Hepatitis C virus p7 mediates membrane-to-membrane adhesion

Gi Young Lee, Sora Lee, Hye Ra Lee, Do Yoo Young

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


Viroporin p7 of the hepatitis C virus (HCV) acts as an ion channel for pH equilibration to stabilize HCV particles; most studies of p7 have focused on this role. However, pH equilibration by p7 via its ion channel activity does not fully explain the importance of p7 in HCV particle production. Indeed, several researchers have suggested p7 to have an unidentified ion channel-independent function. Here, we show that p7 has a novel role as a lipid raft adhesion factor, which is independent of its ion channel activity. We found that p7 targets not only the liquid-disordered (Ld) phase, but also the negatively-charged liquid-ordered (Lo) phase that can be represented as a lipid raft. p7 clusters at the phase boundary of the neutral Ld phase and the negatively-charged Lo phase. Interestingly, p7 targeting the Lo phase facilitates membrane-to-membrane adhesion, and this activity is not inhibited by p7 ion channel inhibitors. Our results demonstrated that HCV p7 has dual roles as a viroporin and as a lipid raft adhesion factor. This ion channel-independent function of p7 might be an attractive target for development of anti-HCV compounds.

Original languageEnglish
Pages (from-to)1096-1101
Number of pages6
JournalBiochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Issue number9
Publication statusPublished - 2016 Sept 1


  • Hepatitis C virus p7
  • Lipid raft
  • Membrane adhesion

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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