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Autoantigenic proteins that bind recombinogenic sequences in Epstein-Barr virus and cellular DNA
1Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520-8064.
Summary
Researchers found cellular proteins that bind to Epstein-Barr virus (EBV) DNA, influencing viral genome alterations. This discovery sheds light on EBV DNA rearrangements and their role in viral biology.
Area of Science:
- Molecular Biology
- Virology
- Genetics
Background:
- Epstein-Barr virus (EBV) DNA undergoes significant rearrangements, crucial for its biology.
- The mechanisms driving EBV DNA alterations, particularly involving cellular components, remain incompletely understood.
Purpose of the Study:
- To identify cellular proteins interacting with EBV DNA.
- To elucidate the role of these interactions in viral genome modifications and recombination.
Main Methods:
- Identification of conserved autoantigenic cellular proteins.
- Analysis of protein binding to G-rich sequence motifs in EBV DNA.
- Investigation of binding sites in EBV terminal repeats and EBNA2 deletion regions.
Main Results:
- Discovered a cellular binding activity, termed TRBP, that recognizes G-rich motifs in recombinogenic EBV DNA regions.
- TRBP binds to EBV terminal repeats and sequences involved in EBNA2 deletion.
- TRBP also binds to repetitive cellular DNA, including VNTR and immunoglobulin heavy-chain class switch regions.
Conclusions:
- EBV likely exploits cellular DNA recombination systems for viral genome alterations.
- TRBP is implicated in mediating various types of EBV DNA rearrangements.
- These findings offer insights into the mechanisms underlying EBV DNA alterations.
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