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

World Journal of Virology 2017年第2期6卷 26-35页

作者： Carolina Alves Hong Cheng Joao Paulo Tavanez Ana Casaca s.verin gudima Heinrich Roder Celso Cunha Global Health and Tropical Medicine GHTMInstituto de Higiene e Medicina Tropical IHMTUniversidade Nova de Lisboa Institute for Cancer Research Fox Chase Cancer Center Global Health and Tropical Medicine GHTM Instituto de Higiene e Medicina Tropical IHMT Universidade Nova de Lisboa Department of Microbiology Molecular Genetics and ImmunologyKansas University Medical Center

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 *** 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 *** 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.

关键词： Hepatitis delta virus Delta antigen Nuclear magnetic resonance Circular dichroism Intrinsically disordered protein

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