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BukuHepatitis C virus: The role of N-glycosylation sites of viral genotype 1b proteins for formation of viral particles in insect and mammalian cells (from Biochemistry and Biophysics Reports 2016, 7, 98-105)
Bibliografi
Author: Beljelarskaya, S. N. ; Orlova, O. V. ; Drutsa, V. L. ; Orlov, V. A. ; Timohova, A. V. ; Koroleva, N. N. ; Popenko, V. I. ; Ivanov, A. V. ; Spirin, P. V. ; Prassolov, P. V. ; Rubtsov, P. M. ; Kochetkov, S. N.
Topik: Hepatitis C virus; HCV envelope glycoproteins; N-glycans; Baculovirus; Insect Sf9 cells; Mammalian Hek293 Tcells; Site-directed mutagenesis; Seminar - thesis lit
Bahasa: (EN )    
Penerbit: Elsevier     Tahun Terbit: 2016    
Jenis: Article - diterbitkan di jurnal ilmiah internasional
Fulltext: 1-s2.0-S2405580816300814-main.pdf (1.6MB; 0 download)
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Abstract
Hepatitis C virus (HCV) is characterized by considerable genetic variability and, as a consequence, it has 6 genotypes and multitude of subtypes. HCV envelope glycoproteins are involved in the virion formation; the correct folding of these proteins plays the key role in virus infectivity. Glycosylation at certain sites of different genotypes HCV glycoproteins shows substantial differences infunctions of the individual glycans (Goffardetal., 2005; Helleetal., 2010) [1,2]. In this study, differential glycosylation sites of HCV genotype 1b envelope proteins in insect and mammalian cells was demonstrated. We showed that part of glyco-
sylation sites was important for folding of the proteins involved in the formation of viral particles. Point mutations were introduced in the protein N-glycosylation sites of HCV (genotype 1b) and the mutant proteins were analyzed using baculovirus expression system in mammalian and insect cells. Our data showed that, incontrast to HCV 1a and 2a, the folding of HCV 1b envelope proteins E2 (sites N1, N2, N10) and E1 (sites N1, N5) was disrupted, however that did not prevent the formation of virus-like particles (VLP)with misfolded glycoproteins having densities typical for HCV particles containing RNA fragments. Experimental data are supported by mathematical modeling of the structure of E1 mutant variants.

[seminar - thesis lit]
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