Journal article
An Optimized Hepatitis C Virus E2 Glycoprotein Core Adopts a Functional Homodimer That Efficiently Blocks Virus Entry
Kathleen McCaffrey, Irene Boo, Catherine M Owczarek, Matthew P Hardy, Matthew A Perugini, Louis Fabri, Pierre Scotney, Pantelis Poumbourios, Heidi E Drummer
Journal of Virology | AMER SOC MICROBIOLOGY | Published : 2017
DOI: 10.1128/JVI.01668-16
Abstract
The hepatitis C virus (HCV) envelope glycoprotein E2 is the major target of broadly neutralizing antibodies in vivo and is the focus of efforts in the rational design of a universal B cell vaccine against HCV. The E2 glycoprotein exhibits a high degree of amino acid variability which localizes to three discrete regions: hypervariable region 1 (HVR1), hypervariable region 2 (HVR2), and the intergenotypic variable region (igVR). All three variable regions contribute to immune evasion and/or isolate-specific structural variations, both important considerations for vaccine design. A high-resolution structural definition of the intact HCV envelope glycoprotein complex containing E1 and E2 remains..
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Awarded by National Health and Medical Research Council (NHMRC)
Awarded by NHMRC
Funding Acknowledgements
We gratefully acknowledge funding support from the National Health and Medical Research Council (NHMRC) through project grants 543113, 1020175, and 1080045. H.E.D. was the recipient of RD Wright Fellowship 433929 and is currently supported by Senior Research Fellowship 1041897 from the NHMRC. K.M. was the recipient of Dora Lush Postgraduate Biomedical Scholarship 433913 and is currently supported by a Marie Curie International Postdoctoral Fellowship from the European Commission. We also gratefully acknowledge the contribution to this work of the Victorian Operational Infrastructure Support Program received by the Burnet Institute.