Capsids of hepatitis B virus e antigen with authentic C termini are stabilized by electrostatic interactions

FEBS Letters

article

Norman R. Watts¹  Ira W. Palmer¹  Elif Eren²  Alasdair C. Steven²  Paul T. Wingfield¹ 

[1] Protein Expression Laboratory, National Institutes of Health;Laboratory of Structural Biology Research, National Institutes of Health

关键词: conformational rearrangement;    e antigen;    encapsidation;    furin cleavage;    HBeAg;    hepatitis B virus;   

DOI  :  10.1002/1873-3468.13706

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown