A hydrophobic heptad repeat of the core protein of woodchuck hepatitis virus is required for capsid assembly
نویسندگان
چکیده
منابع مشابه
A C-terminal hydrophobic region is required for homo-oligomerization of the hepatitis E virus capsid (ORF2) protein
Hepatitis E virus (HEV) is the causative agent of hepatitis E, an acute form of viral hepatitis. The open reading frame 2 (ORF2) of HEV encodes the viral capsid protein, which can self-oligomerize into virus-like particles. To understand the domains within this protein important for capsid biogenesis, we have carried out in vitro analyses of association and folding patterns of wild type and mut...
متن کاملA domain of the hepadnavirus capsid protein is specifically required for DNA maturation and virus assembly.
Mutations introduced into the capsid gene of duck hepatitis B virus (DHBV) were tested for their effects on viral DNA synthesis and assembly of enveloped viruses. Four classes of mutant phenotypes were observed among a series of deletions of covering the 3' end of the capsid open reading frame. Class I mutant capsids were able to support normal single-stranded and relaxed circular viral DNA syn...
متن کاملCore protein cleavage by signal peptide peptidase is required for hepatitis C virus-like particle assembly.
Hepatitis C virus (HCV) core protein, expressed with a Semliki Forest virus replicon, self-assembles into HCV-like particles (HCV-LP) at the endoplasmic reticulum (ER) membrane, providing an opportunity to study HCV assembly and morphogenesis by electron microscopy. This model was used to investigate whether the processing of the HCV core protein by the signal peptide peptidase (SPP) is require...
متن کاملThe Hepatitis B Virus Core Protein Intradimer Interface Modulates Capsid Assembly and Stability
During the hepatitis B virus (HBV) life cycle, capsid assembly and disassembly must ensure correct packaging and release of the viral genome. Here we show that changes in the dynamics of the core protein play an important role in regulating these processes. The HBV capsid assembles from 120 copies of the core protein homodimer. Each monomer contains a conserved cysteine at position 61 that can ...
متن کاملThe first hydrophobic domain of the hepatitis C virus E1 protein is important for interaction with the capsid protein.
The interaction between the hepatitis C virus capsid protein and the envelope protein E1 has been demonstrated previously in vivo. To determine the binding region of the E1 protein with the capsid protein, this interaction was characterized in vitro. This study shows that the interaction between these proteins should occur in the endoplasmic reticulum membrane rather than in the cytosol and tha...
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ژورنال
عنوان ژورنال: Journal of Virology
سال: 1996
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.70.10.7085-7091.1996