proliferation of stroma vasculature and fibrous tissue. A similar jet injection of the diluent produced an early, transient, acute, and mild inflammation. A mechanism is postulated for fixation of one or more of the chemically characterized antigens in or near the synovium as a means of inducing the localized inflammatory response that predisposes the joint to infection.

Animals↗

PubMed1990

Modified Feist broth as a serum-free alternative for enhanced production of protective antigen of Erysipelothrix rhusiopathiae.

The production of protective antigen in modified serum-free nutrient broth (H. Feist, K.-D. Flossmann, and W. Erler, Arch. Exp. Veterinaermed. 30:49-57, 1976) and in brain heart infusion broth supplemented with 10% horse serum (BHIS) was evaluated for six strains of Erysipelothrix rhusiopathiae serotypes 1a, 2, 2b, 4, and N. All six strains grew to higher cell densities in modified Feist medium than in BHIS and produced larger amounts of 64,000- to 66,000- and 39,000- to 40,000-molecular-weight antigens involved in immunity to erysipelas. A vaccine produced in Feist medium from E. rhusiopathiae SE-9 (serotype 2) was highly effective in a mouse protection test. We therefore suggest that modified Feist medium is an excellent, if not superior, alternative to BHIS for production of erysipelas vaccine.

Animals↗

PubMed2000

Potential errors in recognition of Erysipelothrix rhusiopathiae.

Here we describe four isolations of Erysipelothrix rhusiopathiae associated with polyarthralgia and renal failure, septic arthritis, classic erysipeloid, and peritonitis. Although the biochemical identification was straightforward in each case, recognition presented a challenge to the clinical microbiologist, since in three cases E. rhusiopathiae was not initially considered due to unusual clinical presentations, in two cases the significance might not have been appreciated because growth was in broth only, and in one case the infection was thought to be polymicrobic. Because the Gram stain can be confusing, abbreviated identification schemes that do not include testing for H(2)S production could allow E. rhusiopathiae isolates to be misidentified as Lactobacillus spp. or Enterococcus spp. in atypical infections.

Aged↗

PubMed2026

Prevalence of Erysipelothrix rhusiopathiae in tonsils of domestic pigs and wild boars in Sweden.

Erysipelothrix rhusiopathiae (ER) causes erysipelas in multiple animal species and may persist in the environment or be carried asymptomatically. It is estimated that 30-50% of apparently healthy or convalescent pigs harbour ER in their tonsils and other lymphoid tissues. This study aimed to determine the prevalence of ER in the tonsils of healthy Swedish fattening pigs and wild boars. Tonsils were collected from 200 fattening pigs at slaughter from ten abattoirs across Sweden in 2017, with one pig per herd sampled. Wild boars (n = 180) were sampled during hunting, primarily in Östergötland County, in 2018. Cultures were performed using selective media and isolates were confirmed as ER by MALDI-TOF MS. ER was recovered from 6/200 pig tonsils (3.0%), all originating from three abattoirs in southern Sweden. ER was isolated from 76/167 (45.5%) of wild boar tonsils. Whole-genome sequencing revealed a high genetic diversity among the isolates with no dominant clones. Overall, these results indicate that Swedish pig husbandry, characterized by indoor rearing of fattening pigs, age-segregated rearing, sow vaccination, enhanced biosecurity, and restricted straw access largely prevents tonsillar colonization by ER aligning with the low occurrence of clinically diagnosed erysipelas in such herds. For wild boars, the high isolation rate suggests that wild boar could act as a reservoir and potential source of infection for domestic pigs. The potential zoonotic risk should also be considered.

Animals↗

PubMed1993

Detection of plasmid DNA in Erysipelothrix rhusiopathiae isolated from pigs with chronic swine erysipelas.

Forty-three strains of Erysipelothrix rhusiopathiae, isolated from pigs with chronic swine erysipelas, were examined for the presence of plasmid DNA by agarose gel electrophoresis and electron microscopy. Seven of these strains were found to contain plasmids of which number were varied from 1 to 6. The plasmids ranged from 1.4 to 86 kb in size. This is the first reported evidence for plasmid DNA in E. rhusiopathiae. The functions of the plasmids are unknown at present.

Animals↗

PubMed1993

Comparison of etiological and immunological characteristics of two attenuated Erysipelothrix rhusiopathiae strains of serotypes 1a and 2.

