Stability and function of the influenza A virus M2 ion channel protein is determined by both extracellular and cytoplasmic domains
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A series of M2/NB chimeras were used to investigate the ion channel activity of the IAV M2 protein. Replacing the M2 cytoplasmic domain with the equivalent NB domain (AAB chimera) did not influence ion channel activity, while replacement of N-terminal domains (BAA and BAB chimeras) resulted in loss of activity. Extension of the M2 protein N-terminal domain resulted in full restoration of ion channel activity in BAA chimeras but only partial restoration in BAB. While not directly involved in ion channel activity, the N- and C-terminals of M2 are important for stabilization of the transmembrane domain structure.
KeywordsInfluenza Cytoplasmic Tail Rimantadine Internal Viral Protein Vaccinia Virus vTF7
trans Golgi network
Influenza A virus
Influenza B virus
We thank Michael S. Bennet and Seti Grambas for excellent assistance. This research was partially supported by the Slovak Research and Development Agency (grant no. APVV-51-004105) and the VEGA-Grant Agency of Science (grant no. 2/6152/06).
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