Differential formation of disulfide linkages in the core antigen of extracellular and intracellular hepatitis B virus core particles.
Our understanding of the assembly of hepatitis B virus is still very limited. We present evidence to demonstrate that the HBc antigen formed oligomers through disulfide linkages in the extracellular hepatitis B virus core (HBc) particles. However, the intracellular HBV core particles did not contain disulfide-linked HBc antigens. Furthermore, the extracellular particles which had disulfide bonds were more stable than intracellular particles at pH 7.5 and 10 and in 3 M NaCl and 4 M urea. These data suggest that the formation of disulfide bonds in the HBc antigen is important for the integrity of the viral core particles.
Jeng
K S
KS
Graduate Institute of Microbiology and Immunology, National Yang-Ming Medical College, Taipei, Taiwan, Republic of China.
Hu
C P
CP
Chang
C M
CM
D002213:Capsid / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D006512:Hepatitis B Core Antigens / Q000737:chemistry / Q000378:metabolism*; D006515:Hepatitis B virus / Q000648:ultrastructure*; D007460:Iodoacetamide / Q000737:chemistry; D014758:Viral Core Proteins / Q000737:chemistry
D004220:Disulfides; D006512:Hepatitis B Core Antigens; D014758:Viral Core Proteins; D007460:Iodoacetamide