Author(s): Ge J, Huang Y, Hu X, Zhong J
Abstract Share this page
Abstract A short peptide motif from gp350/220 of Epstein-Barr virus, EDPGFFNVEI, which was known to bind to CD21, a surface protein on B-lymphocyte, was inserted into the baculovirus surface protein gp64. The recombinant virus carrying the hybrid gp64/gp350 gene, vAc-gp350EGFP, was obtained, and the expression of gp64/gp350 protein was confirmed with immunoblot using anti-gp350 antibody. When compared with a control virus with wild type gp64, vAc-gp350EGFP showed increased transduction efficiency in B cell lines Raji, HR1, B95-8, BJAB, and DG75, regardless of their being EBV-positive or EBV-negative. No such increase was seen in non-B cell lines HEK293 and HeLa. When Raji cells were transduced with increased amount of vAc-gp350EGFP, transduction became saturated when the multiplicity of infection was higher than 20pfu/cell. The transduction of Raji cells by vAc-gp350EGFP was dose-dependently inhibited by pre-treatment of cells with anti-CD21 antibody. These results showed that vAc-gp350EGFP entered B cells by interacting with CD21.
This article was published in J Biotechnol
and referenced in Journal of Molecular and Genetic Medicine