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The protective M proteins of the equine group C streptococci

J F Timoney1, M M Mukhtar

  • 1Gluck Equine Research Center, University of Kentucky, Lexington.

Veterinary Microbiology
|November 1, 1993
PubMed

Insights

Group C streptococci cause horse diseases, with M protein being a key virulence factor. Current vaccines offer limited protection, highlighting the need for better understanding of protective antibodies against Streptococcus equi and Streptococcus zooepidemicus.

Area of Science:

  • Veterinary Microbiology
  • Equine Infectious Diseases
  • Bacterial Pathogenesis

Background:

  • Group C streptococci, specifically Streptococcus equi and Streptococcus zooepidemicus, are primary causes of disease in horses.
  • Key virulence factors include the hyaluronic acid capsule and the antiphagocytic M protein, crucial for bacterial survival and host interaction.

Purpose of the Study:

  • To investigate the role of M protein in Streptococcus equi and Streptococcus zooepidemicus infections in horses.
  • To evaluate the efficacy of current vaccines and identify challenges in achieving protective immunity against these pathogens.

Main Methods:

  • Analysis of bacterial virulence factors, including hyaluronic acid capsule and M protein.
  • Assessment of immune responses, including B and T cell activation and antibody production (IgG, IgA).
  • Evaluation of protective immunity using bactericidal tests with equine neutrophils and a mouse-challenge model.

Main Results:

  • Hyaluronic acid capsule is non-antigenic and not involved in protective immunity.
  • M protein elicits strong immune responses, potentially leading to protective immunity via opsonic antibodies.
  • Vaccines based on extracted M protein provide insufficient protection against field exposure.

Conclusions:

  • M protein is a critical target for protective immunity against group C streptococci in horses.
  • Current vaccine strategies are limited in conferring adequate protection.
  • Further research is needed to differentiate protective antibodies from non-protective ones against M protein epitopes.

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