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Homotypic interaction and multimerization of hepatitis C virus core protein
M Matsumoto1, S B Hwang, K S Jeng
1Howard Hughes Medical Institute,University of Southern California School of Medicine, Los Angeles, California, 90033, USA.
Virology
|April 1, 1996
Summary
Hepatitis C virus (HCV) core protein self-interacts and forms multimers. This multimerization, occurring early in viral assembly, involves the N-terminal region and suggests diverse functions for HCV core protein.
Area of Science:
- Virology
- Molecular Biology
- Biochemistry
Background:
- Hepatitis C virus (HCV) core protein forms the viral nucleocapsid.
- The HCV core protein is known to have multiple functions beyond structural roles.
Purpose of the Study:
- To investigate the homotypic interaction and multimerization of the HCV core protein.
- To identify the specific domains responsible for these interactions and multimerization.
Main Methods:
- Yeast two-hybrid system to detect protein-protein interactions.
- In vitro protein-protein blotting assays using recombinant proteins.
- Glutathione S-transferase (GST) pull-down assays.
- Detection of multimeric forms in mammalian cells.
Main Results:
- Demonstrated homotypic interaction of HCV core protein in vitro and in vivo.
- Identified amino acids 36-91 within the N-terminal hydrophilic region (1-115) as crucial for interaction.
- Confirmed the presence of dimeric and multimeric forms of HCV core protein in mammalian cells.
- The N-terminal hydrophilic region (1-115) is responsible for multimerization.
Conclusions:
- HCV core protein self-interaction and multimerization are significant biological events.
- Multimerization occurs early in the viral assembly process.
- The multimeric forms of HCV core protein likely play roles in various viral functions.