1887

Journal of General Virology header logo

Volume 69, Issue 10

Attachment of Influenza C Virus to Human Erythrocytes Free

Abstract

Summary

Binding experiments with radioactively labelled influenza C virions were carried out to investigate the interaction of the virus with human erythrocytes. The erythrocytes from any of 35 different individuals were found to contain influenza C virus-binding sites though their number was variable among the individuals and was much less than that on mouse, rat and chicken erythrocytes. Attachment of influenza C virus to human erythrocytes was inhibited completely by prior treatment of the virus with anti-HE monoclonal antibody having a strong haemagglutination inhibition activity. Pretreatment of erythrocytes with neuraminidase or the neuraminate--acetylesterase of influenza C virus resulted in a marked reduction in the level of virus binding. Thus it appears that human erythrocytes have a low level of -acetylated sialic acid-containing glycoconjugates that can interact specifically with the HE glycoprotein of influenza C virus. Proteolytic digestion of erythrocytes with ficin, bromelain or V-8 protease inhibited virus binding almost completely, suggesting that the erythrocyte receptor for influenza C virus is a glycoprotein. In contrast to these enzymes, trypsin treatment of erythrocytes reduced virus binding by only about 50%, and α-chymotrypsin treatment did not inhibit at all. It was also found that treatment of erythrocytes with monoclonal antibody to the M or N blood group antigen greatly inhibited virus binding to the cells. These results, taken together, suggest that most influenza C virus receptors on human erythrocytes, if not all, reside on glycophorin A which is known to possess the M or N blood group activity.

  • Received:
  • Accepted:
  • Published Online:
Keyword(s): glycophorin , influenza C virus and receptor
© Society for General Microbiology 1988
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1988-10-01
2024-04-26
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Attachment of Influenza C Virus to Human Erythrocytes
J. Gen. Virol. 69, 2545 (1988); https://doi.org/10.1099/0022-1317-69-10-2545
/content/journal/jgv/10.1099/0022-1317-69-10-2545
/content/journal/jgv/10.1099/0022-1317-69-10-2545
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