Characterization of Monoclonal Antibody Specific for Hepatitis C Virus E2 Envelope Protein.
- Author:
Joon Sang PARK
;
Bum Young LEE
;
Soo IL CHUNG
;
Mi Kyung MIN
- Publication Type:Original Article
- MeSH:
Animals;
Antibody Formation;
Ascites;
Cell Membrane;
CHO Cells;
Clone Cells;
Cricetinae;
Hepacivirus*;
Hepatitis C*;
Hepatitis*;
Humans;
Hybridomas;
Insects;
Mice
- From:Journal of the Korean Society of Virology
1997;27(1):9-17
- CountryRepublic of Korea
- Language:Korean
-
Abstract:
Hepatitis C virus (HCV) E2 protein is known to be one of putative envelope proteins. To develop a sensitive detection method for HCV infected tissues and cells, monoclonal antibodys (MAbs) to the E2 protein of HCV were prepared from mice immunized with recombinant baculovirus-expressing E2 protein (Bac-E2). Several hybridoma clones secreting various levels of MAb were isolated and isotypes of these MAb were determined. One clone (L.2.3.3) was used for ascites production and the E2-MAb was purified and characterized. The L.2.3.3 reacted well with both Bac-E2 and E. coli expressed glutathione-5-transferase-E2 (GST-E2) fusion proteins. Using HCV patient sera, E2 envelope protein was found to be localized in the cell membrane boundary both in CHO cells and insect cells which express HCV E2 protein. Similar result was obtained when same cells were treated with the MAb L.2.3.3. These results demonstrated that Bac-E2 protein is capable of eliciting high titer antibody production in mice.
