共 55 条
SARS coronavirus E protein forms cation-selective ion channels
被引:218
作者:

Wilson, L
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机构: Australian Natl Univ, Biotron Ltd, Canberra, ACT 2601, Australia

Mckinlay, C
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h-index: 0
机构: Australian Natl Univ, Biotron Ltd, Canberra, ACT 2601, Australia

Gage, P
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h-index: 0
机构: Australian Natl Univ, Biotron Ltd, Canberra, ACT 2601, Australia

Ewart, G
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h-index: 0
机构: Australian Natl Univ, Biotron Ltd, Canberra, ACT 2601, Australia
机构:
[1] Australian Natl Univ, Biotron Ltd, Canberra, ACT 2601, Australia
[2] Australian Natl Univ, Sch Med, Canberra, ACT 2601, Australia
[3] Australian Natl Univ, John Curtin Sch Med Res, Canberra, ACT 2601, Australia
来源:
关键词:
Severe Acute Respiratory Syndrome (SARS);
coronavirus;
budding;
E protein;
ion channel;
conductance;
Vpu;
hydrophobic;
monovalent cation;
mouse hepatitis virus (MHV);
D O I:
10.1016/j.virol.2004.09.033
中图分类号:
Q93 [微生物学];
学科分类号:
071005 ;
100705 ;
摘要:
Severe Acute Respiratory Syndrome (SARS) is caused by a novel coronavirus (SARS-CoV). Coronaviruses including SARS-CoV encode an envelope (E) protein, a small, hydrophobic membrane protein. We report that, in planar lipid bilayers, synthetic peptides corresponding to the SARS-CoV E protein forms ion channels that are more permeable to monovalent cations than to monovalent anions. Affinity-purified polyclonal antibodies recognizing the N-terminal 19 residues of SARS-CoV E protein were used to establish the specificity of channel forination by inhibiting the ion currents generated in the presence of the E protein peptides. (C) 2004 Elsevier Inc. All rights reserved.
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页码:322 / 331
页数:10
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