Amantadine blocks channel activity of the transmembrane segment of the NB protein from influenza B

被引:16
作者
Fischer, WB
Pitkeathly, M
Sansom, MSP
机构
[1] Univ Oxford, Dept Biochem, Mol Biophys Lab, Oxford OX1 3QU, England
[2] Oxford Ctr Mol Sci, Oxford OX1 3QT, England
来源
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS | 2001年 / 30卷 / 06期
关键词
viral ion channels; NB protein; influenza B; conductance measurements;
D O I
10.1007/s002490100157
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
NB is short auxiliary protein with ca. 100 amino acids, encoded in the viral genome of influenza B. It is believed to be similar to M2 from influenza A and Vpu from HIV-1 in that it demonstrates ion channel activity. Channels formed by the protein can be blocked by amantadine. We have synthesized the putative transmembrane segment of NB (IRG S-20 IIITICVSL I-30 VILIVFGCI A(40) KIFI (NB, Lee)). Reconstituted in a lipid bilayer the peptide shows channel activity. The addition of amantadine leads to dose-dependent loss of channel activity. Channel blocking is reversible. Channel behaviour of the peptide in the presence of amantadine is in accordance with findings, for the intact channel. Thus, the synthetic transmembrane peptide captures the ion channel activity of the intact NB protein.
引用
收藏
页码:416 / 420
页数:5
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