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EBV membrane receptor (CR2) is phosphorylated by protein kinase C (PKC) in the early stages of virus entry into lymphoblastoid cells line (Raji).

Authors :
Aquino A
Lisi A
Pozzi D
Ravagnan G
Grimaldi S
Source :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1993 Oct 29; Vol. 196 (2), pp. 794-802.
Publication Year :
1993

Abstract

Labeling the EBV membrane with octadecylrhodamine-b-chloride (R18) we were able to monitor spectrofluorometrically the early events of EBV fusion, under conditions in which we could affect PKC activity. Binding of EBV to Raji cells induces PKC translocation from the cytosol to the plasma membrane and 32P incorporation into its cellular receptor CR2. CR2 phosphorylation is completely inhibited when cells are preincubated with the PKC inhibitor calphostin c. This treatment also generates a strong inhibition of EBV fusion. Taken together this result suggests a key role of CR2 phosphorylation in the EBV entry into Raji cells.

Details

Language :
English
ISSN :
0006-291X
Volume :
196
Issue :
2
Database :
MEDLINE
Journal :
Biochemical and biophysical research communications
Publication Type :
Academic Journal
Accession number :
7694579
Full Text :
https://doi.org/10.1006/bbrc.1993.2319