Structure-Based Design of Hepatitis C Virus E2 Glycoprotein Improves Serum Binding and Cross-Neutralization

Brian G. Pierce, Zhen–Yong Keck, Ruixue Wang, Patrick Lau, Kyle Garagusi, Khadija Elkholy, Eric A. Toth, Richard A. Urbanowicz, Johnathan D. Guest, Pragati Agnihotri,

Journal of Virology · 2020 · 34 citations · 59 references

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Abstract

Hepatitis C virus infects approximately 1% of the world’s population, and no vaccine is currently available. Due to the high variability of HCV and its ability to actively escape the immune response, a goal of HCV vaccine design is to induce neutralizing antibodies that target conserved epitopes. Here, we performed structure-based design of several epitopes of the HCV E2 envelope glycoprotein to engineer its antigenic properties. Designs were tested in vitro and in vivo , demonstrating alteration of the E2 antigenic profile in several cases, and one design led to improvement of cross-neutralization of heterologous viruses. This represents a proof of concept that rational engineering of HCV envelope glycoproteins can be used to modulate E2 antigenicity and optimize a vaccine for this challenging viral target.

References

59