Journal
FEBS LETTERS
Volume 594, Issue 6, Pages 1052-1061Publisher
WILEY
DOI: 10.1002/1873-3468.13706
Keywords
conformational rearrangement; e antigen; encapsidation; furin cleavage; HBeAg; hepatitis B virus
Funding
- Intramural Research Program of the National Institute of Arthritis and Musculoskeletal and Skin Diseases of the National Institutes of Health
- NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES [ZIAAR027002, ZIAAR041115] Funding Source: NIH RePORTER
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The hepatitis B virus e antigen, an alternative transcript of the core gene, is a secreted protein that maintains viral persistence. The physiological form has extended C termini relative to Cp(-10)149, the construct used in many studies. To examine the role of the C termini, we expressed the constructs Cp(-10)151 and Cp(-10)154, which have additional arginine residues. Both constructs when treated with reductant formed capsids more efficiently than Cp(-10)149. These capsids were also substantially more stable, as measured by thermal denaturation and resistance to urea dissociation. Mutagenesis suggests that electrostatic interactions between the additional arginine residues and glutamate residues on adjacent subunits play a role in the extra stabilization. These findings have implications for the physiological role and biotechnological potential of this protein.
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