Next Article in Journal
Structural Insights into the Respiratory Syncytial Virus RNA Synthesis Complexes
Next Article in Special Issue
Structure-Based and Rational Design of a Hepatitis C Virus Vaccine
Previous Article in Journal
Identification of the SHREK Family of Proteins as Broad-Spectrum Host Antiviral Factors
Previous Article in Special Issue
To Include or Occlude: Rational Engineering of HCV Vaccines for Humoral Immunity
Open AccessReview

From Structural Studies to HCV Vaccine Design

1
Department of Biological Chemistry, Alexander Silberman Institute of Life Sciences, Faculty of Mathematics & Science, The Hebrew University of Jerusalem, Jerusalem 9190401, Israel
2
Department of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA
*
Authors to whom correspondence should be addressed.
Academic Editor: Thomas Fuerst
Viruses 2021, 13(5), 833; https://doi.org/10.3390/v13050833
Received: 2 April 2021 / Revised: 21 April 2021 / Accepted: 28 April 2021 / Published: 4 May 2021
(This article belongs to the Special Issue Novel Advances in Vaccines against HCV)
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 conformational plasticity of the Env proteins, and the knowledge applicable to rational vaccine design. View Full-Text
Keywords: hepatitis C virus (HCV); neutralizing antibodies; structural studies; envelope glycoproteins; E1; E2; E1E2 complex; VH1-69; neutralization face; vaccine design hepatitis C virus (HCV); neutralizing antibodies; structural studies; envelope glycoproteins; E1; E2; E1E2 complex; VH1-69; neutralization face; vaccine design
Show Figures

Figure 1

MDPI and ACS Style

Yechezkel, I.; Law, M.; Tzarum, N. From Structural Studies to HCV Vaccine Design. Viruses 2021, 13, 833. https://doi.org/10.3390/v13050833

AMA Style

Yechezkel I, Law M, Tzarum N. From Structural Studies to HCV Vaccine Design. Viruses. 2021; 13(5):833. https://doi.org/10.3390/v13050833

Chicago/Turabian Style

Yechezkel, Itai; Law, Mansun; Tzarum, Netanel. 2021. "From Structural Studies to HCV Vaccine Design" Viruses 13, no. 5: 833. https://doi.org/10.3390/v13050833

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop