期刊
VIROLOGY
卷 353, 期 2, 页码 294-306出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2006.05.028
关键词
E protein; coronavirus; ion channel; mouse hepatitis virus (MHV); human coronavirus 229E (HCoV-229E); infectious bronchitis virus (IBV); amiloride; hexamethylene amiloride (HMA); antiviral compound
类别
All coronaviruses encode a small hydrophobic envelope (E) protein, which mediates viral assembly and morphogenesis by an unknown mechanism. We have previously shown that the E protein from Severe Acute Respiratory Syndrome coronavirus (SARS-CoV) forms cation-selective ion channels in planar lipid bilayers (Wilson, L., McKinlay, C., Gage, P., Ewart, G., 2004. SARS coronavirus E protein forms cation-selective ion channels. Virology 330(1), 322-331). We now report that three other E proteins also form cation-selective ion channels. These E proteins were from coronaviruses representative of taxonomic groups 1-3: human coronavirus 229E (HCoV-229E), mouse hepatitis virus (MHV), and infectious bronchitis virus (IBV), respectively. It appears, therefore, that coronavirus E proteins in general, belong to the virus ion channels family. Hexamethylene amiloride (HMA) - an inhibitor of the HIV-1 Vpu virus ion channel - inhibited the HCoV-229E and MHV E protein ion channel conductance in bilayers and also inhibited replication of the parent coronaviruses in cultured cells, as determined by plaque assay. Conversely, HMA had no antiviral effect on a recombinant MHV with the entire coding region of E protein deleted (MHV Delta E). Taken together, the data provide evidence of a link between inhibition of E protein ion channel activity and the antiviral activity of HMA. (c) 2006 Elsevier Inc. All rights reserved.
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