Characterization of hepatitis C virus structural proteins and HCV-like particles produced in recombinant baculovirus infected insect cells

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

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Published inMolekuliarnaia biologiia Vol. 44; no. 1; p. 107
Main Authors Belzhelarskaia, S N, Koroleva, N N, Popenko, V V, Drutsa, V L, Orlova, O V, Rubtsov, P M, Kochetkov, S N
Format Journal Article
LanguageRussian
Published Russia (Federation) 01.01.2010
Subjects
Animals
Baculoviridae
Cell Line
Glycosylation
Hepacivirus - genetics
Hepacivirus - metabolism
Hepacivirus - physiology
Humans
Insecta - cytology
Viral Core Proteins - genetics
Viral Core Proteins - metabolism
Viral Envelope Proteins - genetics
Viral Envelope Proteins - metabolism
Virion - genetics
Virion - metabolism
Virus Assembly
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Summary:Three proteins, namely: "core" protein C and glycoproteins E1 and E2, are main structural proteins forming a hepatitis C vius (HCV) virion. The virus structure and assembly, a 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. Using recombinant baculoviruses expressing HCV structural protein genes in insect cells the specific structural proteins at the level of 25-35% relative to a common cell protein content, heterodimers of the glcoproteins, and HCV-like particles have been obtained. It has been demonstrated that recombinant proteins C, E1, and E2 go through the posttranslation modification, the glycoproteins form the non-covalent heterodimer, and HCV-like particles are located in endoplasmatic reticulum membrains of infected cells. An ability of the expressed proteins for forming E1E2 dimers and HCV-like particles was used for studying the role of E1 protein glcosylation upon expression and processing of the glycoproteins.
ISSN:0026-8984