RT Journal Article SR Electronic(1) A1 Betakova, Tatiana A1 Hay, Alan J.YR 2007 T1 Evidence that the CM2 protein of influenza C virus can modify the pH of the exocytic pathway of transfected cells JF Journal of General Virology, VO 88 IS 8 SP 2291 OP 2296 DO https://doi.org/10.1099/vir.0.82785-0 PB Microbiology Society, SN 1465-2099, AB 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., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.82785-0