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A 70 kDa MHC class I associated protein (MAP-70) identified as a receptor molecule for Coxsackievirus A9 cell

M Triantafilou1, K Triantafilou, K M Wilson

  • 1Department of Biological Sciences, University of Essex, Colchester, Essex, United Kingdom. mtrian@essex.ac.uk

Human Immunology
|October 29, 2000
PubMed

Insights

Researchers identified key cell surface molecules involved in Coxsackievirus A9 (CAV-9) infection. Integrin alpha v beta 3 and MHC class I associated protein (MAP-70) were found to be crucial for CAV-9 attachment and entry into host cells.

Area of Science:

  • Virology
  • Cell Biology
  • Immunology

Background:

  • Viruses cause disease and their infection involves complex interactions between viral and host cell surface molecules.
  • Coxsackievirus A9 (CAV-9), a Picornavirus, is a common human pathogen.
  • Understanding virus-host interactions is crucial for developing antiviral strategies.

Purpose of the Study:

  • To identify the specific cell surface molecules utilized by Coxsackievirus A9 (CAV-9) during its infectious process.
  • To elucidate the role of these molecules in viral attachment and cell entry.

Main Methods:

  • GMK cells were surface-labeled and solubilized.
  • Coxsackievirus A9 (CAV-9) virions were used to affinity-purify binding receptors.
  • Virus-receptor complexes were immunoprecipitated using anti-CAV-9 serum and protein-A sepharose.
  • SDS-PAGE, 2D electrophoresis, immunoprecipitation, and Western blotting were employed for analysis.

Main Results:

  • Integrin alpha v beta 3 and a 70 kDa protein were identified as potential CAV-9 receptors.
  • The 70 kDa protein was confirmed to be MHC class I associated protein (MAP-70).
  • Both integrin alpha v beta 3 and MAP-70 were found to be involved in CAV-9 infection.

Conclusions:

  • Integrin alpha v beta 3 and MAP-70 are critical cell surface molecules for Coxsackievirus A9 (CAV-9) entry.
  • This study provides insights into the molecular mechanisms of CAV-9 pathogenesis.
  • Further research into the role of MAP-70 could lead to novel therapeutic targets.

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