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Alves C , Cheng H , Roder H , Taylor J
Intrinsic disorder and oligomerization of the hepatitis delta virus antigen
Virology. 2010 Nov 25;407(2) :333-40
PMID: 20855099    PMCID: PMC2952689   
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Abstract
The 195 amino acid basic protein (deltaAg) of hepatitis delta virus (HDV) is essential for replication of the HDV RNA genome. Numerous properties have been mapped to full-length deltaAg and attempts made to link these to secondary, tertiary and quaternary structures. Here, for the full-size deltaAg, extensive intrinsic disorder was predicted using PONDR-FIT, a meta-predictor of intrinsic disorder, and evidenced by circular dichroism measurements. Most deltaAg amino acids are in disordered configurations with no more than 30% adopting an alpha-helical structure. In addition, dynamic light scattering studies indicated that purified deltaAg assembled into structures of as large as dodecamers. Cross-linking followed by denaturing polyacrylamide gel electrophoresis revealed hexamers to octamers for this purified deltaAg and at least this size for deltaAg found in virus-like particles. Oligomers of purified deltaAg were resistant to elevated NaCl and urea concentrations, and bound without specificity to RNA and single- and double-stranded DNAs.
Notes
Alves, Carolina Cheng, Hong Roder, Heinrich Taylor, John AI-256522/AI/NIAID NIH HHS/United States CA-06927/CA/NCI NIH HHS/United States R01 GM056250/GM/NIGMS NIH HHS/United States Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't United States Virology Virology. 2010 Nov 25;407(2):333-40. Epub 2010 Sep 19.