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 in | Molecular biology (New York) Vol. 44; no. 1; pp. 97 - 108 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
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Dordrecht
SP MAIK Nauka/Interperiodica
01.02.2010
Springer Nature B.V |
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Abstract | 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. |
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AbstractList | 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.[PUBLICATION ABSTRACT] 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. |
Author | Drutza, V. L. Orlova, O. V. Kochetkov, S. N. Koroleva, N. N. Popenko, V. V. Belzhelarskaya, S. N. Rubtzov, P. M. |
Author_xml | – sequence: 1 givenname: S. N. surname: Belzhelarskaya fullname: Belzhelarskaya, S. N. email: belj@eimb.ru organization: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences – sequence: 2 givenname: N. N. surname: Koroleva fullname: Koroleva, N. N. organization: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences – sequence: 3 givenname: V. V. surname: Popenko fullname: Popenko, V. V. organization: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences – sequence: 4 givenname: V. L. surname: Drutza fullname: Drutza, V. L. organization: Chemical Department, Moscow State University – sequence: 5 givenname: O. V. surname: Orlova fullname: Orlova, O. V. organization: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences – sequence: 6 givenname: P. M. surname: Rubtzov fullname: Rubtzov, P. M. organization: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences – sequence: 7 givenname: S. N. surname: Kochetkov fullname: Kochetkov, S. N. organization: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences |
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CitedBy_id | crossref_primary_10_1016_j_bbrep_2016_05_019 crossref_primary_10_1021_jm400125h crossref_primary_10_1134_S002689331101002X crossref_primary_10_1134_S0026893312040115 crossref_primary_10_1016_j_pep_2021_105864 crossref_primary_10_1134_S0026893313010123 |
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Keywords | virus-like particles core-like particles hepatitis C virus HCV structural proteins insect cells glycoprotein glycosylation recombinant baculovirus |
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SubjectTerms | Baculovirus Biochemistry Biomedical and Life Sciences Cell Molecular Biology Gene expression Hepatitis Hepatitis C virus Human Genetics Insects Life Sciences Molecular biology Proteins |
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Title | Hepatitis C virus structural proteins and virus-like particles produced in recombinant baculovirus-infected insect cells |
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