The native form and maturation process of hepatitis C virus core protein.
نویسندگان
چکیده
The maturation and subcellular localization of hepatitis C virus (HCV) core protein were investigated with both a vaccinia virus expression system and CHO cell lines stably transformed with HCV cDNA. Two HCV core proteins, with molecular sizes of 21 kDa (p21) and 23 kDa (p23), were identified. The C-terminal end of p23 is amino acid 191 of the HCV polyprotein, and p21 is produced as a result of processing between amino acids 174 and 191. The subcellular localization of the HCV core protein was examined by confocal laser scanning microscopy. Although HCV core protein resided predominantly in the cytoplasm, it was also found in the nucleus and had the same molecular size as p21 in both locations, as determined by subcellular fractionation. The HCV core proteins had different immunoreactivities to a panel of monoclonal antibodies. Antibody 5E3 stained core protein in both the cytoplasm and the nucleus, C7-50 stained core protein only in the cytoplasm, and 499S stained core protein only in the nucleus. These results clearly indicate that the p23 form of HCV core protein is processed to p21 in the cytoplasm and that the core protein in the nucleus has a higher-order structure different from that of p21 in the cytoplasm. HCV core protein in sera of patients with HCV infection was analyzed in order to determine the molecular size of genuinely processed HCV core protein. HCV core protein in sera was found to have exactly the same molecular weight as the p21 protein. These results suggest that p21 core protein is a component of native viral particles.
منابع مشابه
Overexpression of Full-Length Core Protein of Hepatitis C Virus by Escherichia coli Cultivated in Stirred Tank Fermentor
The mature core protein of the Hepatitis C virus (HCVC173) carrying pelB as a signal peptide (PelB::core) was overexpressed in Escherichia coli as 18% and 23.3% of the host’s total protein, in flask and fermentor cultivation, respectively. A final specific yield of 25 ± 1 mg HCVC173/g dry cell weight and an overallproductivity of 51±1 mg HCVC173/l/h were obtained in the stirred-tank ferme...
متن کاملExpression of Hepatitis B Virus Core Antigen in Native and Fusion Forms in E. coli
DNA coding for the core antigen from hepatitis B Virus (HBcAg) was amplified, cloned and propagated in E. coli. The core protein was expressed in E. coli and the product was readily detected by Western blot. This protein can be used as a diagnostic material in serum screening tests. To increase the level of expression of this antigen in bacteria, two plasmids were constructed in which the gene ...
متن کاملCpG Motif as an Adjuvant in Immunization of a Recombinant Plasmid Encoding Hepatitis C Virus Core Protein
متن کامل
Using Boehmite Nanoparticles as an Undercoat, and Riboflavin as a Redox Probe for Immunosensor Designing: Ultrasensitive Detection of Hepatitis C Virus Core Antigen
In this study a label-free electrochemical Immunosensor for ultrasensitive detection of Hepatitis C virus core antigen in serum samples was fabricated by using a simple approach. In this method a low-cost and sensitive immunosensor was fabricated based on a boehmite nanoparticles (BNPs) modified glassy carbon. The BNPs provide a specific platform with increased surface area which is capable of ...
متن کاملPriming Hepatitis B Surface (HBsAg)- and Core Antigen (HBcAg)-Specific Immune Responses by Chimeric, HBcAg with a HBsAg ‘a’ Determinant
We developed an immunogen to stimulate multivalent immunity against hepatitis B surface antigen (HBsAg) and hepatitis B core antigens (HBcAg). Immune responses specific for both HBsAg and HBcAg play an important role in controlling the infection. HBsAg-specific antibodies mediate elimination of virions at an early stage of infection and prevent the spread of virus. The immunogen was constructed...
متن کاملPreparation and characterization of PLGA Nanoparticles containing recombinant core-NS3 Fusion protein of hepatitis C virus as a nano-vaccine candidate
Introduction: Hepatitis C virus (HCV) is one of the most serious causes of cirrhosis, liver cancer and ultimately death, worldwide. The new direct-acting drugs are not accessible for many patients around the world and progress toward new therapeutic and anaphylactic vaccines design has not been fast enough. This study was aimed to prepare and assess a recombinant fusion protein core-NS3 (rC-N) ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of virology
دوره 72 7 شماره
صفحات -
تاریخ انتشار 1998