Intrinsic disorder and oligomerization of the hepatitis delta virus antigen
| Autor: | Carolina Alves, Heinrich Roder, Hong Cheng, John M. Taylor |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Circular dichroism
Molecular Sequence Data Biology Article 03 medical and health sciences chemistry.chemical_compound Virus antigen Protein structure Virology Protein oligomerization Animals Amino Acid Sequence Protein Structure Quaternary Polyacrylamide gel electrophoresis 030304 developmental biology chemistry.chemical_classification Hepatitis delta Antigens 0303 health sciences Circular Dichroism 030302 biochemistry & molecular biology RNA Molecular biology 3. Good health Amino acid chemistry Biochemistry DNA Viral RNA Viral Electrophoresis Polyacrylamide Gel Hepatitis Delta Virus Protein Multimerization DNA Software |
| Zdroj: | Virology. 407(2):333-340 |
| ISSN: | 0042-6822 |
| DOI: | 10.1016/j.virol.2010.08.019 |
| Popis: | The 195 amino acid basic protein (δAg) of hepatitis delta virus (HDV) is essential for replication of the HDV RNA genome. Numerous properties have been mapped to full-length δAg and attempts made to link these to secondary, tertiary and quaternary structures. Here, for the full-size δAg, extensive intrinsic disorder was predicted using PONDR-FIT, a meta-predictor of intrinsic disorder, and evidenced by circular dichroism measurements. Most δAg amino acids are in disordered configurations with no more than 30% adopting an α-helical structure. In addition, dynamic light scattering studies indicated that purified δAg assembled into structures of as large as dodecamers. Cross-linking followed by denaturing polyacrylamide gel electrophoresis revealed hexamers to octamers for this purified δAg and at least this size for δAg found in virus-like particles. Oligomers of purified δAg were resistant to elevated NaCl and urea concentrations, and bound without specificity to RNA and single- and double-stranded DNAs. |
| Databáze: | OpenAIRE |
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