» Articles » PMID: 34064532

From Structural Studies to HCV Vaccine Design

Overview
Journal Viruses
Publisher MDPI
Specialty Microbiology
Date 2021 Jun 2
PMID 34064532
Citations 9
Authors
Affiliations
Soon will be listed here.
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 conformational plasticity of the Env proteins, and the knowledge applicable to rational vaccine design.

Citing Articles

Development of Virus-Like Particles (VLPs) for Hepatitis C Virus genotype 4: a novel approach for vaccine development in Egypt.

Ali A, Azouz R, Hussein N, El-Shenawy R, Helmy N, El-Abd Y BMC Biotechnol. 2025; 25(1):8.

PMID: 39827115 PMC: 11742997. DOI: 10.1186/s12896-024-00935-5.


Sustained Long-Term Decline in Anti-HCV Neutralizing Antibodies in HIV/HCV-Coinfected Patients Five Years after HCV Therapy: A Retrospective Study.

Sepulveda-Crespo D, Volpi C, Amigot-Sanchez R, Yelamos M, Diez C, Gomez J Pharmaceuticals (Basel). 2024; 17(9).

PMID: 39338314 PMC: 11434851. DOI: 10.3390/ph17091152.


Vaccination induces broadly neutralizing antibody precursors to HIV gp41.

Schiffner T, Phung I, Ray R, Irimia A, Tian M, Swanson O Nat Immunol. 2024; 25(6):1073-1082.

PMID: 38816615 PMC: 11147780. DOI: 10.1038/s41590-024-01833-w.


Hepatitis C Virus E1E2 Structure, Diversity, and Implications for Vaccine Development.

Pierce B, Felbinger N, Metcalf M, Toth E, Ofek G, Fuerst T Viruses. 2024; 16(5).

PMID: 38793684 PMC: 11125608. DOI: 10.3390/v16050803.


Future Prospects, Approaches, and the Government's Role in the Development of a Hepatitis C Virus Vaccine.

Tabll A, Sohrab S, Ali A, Petrovic A, Steiner Srdarevic S, Siber S Pathogens. 2024; 13(1).

PMID: 38251345 PMC: 10820710. DOI: 10.3390/pathogens13010038.


References
1.
Wong J, Bhat R, Hockman D, Logan M, Chen C, Levin A . Recombinant hepatitis C virus envelope glycoprotein vaccine elicits antibodies targeting multiple epitopes on the envelope glycoproteins associated with broad cross-neutralization. J Virol. 2014; 88(24):14278-88. PMC: 4249152. DOI: 10.1128/JVI.01911-14. View

2.
Duan H, Kachko A, Zhong L, Struble E, Pandey S, Yan H . Amino acid residue-specific neutralization and nonneutralization of hepatitis C virus by monoclonal antibodies to the E2 protein. J Virol. 2012; 86(23):12686-94. PMC: 3497666. DOI: 10.1128/JVI.00994-12. View

3.
Flint M, Dubuisson J, Maidens C, Harrop R, Guile G, Borrow P . Functional characterization of intracellular and secreted forms of a truncated hepatitis C virus E2 glycoprotein. J Virol. 2000; 74(2):702-9. PMC: 111590. DOI: 10.1128/jvi.74.2.702-709.2000. View

4.
Owsianka A, Tarr A, Juttla V, Lavillette D, Bartosch B, Cosset F . Monoclonal antibody AP33 defines a broadly neutralizing epitope on the hepatitis C virus E2 envelope glycoprotein. J Virol. 2005; 79(17):11095-104. PMC: 1193588. DOI: 10.1128/JVI.79.17.11095-11104.2005. View

5.
Guest J, Pierce B . Computational Modeling of Hepatitis C Virus Envelope Glycoprotein Structure and Recognition. Front Immunol. 2018; 9:1117. PMC: 5985375. DOI: 10.3389/fimmu.2018.01117. View