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Updated: Jul 18, 2026

Affinity Purification of Influenza Virus Ribonucleoprotein Complexes from the Chromatin of Infected Cells
Published on: June 3, 2012
pH modulating activity of ion channels of influenza A, B, and C viruses
1Institute of Virology, Slovak Academy of Sciences, Dúbravská cesta 9, 845 05 Bratislava, Slovak Republic. virubeta@savba.sk
Abstract:
The BM2 and NB proteins of Influenza B virus (the B virus) and the CM2 protein of Influenza C virus (the C virus) are structural homologs of the M2 protein of Influenza A virus (the A virus). It was shown recently that CM2 in vitro forms a voltage-activated ion channel permeable to chloride ion (Hongo et al., Arch. Virol. 149, 35-50, 2004). To demonstrate a possible pH modulating activity of BM2, NB and CM2, the latters were co-expressed with a pH-sensitive hemagglutinin (HA) of the A virus. BM2 was able to replace functionally M2 and prevented the A virus HA from adopting its low-pH conformation during transport to the cell surface. In contrast, NB had a negative effect on the quality of the co-expressed HA and was unable to modulate the pH in the trans-Golgi network (TGN) and to protect HA. A pH modulating activity was also demonstrated for CM2, but it was much lower than that of M2.
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