Early events of rotavirus infection: the search for the receptor(s)

C F Arias1, C A Guerrero, E Méndez

  • 1Departamento de Genética y Fisiología Molecular, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca, Morelos 62250, Mexico.

Novartis Foundation Symposium
|July 11, 2001
PubMed

Insights

Rotaviruses enter epithelial cells through multiple interactions. Integrin alpha 2 beta 1 serves as a primary attachment site for some strains, while integrin alpha V beta 3 acts as a co-receptor for all strains studied.

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Interactions

Background:

  • Rotavirus entry into epithelial cells is a complex, multistep process.
  • Glycolipids and glycoproteins are implicated as initial rotavirus attachment receptors.
  • Sialic acid presence influences rotavirus infectivity, but a neuraminidase-resistant receptor is also involved.

Purpose of the Study:

  • To comparatively characterize the cell attachment mechanisms of rotavirus strains RRV, nar3, and Wa.
  • To identify specific cell surface molecules involved in rotavirus entry.
  • To elucidate the role of integrins in rotavirus-cell interactions.

Main Methods:

  • Infection competition experiments were utilized.
  • Comparative characterization of rotavirus strains (RRV, nar3, Wa) was performed.
  • Analysis of cell surface molecule interactions during viral entry.

Main Results:

  • Integrin alpha 2 beta 1 is the primary attachment site for the neuraminidase-resistant variant nar3 and a secondary interaction site for RRV.
  • Integrin alpha V beta 3 functions as a co-receptor for all three rotavirus strains (RRV, nar3, Wa) after initial attachment.
  • Rotavirus infectivity involves a complex of cell molecules, likely within glycosphingolipid-enriched membrane microdomains.

Conclusions:

  • Rotavirus cell entry involves sequential interactions with multiple cell surface molecules.
  • Integrins play crucial roles as both primary attachment sites and co-receptors in rotavirus infection.
  • The functional rotavirus receptor is likely a complex molecular assembly within specific membrane domains.

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