Abstract:
:The p7 protein from hepatitis C virus is critical for the assembly and secretion of infectious virus, making it an attractive drug target. It is thought to be a viroporin with a demonstrated ion channel activity when reconstituted into planar lipid bilayers. Electron microscopy experiments suggest that p7 oligomers coexist as hexamers and heptamers. Proposed models of p7 oligomers assume the N-terminal helix to be the pore lining helix. Here, we demonstrate, via electrophysiology, that Cu(2+) has an inhibitory effect on the p7 ion channel and that the amino acid responsible for this inhibition is one histidine in each monomer. This information coupled with the p7 sequence data suggests that the N-terminal helix of p7 does indeed form the transmembrane pore and that this histidine is pore-lining. The information will aid in the construction of oligomeric pore-models and the interpretation of electron microscopy data.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Chew CF,Vijayan R,Chang J,Zitzmann N,Biggin PCdoi
10.1016/j.bpj.2008.10.004subject
Has Abstractpub_date
2009-01-01 00:00:00pages
L10-2issue
2eissn
0006-3495issn
1542-0086pii
S0006-3495(08)00048-9journal_volume
96pub_type
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