Isolation and characterization of human monoclonal antibodies against hepatitis C virus envelope glycoproteins

Details

Serval ID
serval:BIB_06A73E4AC6FC
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Isolation and characterization of human monoclonal antibodies against hepatitis C virus envelope glycoproteins
Journal
Journal of Medical Virology
Author(s)
da Silva Cardoso  M., Siemoneit  K., Sturm  D., Krone  C., Moradpour  D., Kubanek  B.
ISSN
0146-6615 (Print)
Publication state
Published
Issued date
05/1998
Volume
55
Number
1
Pages
28-34
Notes
Journal Article --- Old month value: May
Abstract
The isolation and characterization of human monoclonal antibodies (humAbs) against the hepatitis C Virus (HCV) glycoproteins E1 and E2 are described. B-cells from blood donors with anti-HCV were transformed with Epstein-Barr virus. The supernatants of the resulting lymphoblastoid clones were screened by ELISA with an extract of cells infected with a recombinant vaccinia virus RMPA95 expressing the envelope proteins E1 and E2 of an HCV genotype 1a virus (H strain). Positive clones were fused to the heteromyeloma cell line K6H6/B5. Fifteen heterohybridoma cell lines have been established. The specificity of the isolated humAbs was determined both by ELISA and Western blot assays. Several recombinant extracts expressing either the E1 or E2 protein or truncated forms were used in an attempt to map the epitopes on the viral glycoproteins. Some of the humAbs were used successfully for immunofluorescence investigation of transfected cells. Seven specific anti-E2 humAbs, which react with the envelope protein 2 of genotype 1a and 1b isolates, were characterized.
Keywords
Animals Antibodies, Monoclonal/*immunology/isolation & purification Cell Line Cricetinae Enzyme-Linked Immunosorbent Assay Hepacivirus/*immunology Hepatitis C Antibodies/*immunology/isolation & purification Humans Immunoblotting Tumor Cells, Cultured Viral Envelope Proteins/*immunology
Pubmed
Create date
25/01/2008 16:05
Last modification date
20/08/2019 12:28
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