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Isolating the Epstein-Barr virus gp350/220 binding site on complement receptor type 2 (CR2/CD21)
Kendra A Young1, Xiaojiang S Chen, V Michael Holers
1Department of Medicine and Immunology, University of Colorado at Denver and Health Sciences Center, Aurora, Colorado 80045, USA.
The Journal of Biological Chemistry
|October 11, 2007
Summary
This study identifies the binding site of Epstein-Barr virus (EBV) glycoprotein gp350 on complement receptor type 2 (CR2/CD21). Positively charged residues on CR2 SCR1-2 are crucial for binding to the negatively charged gp350, confirming the interaction site.
Area of Science:
- Immunology
- Virology
- Structural Biology
Background:
- Complement receptor type 2 (CR2/CD21) mediates Epstein-Barr virus (EBV) attachment to B-lymphocytes via the viral glycoprotein gp350.
- The EBV gp350 structure and its CR2 binding site have been characterized.
Purpose of the Study:
- To identify the specific binding site of EBV gp350 on CR2/CD21.
- To investigate the role of CR2/CD21 N-terminal domains (SCR1-2) in gp350 interaction.
Main Methods:
- Site-directed mutagenesis of CR2/CD21.
- Expression of wild-type and mutant CR2/CD21 on K562 cells.
- Flow cytometry to measure gp350 binding to CR2-expressing cells.
- Utilized anti-CR2 monoclonal antibodies to probe binding sites.
Main Results:
- Mutations in CR2/CD21 SCR1-2 revealed a large binding surface for gp350.
- Positively charged residues (Arg, Lys) in CR2 SCR1-2 are critical for gp350 binding.
- Both SCR1 and SCR2 domains of CR2/CD21 contribute to gp350 interaction, with specific mutations and antibody epitopes confirming this.
Conclusions:
- The CR2/CD21 binding site on gp350 is characterized by a complementary charge distribution.
- Both N-terminal domains (SCR1 and SCR2) of CR2/CD21 are involved in the interaction with EBV gp350.
- This detailed mapping provides insights into EBV-host cell interactions and potential therapeutic targets.
