Epstein-Barr viruses that express a CD21 antibody provide evidence that gp350's functions extend beyond B-cell surface binding.

ABSTRACT: The gp350 glycoprotein encoded by BLLF1 is crucial for efficient Epstein-Barr virus (EBV) infection of resting B cells. Gp350 binds to CD21, but whether this interaction sums up its functions remains unknown. We generated gp350-null EBVs that display CD19-, CD21-, or CD22-specific antibodies at their surface (designated as DeltaBLLF1-Ab). Gp350-complemented (DeltaBLLF1-C) and DeltaBLLF1-Ab were found to bind equally well to B cells. Surprisingly, DeltaBLLF1 binding was reduced only 1.7-fold relative to its complemented counterparts. Furthermore, B cells exposed to DeltaBLLF1-Ab or DeltaBLLF1 viruses presented structural antigens with comparable efficiency and achieved 25 to 80% of the T-cell activation elicited by DeltaBLLF1-C. These findings show that the gp350-CD21 interaction pair plays

SUBMITTER: Busse C 

PROVIDER: S-EPMC2798361 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature