From structural studies to hcv vaccine design

Itai Yechezkel, Mansun Law*, Netanel Tzarum*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

7 Scopus citations

Abstract

Hepatitis C virus (HCV) is a serious and growing public health problem despite recent developments of antiviral therapeutics. To achieve global elimination of HCV, an effective cross-genotype vaccine is needed. The failure of previous vaccination trials to elicit an effective cross-reactive immune response demands better vaccine antigens to induce a potent cross-neutralizing response to improve vaccine efficacy. HCV E1 and E2 envelope (Env) glycoproteins are the main targets for neutralizing antibodies (nAbs), which aid in HCV clearance and protection. Therefore, a molecular-level understanding of the nAb responses against HCV is imperative for the rational design of cross-genotype vaccine antigens. Here we summarize the recent advances in structural studies of HCV Env and Env-nAb complexes and how they improve our understanding of immune recognition of HCV. We review the structural data defining HCV neutralization epitopes and con-formational plasticity of the Env proteins, and the knowledge applicable to rational vaccine design.

Original languageAmerican English
Article number833
JournalViruses
Volume13
Issue number5
DOIs
StatePublished - May 2021

Bibliographical note

Publisher Copyright:
© 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Keywords

  • E1
  • E1E2 complex
  • E2
  • Envelope glycopro-teins
  • Hepatitis C virus (HCV), neutralizing antibodies
  • Neutralization face
  • Structural studies
  • VH1-69
  • Vaccine design

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