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Clinical and vaccine immunology : CVI2013; 20(8); 1181-1188; doi: 10.1128/CVI.00069-13

Characterization and protective immunogenicity of the SzM protein of Streptococcus zooepidemicus NC78 from a clonal outbreak of equine respiratory disease.

Abstract: Streptococcus zooepidemicus of Lancefield group C is a highly variable tonsillar and mucosal commensal that usually is associated with opportunistic infections of the respiratory tract of vertebrate hosts. More-virulent clones have caused epizootics of severe respiratory disease in dogs and horses. The virulence factors of these strains are poorly understood. The antiphagocytic protein SeM is a major virulence factor and protective antigen of Streptococcus equi, a clonal biovar of an ancestral S. zooepidemicus strain. Although the genome of S. zooepidemicus strain H70, an equine isolate, contains a partial homolog (szm) of sem, expression of the gene has not been documented. We have identified and characterized SzM from an encapsulated S. zooepidemicus strain from an epizootic of equine respiratory disease in New Caledonia. The SzM protein of strain NC78 (SzM(NC78)) has a predicted predominantly alpha-helical fibrillar structure with an LPSTG cell surface anchor motif and resistance to hot acid. A putative binding site for plasminogen is present in the B repeat region, the sequence of which shares homology with repeats of the plasminogen binding proteins of human group C and G streptococci. Equine plasminogen is activated in a dose-dependent manner by recombinant SzM(NC78). Only 23.20 and 25.46% DNA homology is shared with SeM proteins of S. equi strains CF32 and 4047, respectively, and homology ranges from 19.60 to 54.70% for SzM proteins of other S. zooepidemicus strains. As expected, SzM(NC78) reacted with convalescent-phase sera from horses with respiratory disease associated with strains of S. zooepidemicus. SzM(NC78) resembles SeM in binding equine fibrinogen and eliciting strong protective antibody responses in mice. Sera of vaccinated mice opsonized S. zooepidemicus strains NC78 and W60, the SzM protein of which shared partial amino acid homology with SzM(NC78). We conclude that SzM is a protective antigen of NC78; it was strongly reactive with serum antibodies from horses during recovery from S. zooepidemicus-associated respiratory disease.
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Publication Date: 2013-06-05 PubMed ID: 23740925PubMed Central: PMC3754524DOI: 10.1128/CVI.00069-13Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research investigates the characteristics and immunogenic properties of a protein identified in a strain of Streptococcus zooepidemicus (S. zooepidemicus) found in equines suffering from respiratory diseases. The primary finding is that the protein, named SzM, shows protective capabilities against the strain, suggesting its potential use for disease prevention.

Investigation of SzM Protein

The researchers examined SzM, a protein found in S. zooepidemicus, a bacterium typically associated with respiratory tract infections in vertebrates. The strain studied was isolated from an outbreak of a respiratory disease in horses in New Caledonia. The structure of the protein was found to be predominantly alpha-helical and possesses various features, including a cell surface anchor motif and resistance to high temperatures and acidic conditions.

  • The SzM protein also exhibits a potential binding site for plasminogen, a vital enzyme involved in the breakdown of blood clots. The sequence of this region shows similarities with the plasminogen-binding proteins of certain human streptococcal bacteria.
  • The researchers further found that equine plasminogen activation is influenced by the presence of the SzM protein – an activity that increases with the raised amount of the protein.

Comparative Analysis and Reactivity

A comparative study was undertaken to ascertain the relationship between the SzM protein of S. zooepidemicus NC78 strain and the proteins of other associated strains. The results show that the level of shared DNA with other SeM proteins of the S. equi strains was relatively low, ranging around 23.20% and 25.46% for strains CF32 and 4047, respectively. There was an even wider range of homology amongst SzM proteins of other S. zooepidemicus strains – from 19.60% to 54.70%.

  • The SzM protein proved reactive with antibodies in the sera of horses recovering from a respiratory disease associated with S. zooepidemicus.

Vaccination Research Results

The protein’s protective capabilities were tested by exposing mice to it. The SzM protein was successful in eliciting a strong protective antibody response in the mice, similar to the SeM protein’s reaction with equine fibrinogen. These antibodies in the vaccinated mice’s sera were then found to opsonize, or mark for destruction, two strains of S. zooepidemicus, including the NC78 strain where the SzM protein was first identified. This was especially significant in cases where the enzyme exhibited partial amino acid homology with the SzM protein in the NC78 strain.

The results point toward the protein being a protective antigen for the NC78 strain, given its strong reactivity with the serum antibodies of horses during recovery from the associated respiratory disease. This suggests the potential use of SzM as a vaccine, which could enhance a horse’s immune system response to S. zooepidemicus infection, providing a promising avenue for future research.

Cite This Article

APA
Velineni S, Timoney JF. (2013). Characterization and protective immunogenicity of the SzM protein of Streptococcus zooepidemicus NC78 from a clonal outbreak of equine respiratory disease. Clin Vaccine Immunol, 20(8), 1181-1188. https://doi.org/10.1128/CVI.00069-13

Publication

Clinical and vaccine immunology : CVI
ISSN: 1556-679X
NlmUniqueID: 101252125
Country: United States
Language: English
Volume: 20
Issue: 8
Pages: 1181-1188

Researcher Affiliations

Velineni, Sridhar
  • Gluck Equine Research Center, University of Kentucky, Lexington, KY, USA.
Timoney, John F

    MeSH Terms

    • Animals
    • Antibodies, Bacterial / blood
    • Antigens, Bacterial / genetics
    • Antigens, Bacterial / immunology
    • Antigens, Bacterial / isolation & purification
    • Bacterial Proteins / genetics
    • Bacterial Proteins / immunology
    • Bacterial Proteins / isolation & purification
    • Disease Outbreaks
    • Female
    • Horse Diseases / epidemiology
    • Horse Diseases / microbiology
    • Horse Diseases / prevention & control
    • Horses
    • Male
    • Mice
    • New Caledonia
    • Opsonin Proteins / blood
    • Respiratory Tract Infections / epidemiology
    • Respiratory Tract Infections / immunology
    • Respiratory Tract Infections / microbiology
    • Respiratory Tract Infections / veterinary
    • Streptococcal Infections / epidemiology
    • Streptococcal Infections / immunology
    • Streptococcal Infections / microbiology
    • Streptococcal Infections / veterinary
    • Streptococcal Vaccines / administration & dosage
    • Streptococcal Vaccines / genetics
    • Streptococcal Vaccines / immunology
    • Streptococcus equi / genetics
    • Streptococcus equi / immunology
    • Streptococcus equi / isolation & purification

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    Citations

    This article has been cited 8 times.
    1. Bergmann R, Schroedl W, Müller U, Baums CG. A distinct variant of the SzM protein of Streptococcus equi subsp. zooepidemicus recruits C1q independent of IgG binding and inhibits activation of the classical complement pathway. Virulence 2023 Dec;14(1):2235461.
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