Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1926356 | Archives of Biochemistry and Biophysics | 2009 | 5 Pages |
Abstract
The cytoplasmic domain of influenza M2 protein (M2c) consists of 54 amino acid (aa) residues from aa44 to aa97. In this paper, M2c and its deletion mutant M2cÎ47-55 were expressed using prokaryotic expression system. First, glutaraldehyde crosslinking assay showed that M2c had multimerization potential mediated by aa47-55. Then, M2c, instead of M2cÎ47-55, directed eGFP from the whole cell localization to a predominately perinuclear region in CHO cells, which indicated that aa47-55 of M2c mediated the localization. Moreover, M2c colocalized with caveolin-1 (Cav) when CHO cells were cotransfected with Cav. A caveolin-1 binding motif ΦxxxxΦxxΦ (Φ represents aromatic amino acid residues) in aa47-55 of M2c was found by sequence alignment and analysis. Further overlay ELISA result showed that M2c, but not M2cÎ47-55, bound to prokaryotically expressed cholesterol-free Cav2-101, which illustrated the interaction could be cholesterol-independent. That was the first report of cellular protein bound to M2c.
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Authors
Peng Zou, Fan Wu, Lu Lu, Jing-He Huang, Ying-Hua Chen,