Simple method for efficient production of hepatitis B virus core antigen in Escherichia coli.
To obtain good antigenicity and high purity of the hepatitis B virus core antigen (HBcAg) in large quantities without using the fused protein technique employed in recombinant DNA technology, a protein molecule with the same primary sequence as that of wild-type HBcAg (subtype adr) was directly expressed in Escherichia coli JM109 (DE3) using pGd1 expression vector. Purification of the expressed HBcAg yielded high-quality protein by means of simple purification steps, such as sonication, ammonium sulphate precipitation and heat treatment, before final purification by conventional ultra-centrifugation. The HBcAg preparation thus obtained contains small round particles similar in appearance to the HBcAg particles from the HBV-infected human liver tissue.
Naito
M
M
Department of Gene Research, Cancer Institute, JFCR, Tokyo, Japan.
Ishii
K
K
Nakamura
Y
Y
Kobayashi
M
M
Takada
S
S
Koike
K
K
D004926:Escherichia coli / Q000235:genetics; D005814:Genes, Viral; D005822:Genetic Vectors; D006512:Hepatitis B Core Antigens / Q000096:biosynthesis* / Q000235:genetics / Q000302:isolation & purification* / Q000648:ultrastructure; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification*; D015678:Viral Structural Proteins / Q000235:genetics
D006512:Hepatitis B Core Antigens; D011994:Recombinant Proteins; D015678:Viral Structural Proteins