Hepatitis C virus structural proteins and virus-like particles produced in recombinant baculovirus-infected insect cells

Three proteins, namely, the core protein C and envelope glycoproteins E1 and E2, are main structural proteins forming a hepatitis C virus (HCV) virion. The virus structure and assembly and the role of the structural proteins in virion morphogenesis remain unknown because of the lack of an efficient...

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Published inMolecular biology (New York) Vol. 44; no. 1; pp. 97 - 108
Main Authors Belzhelarskaya, S. N., Koroleva, N. N., Popenko, V. V., Drutza, V. L., Orlova, O. V., Rubtzov, P. M., Kochetkov, S. N.
Format Journal Article
LanguageEnglish
Published Dordrecht SP MAIK Nauka/Interperiodica 01.02.2010
Springer Nature B.V
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Summary:Three proteins, namely, the core protein C and envelope glycoproteins E1 and E2, are main structural proteins forming a hepatitis C virus (HCV) virion. The virus structure and assembly and the role of the structural proteins in virion morphogenesis remain unknown because of the lack of an efficient culture system for HCV to be grown in vitro. Highly efficient heterologous expression systems make it possible to obtain self-assembled, nonreplicating, genome-lacking particles that are morphologically similar to intact virions. Using recombinant baculoviruses expressing the HCV structural protein genes in insect cells, the individual HCV structural proteins were expressed to 25–35% of the total cell protein, and the CE1 and E1E2 heterodimers and HCV-like particles were obtained. It was demonstrated that the recombinant C, E1, and E2 proteins underwent posttranslational modification, the glycoproteins formed a noncovalent heterodimer, and HCV- like particles were located in endoplasmic reticulum membranes of infected cells. The formation of E1E2 dimers and HCV-like particles was used to study the effect of E1 glycosylation on the expression and processing of the coat proteins.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
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ISSN:0026-8933
1608-3245
DOI:10.1134/S0026893310010139