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Analysis of cellular receptors for human coronavirus OC43

C Krempl1, B Schultze, G Herrler

  • 1Institut für Virologie, Philipps-Universität Marburg, Germany.

Insights

Three related coronaviruses, including human coronavirus OC43 (HCV-OC43), bind to N-acetyl-9-O-acetylneuraminic acid (Neu5,9Ac2) on red blood cells. This specific sialic acid is crucial for viral attachment and infection.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Bovine coronavirus (BCV), human coronavirus OC43 (HCV-OC43), and hemagglutinating encephalomyelitis virus (HEV) are serologically related and exhibit hemagglutinating activity.
  • N-acetyl-9-O-acetylneuraminic acid (Neu5,9Ac2) is identified as the receptor determinant for viral attachment to erythrocytes.

Purpose of the Study:

  • To compare the binding specificities of BCV, HCV-OC43, and HEV to 9-O-acetylated sialic acids.
  • To investigate the role of Neu5,9Ac2 as a receptor determinant for HCV-OC43 in erythrocyte agglutination and cell infection.

Main Methods:

  • Comparative analysis of coronavirus binding to sialic acid derivatives.
  • Erythrocyte agglutination assays.
  • Cell culture experiments using MDCK I cells to assess viral attachment and infection.

Main Results:

  • All three coronaviruses bind to Neu5,9Ac2 linked to galactose via either α2,3 or α2,6 linkages.
  • Differences were observed in the minimal sialic acid concentration required for viral agglutination.
  • HCV-OC43 utilizes Neu5,9Ac2 for both erythrocyte agglutination and infection of MDCK I cells.

Conclusions:

  • The studied coronaviruses share a common receptor determinant, Neu5,9Ac2, for attachment.
  • HCV-OC43 employs Neu5,9Ac2 as a critical receptor for both hemagglutination and cellular infection, highlighting its importance in viral pathogenesis.

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