Two acriflavine-fast attenuated Erysipelothrix rhusiopathiae strains Koganei 65-0.15 of serotype 1a (strain Kg-1a) and 2 (strain Kg-2) were comparatively characterized. Biochemical characterization showed the similar reactions with slight variation between the strains. Strain Kg-2 was more resistant to acriflavine dye than strain Kg-1a. Pathogenicity of strain Kg-2 was higher than strain Kg-1a in mice of strains ddY. C3H/He and A/J. Significant differences of clinical signs between strains Kg-1a and Kg-2 were observed in occurrence of arthritis (P < 0.05) and systemic signs (P < 0.01) of only ddY mice. C3H/He mice was more resistant than ddY and A/J mice to the infection of strains Kg-1a and Kg-2. Three culture fractions, whole culture: WC, culture filtrate: CF and killed cells: KC, of strain Kg-2 were more protective than those of strain Kg-1a in ddY mice. CF of strain Kg-2 was most protective in all fractions. Heating at 56 degrees C and 100 degrees C or treatment with trypsin completely reduced the protective activity of WC of the two strains, indicating that major protective antigens of WC were protein. The present results demonstrated that immunogenicity and pathogenicity for mice were different between the two attenuated strains.

Acriflavine↗

PubMed1996

Growth ability and immunological properties of Erysipelothrix rhusiopathiae serotype 2.

Five field strains of Erysipelothrix rhusiopathiae belonging to serotype 2 were compared for their growth ability, immunogenicity in mice, SDS-PAGE profile of cell surface proteins and their immunoblotting patterns. Strain Tama-96 showed the most stable growth in Feist medium and tryptose phosphate broth with Tween 80 (TPB), and its immunogenicity was highest in a mouse protection test using the inactivated vaccines prepared from 20-h TPB culture. The 50% mouse protective dose of the vaccine was only 12 microliter. SDS-PAGE and immunoblotting patterns of the proteins were similar among the strains in general and indicated that 66 to 64 kDa protein antigens were dominant.

Animals↗

PubMed1997

Effect of attenuated Erysipelothrix rhusiopathiae vaccine in pigs infected with porcine reproductive respiratory syndrome virus.

Twenty 2nd specific pathogen-free pigs were divided into 4 groups: Group A were infected with porcine reproductive and respiratory syndrome (PRRS) virus at 6 weeks of age and treated with available swine erysipelas and swine fever combined vaccine (vaccinated) at 7 weeks of age; Group B were vaccinated at 7 weeks of age and infected with PRRS virus at 8 weeks of age; Group C were vaccinated at 7 weeks of age: Group D were neither vaccinated nor infected with PRRS virus. All pigs were challenged to Erysipelothrix rhusiopathiae C42 strain at 10 weeks of age. No clinical signs appeared after vaccination of group A and B pigs, thus confirming that the safety of the vaccine was not influenced by infection with PRRS virus. None of the pigs in Groups A and C developed erysipelas after challenge exposure to E. rhusiopathiae. In contrast, fever and/or urticaria appeared transiently in all pigs of Group B after challenge exposure. At the time of challenge exposure to E. rhusiopathiae, the PRRS virus titer was high in sera of Group B, but was low in those from Group A. However, vaccination of pigs with attenuated E. rhusiopathiae was effective in dual infection with PRRS virus and E. rhusiopathiae, because the clinical signs were milder and the E. rhusiopathiae strain was less recovered from these pigs compared to pigs of group D.

Animals↗

PubMed1998

Isolation of acriflavine resistant Erysipelothrix rhusiopathiae from slaughter pigs in Japan.

Erysipelothrix rhusiopathiae is the causative agent of swine erysipelas. Although an attenuated vaccine is used in Japan, recent increases in disease occurrence have cast doubts on its efficacy. We investigated the similarity between the vaccine strain and E. rhusiopathiae field isolates by the analysis of acriflavine resistance (the vaccine strain marker), serotype, DNA fingerprinting and pathogenicity to mice. Although 7 acriflavine resistant E. rhusiopathiae isolates were separated from arthritic lesions of slaughter pigs, we were unable to prove that they were identical to the vaccine strain.

Abattoirs↗

PubMed1998

Protective effect of NaOH-extracted Erysipelothrix rhusiopathiae vaccine in pigs.

