Structural comparisons of hepatitis B core antigen particles with different C-terminal lengths.
Core protein of hepatitis B virus (HBV) with various C-terminal lengths (residue 154, 164, 167 and 183) can self-assemble into recombinant hepatitis B core antigen (HBcAg) particles. To understand the RNA encapsidation mechanism of HBV, the three-dimensional structures of these particles were reconstructed by cryo-electron microscopy (cryoEM). Detailed structural comparisons showed that their capsid structures are highly similar, while the RNA content is increased upon the retention of more amino acid residues at the C-terminus of core protein, suggesting the crucial role of the basic C-terminal tail on determining the genome size.
Liu
Shuyu
S
State Key Laboratory of Biocontrol, Sun Yat-sen University, Guangzhou 510275, China.
He
Jian
J
Shih
Chiaho
C
Li
Kunpeng
K
Dai
Aguang
A
Zhou
Z Hong
ZH
Zhang
Jingqiang
J
D002213:Capsid / Q000648:ultrastructure; D020285:Cryoelectron Microscopy; D006512:Hepatitis B Core Antigens / Q000235:genetics* / Q000648:ultrastructure*; D006515:Hepatitis B virus / Q000235:genetics* / Q000648:ultrastructure*; D006801:Humans; D020836:Protein Structure, Quaternary; D012367:RNA, Viral / Q000378:metabolism; D017384:Sequence Deletion
D006512:Hepatitis B Core Antigens; D012367:RNA, Viral