SARS coronavirus E protein forms cation-selective ion channels
| Autor: | Lauren Elizabeth Wilson, Peter W. Gage, Gary Ewart, Carolyn Mckinlay |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Mouse hepatitis virus (MHV)
viruses Lipid Bilayers Molecular Sequence Data Monovalent cation Biology medicine.disease_cause Ion Channels Article Membrane Potentials chemistry.chemical_compound Viral Envelope Proteins Virology Vpu medicine Peptide synthesis Amino Acid Sequence skin and connective tissue diseases Lipid bilayer Peptide sequence Ion channel Coronavirus E protein Membrane potential Budding fungi virus diseases Severe Acute Respiratory Syndrome (SARS) Hydrophobic Peptide Fragments body regions Severe acute respiratory syndrome-related coronavirus Biochemistry Membrane protein chemistry Polyclonal antibodies Conductance biology.protein Biophysics |
| Zdroj: | Virology |
| ISSN: | 0042-6822 |
| DOI: | 10.1016/j.virol.2004.09.033 |
| Popis: | 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 formation by inhibiting the ion currents generated in the presence of the E protein peptides. |
| Databáze: | OpenAIRE |
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