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Dystrophin disruption in enterovirus-induced myocarditis and dilated cardiomyopathy: from bench to bedside

Cornel Badorff1, Kirk U Knowlton

  • 1Department of Medicine, University of California, San Diego, USA. badorff@em.uni-frankfurt.de

Medical Microbiology and Immunology
|August 16, 2003
PubMed

Insights

Enteroviruses disrupt the dystrophin-glycoprotein complex (DGC) in the heart, causing dilated cardiomyopathy. This study shows coxsackievirus B2 protease cleaves dystrophin in patients, contributing to heart muscle disease.

Area of Science:

  • Cardiology
  • Virology
  • Molecular Biology

Background:

  • Genetic defects in the dystrophin-glycoprotein complex (DGC) are linked to hereditary dilated cardiomyopathy.
  • Enteroviruses are known to cause cardiomyopathy, with a previously identified mechanism involving the viral protease 2A cleaving dystrophin.

Purpose of the Study:

  • To investigate the role of dystrophin cleavage by enteroviruses in human dilated cardiomyopathy.
  • To extend previous findings from mouse models to a clinical case of coxsackievirus B2 myocarditis.

Main Methods:

  • Analysis of endomyocardial biopsy specimens from a patient with coxsackievirus B2 myocarditis.
  • Immunostaining for enteroviral capsid antigen VP1 and DGC components (dystrophin, beta-sarcoglycan).
  • In vitro experiments using coxsackievirus B2 protease 2A and human dystrophin.

Main Results:

  • Patient biopsy showed inflammatory infiltrate, myocytolysis, and virus-infected cardiomyocytes.
  • Loss of sarcolemmal staining for dystrophin and beta-sarcoglycan was observed in infected cardiomyocytes.
  • Coxsackievirus B2 protease 2A was confirmed to cleave human dystrophin in vitro.

Conclusions:

  • Focal disruption of the DGC occurs in human coxsackievirus B myocarditis.
  • Enteroviral protease-mediated dystrophin cleavage may contribute to the pathogenesis of enterovirus-induced dilated cardiomyopathy.

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