Elsevier

Virology

Volume 407, Issue 2, 25 November 2010, Pages 333-340
Virology

Intrinsic disorder and oligomerization of the hepatitis delta virus antigen

https://doi.org/10.1016/j.virol.2010.08.019Get rights and content
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Abstract

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.

Research Highlights

►Majority of hepatitis delta antigen exhibits intrinsic disorder ►Purified delta antigen forms stable multimers ►Delta antigen multimers bind without specificity to nucleic acids.

Keywords

Hepatitis delta virus
Delta antigen
Intrinsic disorder
Protein oligomerization
Nucleic acid binding

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1

Current address: Molecular Biology Unit, Center for Malaria and Tropical Diseases, Institute of Hygiene and Tropical Medicine, New University of Lisbon, Lisbon, Portugal.