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Ian Zon

As seen in: Nature, BioRxiv
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Articles by Ian Zon

Structure-based design of stable recombinant hepatitis C virus E1E2 heterodimers

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By Joan Capella-Pujol, Fabien Cannac, Stan Peters, Maddy L. Newby, Meliawati Poniman, Ian Zon, Wouter Olijhoek, Tim Beaumont, Max Crispin, Andrew Ward, Janke Schinkel, Rogier W. Sanders, Kwinten Sliepen, Fabian Mulder
| Nature Verified
Abstract Hepatitis C virus (HCV) affects 47 million people and causes 239,000 deaths annually, yet no vaccine is on the horizon. Generating a stable native-like mimic of the envelope complex E1E2, the only target for known neutralizing antibodies, is an important aim for HCV vaccine development.
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Bispecific antibodies against the hepatitis C virus E1E2 envelope glycoprotein

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By Laura Radić, Anna Offersgaard, Ian Zon, Tereza Kadavà
| BioRxiv
Abstract Hepatitis C virus (HCV) currently causes about one million infections and 240,000 deaths worldwide each year. To reach the goal set by the World Health Organization (WHO) of global HCV elimination by 2030, it is critical to develop a prophylactic vaccine. Broadly neutralizing antibodies (bNAbs) target the E1E2 envelope glycoproteins on the viral surface, can neutralize a broad range of the highly diverse circulating HCV strains and are essential tools to inform vaccine design.
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Signatures of VH1-69-derived hepatitis C virus neutralizing antibody precursors defined by binding to envelope glycoproteins - Nature Communications

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By Rogier W. Sanders, Joan Capella-Pujol, Laura Radić, Ian Zon, Ana Chumbe
| Nature Verified
Abstract An effective preventive vaccine for hepatitis C virus (HCV) remains a major unmet need. Antigenic region 3 (AR3) on the E1E2 envelope glycoprotein complex overlaps with the CD81 receptor binding site and represents an important epitope for broadly neutralizing antibodies (bNAbs) and is therefore important for HCV vaccine design. Most AR3 bNAbs utilize the VH1-69 gene and share structural features that define the AR3C-class of HCV bNAbs.
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