Effect of Glycan Shift on Antibodies against Hepatitis C Virus E2 412–425 Epitope Elicited by Chimeric sHBsAg-Based Virus-Like Particles

Author:

Czarnota Anna1ORCID,Offersgaard Anna23ORCID,Owsianka Ania4,Alzua Garazi Peña23ORCID,Bukh Jens23ORCID,Gottwein Judith Margarete23ORCID,Patel Arvind H.4ORCID,Bieńkowska-Szewczyk Krystyna1ORCID,Grzyb Katarzyna1ORCID

Affiliation:

1. Laboratory of Virus Molecular Biology, Intercollegiate Faculty of Biotechnology of the University of Gdańsk and Medical University of Gdańsk, Gdańsk, Poland

2. Copenhagen Hepatitis C Program (CO-HEP), Department of Infectious Diseases, Copenhagen University Hospital—Hvidovre, Hvidovre, Denmark

3. Department of Immunology and Microbiology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark

4. MRC-University of Glasgow Centre for Virus Research, Glasgow, United Kingdom

Abstract

Epitope I, located within amino acids 412 to 423 of the HCV E2 glycoprotein, is an important target for an epitope-based HCV vaccine. One interesting feature of epitope I is the N417 glycosylation site, where a single change to S417 or T417 can shift the glycosylation site to position N415.

Funder

National Science Centre, Poland

University of Gdansk LiSMIDOS Research Project

Candys Foundation

University of Copenhagen

Danmarks Frie Forskningsfond

Innovation Fund, Denmark

Hvidovre Hospital

Læge Sophus Carl Emil Friis og hustru Olga Doris Friis' Legat

The Toyota Foundation

UKRI | Medical Research Council

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Cell Biology,Microbiology (medical),Genetics,General Immunology and Microbiology,Ecology,Physiology

Reference55 articles.

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