Studies from T. Betakova et al add new findings in the area of influenza
2007 NOV 20 -- According to recent research published in the Journal of General Virology, "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," wrote T. Betakova and colleagues. The researchers concluded: "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." Betakova and colleagues published their study in the Journal of General Virology (Evidence that the CM2 protein of influenza C virus can modify the pH of the exocytic pathway of transfected cells. Journal of General Virology, 2007;88(Part 8):2291-2296). For additional information, contact T. Betakova, Slovaks Academy Science, Institute Virology, Dubravska Cesta 9, Bratislava 84505, Slovakia. The publisher's contact information for the Journal of General Virology is: Society General Microbiology, Marlborough House, Basingstoke Rd., Spencers Woods, Reading RG7 1AG, Berks, England. Keywords: Slovakia, Bratislava, Flu, Influenza. This article was prepared by Virus Weekly editors from staff and other reports. Copyright 2007, Virus Weekly via NewsRx.com.
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