Stability and function of the influenza A virus M2 ion channel protein is determined by both extracellular and cytoplasmic domains

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...

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Bibliographic Details
Published in:Archives of virology 2009, Vol.154 (1), p.147-151
Main Authors: Betakova, Tatiana, Hay, Alan J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Biological and medical sciences
Biomedical and Life Sciences
Biomedicine
Brief Report
Cell Line
Channel gating
Chimeras
Cytoplasm - metabolism
Extracellular Space - metabolism
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation, Viral
Gene Order
Infectious Diseases
Influenza A
Influenza A virus
Influenza A virus - genetics
Influenza A virus - metabolism
Medical Microbiology
Microbiology
Miscellaneous
Plasmids
Protein Stability
Protein Structure, Tertiary - physiology
Proteins
Viral Matrix Proteins - chemistry
Viral Matrix Proteins - genetics
Viral Matrix Proteins - metabolism
Virology
Viruses
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Summary: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.
ISSN:0304-8608
1432-8798
DOI:10.1007/s00705-008-0283-7