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Hepatitis C virus E1 recruits high-density lipoprotein to support infectivity and evade antibody recognition

Authors
  • Casiano Matos, Jennifer
  • Harichandran, Kaneemozhe
  • Tang, Jingrong
  • Sviridov, Denis O.
  • Sidoti Migliore, Giacomo
  • Suzuki, Motoshi
  • Olano, Lisa R.
  • Hobbs, Alvaro
  • Kumar, Ashish
  • Paskel, Myeisha U.
  • Bonsignori, Mattia
  • Dearborn, Altaira D.
  • Remaley, Alan T.
  • Marcotrigiano, Joseph
Type
Published Article
Journal
Journal of Virology
Publisher
American Society for Microbiology
Publication Date
Jan 04, 2024
Volume
98
Issue
1
Identifiers
DOI: 10.1128/jvi.00849-23
Source
ASM Journals
Keywords
License
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Abstract

Hepatitis C virus (HCV) infection is a significant burden on human health, but vaccine candidates have yet to provide broad protection against this infection. We have developed a method to produce high quantities of soluble E1 or E2, the viral proteins located on the surface of HCV. HCV has an unusually high lipid content due to the recruitment of apolipoproteins. We found that E1 (and not E2) preferentially recruits host high-density lipoprotein (HDL) extracellularly. This recruitment of HDL by E1 prevents binding of E1 by a neutralizing antibody and furthermore prevents antibody-mediated neutralization of the virus. By comparison, low-density lipoprotein does not protect the virus from antibody-mediated neutralization. Our findings provide mechanistic insight into apolipoprotein recruitment, which may be critical for vaccine development.

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