Evidence that the CM2 protein of influenza C virus can modify the pH of the exocytic pathway of transfected cells
Betakova, Tatiana and Hay, Alan J.,, 88, 2291-2296 (2007),
doi = https://doi.org/10.1099/vir.0.82785-0,
publicationName = Microbiology Society,
issn = 0022-1317,
abstract= 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.,
language=,
type=