期刊
JOURNAL OF VIROLOGICAL METHODS
卷 166, 期 1-2, 页码 12-20出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jviromet.2010.01.017
关键词
Hepatitis C virus; Potato virus X; Recombinant protein; Epitope presentation; Chimeric virus particle; Plant-based vaccine
The immunogenic properties of chimeric potato virus X (PVX) particles engineered to display the synthetic R9 peptide have been evaluated. The R9 peptide is a consensus sequence derived from diverse variants of the hypervariable region 1 from the hepatitis C virus (HCV) envelope protein E2. Two different constructs were designed, with the R9 peptide expressed either as an indirect fusion via the ribosomal skip 2A (PVXR9-2ACP) sequence or as a direct PVX coat protein fusion ((PVXCP)-C-R9). Systemic infection of Nicotiana benthamiana plants was only achieved with PVXR9-2ACP constructs, and the presence of the R9 peptide was detected in extracts from these plants by ELISA, Western blot and electron microscopy using specific anti-R9 antibodies. The virus particles were recovered at yields of up to 125 mg/kg from leaf material. BALB/c mice immunized with purified PVXR9-2ACP particles developed specific anti-R9 IgG titers of up to 1:50,000. Monoclonal anti-R9 antibodies were obtained from the spleen of a mouse immunized with PVXR9-2ACP particles and characterized by Western blot and electron microscopy. Sera from patients infected chronically with HCV were found to react specifically with PVXR9-2ACP particles in 35% of cases. (C) 2010 Elsevier B.V. All rights reserved.
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