Cloning and production of functional active recombinant hepatitis B virus surface antigen binding protein.
Endonexin II present on the surface of human hepatocytes has recently been identified as a hepatitis B virus surface antigen (HBsAg) binding protein. A full-length cDNA clone encoding human endonexin II was isolated from a human liver cDNA library and was placed under the control of the polyhedrin promoter of Autographa californica nuclear polyhedrosis virus (AcNPV). Infection of Spodoptera frugiperda cells with recombinant virus resulted in the production of high amounts of recombinant protein. This protein has the same molecular weight and iso-electric point as native human endonexin II. It can be easily purified by methods analogous to those described for the native protein. Moreover, the recombinant product binds very efficiently to hepatitis B surface proteins (HBsAg) in a similar fashion as native human endonexin II.
Leenders
W P
WP
Division of Gastro-enterology and Liver Diseases, St. Radboud University Hospital, Nijmegen, The Netherlands.
de Bruin
W C
WC
D000818:Animals; D017304:Annexin A5 / Q000235:genetics*; D001483:Base Sequence; D002478:Cells, Cultured; D003001:Cloning, Molecular; D018076:DNA, Complementary; D006514:Hepatitis B Surface Antigens / Q000378:metabolism*; D006515:Hepatitis B virus / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D017924:Nucleopolyhedroviruses / Q000235:genetics; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D018411:Spodoptera
D017304:Annexin A5; D018076:DNA, Complementary; D006514:Hepatitis B Surface Antigens; D011994:Recombinant Proteins