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Alves C, Cheng H, Tavanez JP, et al. Structural and nucleic acid binding properties of hepatitis delta virus small antigen. World J Virol. 2017;6(2):26-35doi: 10.5501/wjv.v6.i2.26.
Alves, C., Cheng, H., Tavanez, J. P., Casaca, A., Gudima, S., Roder, H., & Cunha, C. (2017). Structural and nucleic acid binding properties of hepatitis delta virus small antigen. World journal of virology, 6(2), 26-35. https://doi.org/10.5501/wjv.v6.i2.26
Alves, Carolina, et al. "Structural and nucleic acid binding properties of hepatitis delta virus small antigen." World journal of virology vol. 6,2 (2017): 26-35. doi: https://doi.org/10.5501/wjv.v6.i2.26
Alves C, Cheng H, Tavanez JP, Casaca A, Gudima S, Roder H, Cunha C. Structural and nucleic acid binding properties of hepatitis delta virus small antigen. World J Virol. 2017 May 12;6(2):26-35. doi: 10.5501/wjv.v6.i2.26. PMID: 28573087; PMCID: PMC5437381.
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World J Virol. 2017 May 12;6(2):26-35. doi: 10.5501/wjv.v6.i2.26.

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

World journal of virology

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

Affiliations

  1. Carolina Alves, João Paulo Tavanez, Ana Casaca, Celso Cunha, Global Health and Tropical Medicine, GHTM, Instituto de Higiene e Medicina Tropical, IHMT, Universidade Nova de Lisboa, 1349-008 Lisboa, Portugal.

PMID: 28573087 PMCID: PMC5437381 DOI: 10.5501/wjv.v6.i2.26

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.

Keywords: Circular dichroism; Delta antigen; Hepatitis delta virus; Intrinsically disordered protein; Nuclear magnetic resonance

Conflict of interest statement

Conflict-of-interest statement: The authors declare no conflicts of interest.

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