Open AccessEffects of microvirin monomers and oligomers on hepatitis C virus
Author(s) -
YuanQin Min,
Xuchu Duan,
Yidan Zhou,
Anna Kulinich,
Meng Wang,
Zhi-Peng Cai,
Hongyu Ma,
Li Liu,
XiaoLian Zhang,
Josef Voglmeir
Publication year - 2017
Publication title -
bioscience reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.938
H-Index - 77
eISSN - 1573-4935
pISSN - 0144-8463
DOI - 10.1042/bsr20170015
Subject(s) - mannose , glycoprotein , monomer , linker , chemistry , glycan , neutralization , viral envelope , hepatitis c virus , virology , peptide , biochemistry , microbiology and biotechnology , virus , biology , polymer , organic chemistry , computer science , operating system
Microvirin (MVN) is a carbohydrate-binding protein which shows high specificity for high-mannose type N-glycan structures. In the present study, we tried to identify whether MVN could bind to high-mannose containing hepatitis C virus (HCV) envelope glycoproteins, which are heavily decorated high-mannose glycans. In addition, recombinantly expressed MVN oligomers in di-, tri- and tetrameric form were evaluated for their viral inhibition. MVN oligomers bound more efficiently to HCV virions, and displayed in comparison with the MVN monomer a higher neutralization potency against HCV infection. The antiviral effect was furthermore affected by the peptide linker sequence connecting the MVN monomers. The results indicate that MVN oligomers such as trimers and tetramers may be used as future neutralization agents against HCV infections.
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