A vaccine was prepared from a NaOH-extracted antigen of the Kyoto strain (serovar 2) of Erysipelothrix rhusiopathiae (E. rhusiopathiae) with an oil adjuvant, and was injected twice at 3-week intervals into SPF pigs and conventional pigs with maternal antibodies. After the second vaccination, IgG-GA titers of immunized SPF pigs were more than 256-fold at 3 weeks, and immunized pigs with maternal antibodies were 64-fold at 7 weeks. The pig with maternal antibodies vaccinated once with live vaccine had less than 4-fold titers. The ELISA antibody titers which were measured by using the NaOH-extracted antigen showed similar transition to the IgG-GA antibody titers. All immunized pigs and nonvaccinated control pigs were challenged with the strains Fujisawa (serovar 1a) or Saitama-1 (serovar 2). After challenge exposure, all pigs immunized with the NaOH-extracted vaccine showed no clinical signs and survived, and the pig immunized with the live vaccine had a local rhomboidal lesion at the site of the injection. Nonvaccinated pigs developed typical symptoms of E. rhusiopathiae infection and one of them died. After the autopsy, the challenge strains were not recovered from the main organs except tonsils of the pigs immunized with the NaOH-extracted vaccine. These results indicated that the NaOH-extracted vaccine induces a protective effect in pigs with maternal antibodies as well as in SPF pigs negative for such antibodies, and that 67-64, 62-60 kDa proteins in the NaOH-extracted antigen play an important role in protecting against E. rhusiopathiae infection.

Animals↗

PubMed2000

Quantitative diversity of 67 kda protective antigen among serovar 2 strains of Erysipelothrix rhusiopathiae and its implication in protective immune response.

Mouse monoclonal antibodies (MAbs), raised against the NaOH-extracted antigen of Erysipelothrix rhusiopathiae strain Kyoto (serovar 2), recognized two different epitopes on a single protein of molecular weight 67 kDa. The MAbs were classified as protective or non-protective against strain Fujisawa (serovar 1). In immunoblotting analysis using the MAbs, fifteen wild strains were shown to contain different amounts of 67 kDa protective antigen. Each formalin-killed whole cell vaccine (bacterin) prepared from the fifteen wild strains conferred different levels of protection against strain Fujisawa in mice. Bacterins prepared from wild strains with larger amounts of 67 kDa protective antigen tended to give high levels of antigen-specific antibody and better protection to mice. These results indicate that the amount of 67 kDa protective antigen which influences the induction of protective immune responses may vary substantially among the strains of E. rhusiopathiae (serovar 2).

Animals↗

PubMed2002

Hyaluronidase is not essential for the lethality of Erysipelothrix rhusiopathiae infection in mice.

To investigate the role of hyaluronidase in the pathogenicity of Erysipelothrix rhusiopathiae, transposon Tn916 was transferred from Enterococcus faecalis CG110 to a virulent strain of E. rhusiopathiae, and hyaluronidase-deficient mutants were isolated. A virulence assay in the mice showed that of the seven hyaluronidase-deficient mutants tested, six mutants were avirulent, but that one mutant, designated AST121, was as virulent as its parental strain. Western immunoblotting with a monoclonal antibody specific to the capsule, a major virulence factor of the organism, revealed that all of the avirulent mutants had lost the capsular antigen, whereas the mutant AST121 did not. These results suggest that the lack of virulence of the six hyaluronidase-negative mutants could be due to a loss of the capsule and that hyaluronidase does not contribute to the lethality of E. rhusiopathiae infection in mice.

Animals↗

PubMedDate not supplied

Erysipelothrix rhusiopathiae neuraminidase and its role in pathogenicity.

The role of the enzyme neuraminidase in pathogenicity of the bacillus Erysipelothrix rhusiopathiae was studied. Different substances with low and high molecular weight were tested as inducers of E. rhusiopathiae neuraminidase biosynthesis. It was found that macromolecular complexes induce the secretion of the enzyme. K(M) values for different substrates showed that the affinity of the E. rhusiopathiae neuraminidase increases in parallel with the enlargement of the molecular weight of glycoproteins. Results from the rabbits skin test confirmed the role of E. rhusiopathiae neuraminidase as a factor of pathogenicity with spreading functions.

Enzyme Induction↗