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Evidence that the CM2 protein of influenza C virus can modify the pH of the exocytic pathway of transfected cells

¹ Institute of Virology – Slovaks Academy of Sciences, Dubravska cesta 9, 845 05 Bratislava, Slovak Republic
² National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK

Correspondence
Tatiana Betakova
virubeta{at}savba.sk

The 115 residue CM2 protein of influenza C virus is a structural homologue of the M2 protein of influenza A virus. Expression of the CM2 protein in Xenopus oocytes showed that it can form a voltage-activated ion channel permeable to Cl^–. To investigate whether the CM2 protein has pH modulating activity comparable to that of the M2 protein, CM2 was co-expressed with a pH-sensitive haemagglutinin (HA) from influenza A virus. The results indicate that, like the M2 protein, the CM2 protein has a capacity to reduce the acidity of the exocytic pathway and reduce conversion of the pH-sensitive HA to its low pH conformation during transport to the cell surface. By contrast, the NB protein of influenza B virus has no detectable activity. Although, the pH modulating activity of the CM2 protein was substantially less than that of the M2 protein, these observations provide support for a role in virus uncoating analogous to that of M2.