Structural and nucleic acid binding properties of hepatitis delta virus small antigen

Carolina Alves, Hong Cheng, João Paulo Tavanez, Ana Casaca, Severin Gudima, Heinrich Roder, Celso Cunha

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Abstract

AIM: To further characterize the structure and nucleic acid binding properties of the 195 amino acid small delta antigen, S-HDAg, a study was made of a truncated form of S-HDAg, comprising amino acids 61-195 (∆60HDAg), thus lacking the domain considered necessary for dimerization and higher order multimerization.

METHODS: Circular dichroism, and nuclear magnetic resonance experiments were used to assess the structure of ∆60HDAg. Nucleic acid binding properties were investigated by gel retardation assays.

RESULTS: Results showed that the truncated ∆60HDAg protein is intrinsically disordered but compact, whereas the RNA binding domain, comprising residues 94-146, adopts a dynamic helical conformation. We also found that ∆60HDAg fails to multimerize but still contains nucleic acid binding activity, indicating that multimerization is not essential for nucleic acid binding. Moreover, in agreement with what has been previously reported for full-length protein, no apparent specificity was found for the truncated protein regarding nucleic acid binding.

CONCLUSION: Taken together these results allowed concluding that ∆60HDAg is intrinsically disordered but compact; ∆60HDAg is not a multimer but is still capable of nucleic acid binding albeit without apparent specificity.

Original languageEnglish
Pages (from-to)p. 26-35
Number of pages9
JournalWorld journal of virology
VolumeVol. 6
Issue numbern.º 2
DOIs
Publication statusPublished - 12 May 2017

Keywords

  • Hepatitis delta virus
  • Delta antigen
  • Nuclear magnetic resonance
  • Circular dichroism
  • Intrinsically disordered protein

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