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[摘要]：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 M2c(Delta 47-55) were expressed using prokaryotic expression system. First, glutaraldehyde crosslinking assay showed that M2c had multimerization potential mediated by aa47-55. Then, M2c, instead of M2c(Delta 47-55), 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 Phi xxxx Phi xx Phi (Phi 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 M2c(Delta 47-55), bound to prokaryotically expressed cholesterol-free Cav(2-101), which illustrated the interaction could be cholesterol-independent. That was the first report of cellular protein bound to M2c. (C) 2009 Elsevier Inc. All rights reserved. |
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