Analysis of an ankyrin-like region in Epstein Barr Virus encoded (EBV) BZLF-1 (ZEBRA) protein: implications for interactions with NF-κB and p53
2011

Study of ZEBRA Protein in Epstein-Barr Virus

publication Evidence: moderate

Author Information

Author(s): Dreyfus David H, Liu Yang, Ghoda Lucy Y, Chang Joseph T

Primary Institution: Yale University

Hypothesis

The interaction of the ZEBRA protein with NF-κB and p53 may play a role in viral carcinogenesis.

Conclusion

The ZEBRA protein's ankyrin-like domain allows it to bind to NF-κB and p53, potentially influencing viral replication and carcinogenesis.

Supporting Evidence

  • The ZEBRA protein can bind to NF-κB and p53, which are crucial for immune response.
  • ZEBRA's interactions may lead to increased apoptosis in T lymphocytes.
  • An amino acid polymorphism in ZANK could alter ZEBRA's binding to p53.

Takeaway

The ZEBRA protein from the Epstein-Barr virus can interact with important proteins in our body, which might help the virus grow and cause cancer.

Methodology

The study involved randomization of the ZEBRA terminal amino acid sequence followed by statistical analysis and in silico modeling.

Limitations

The existing structure of ZANK is partial and solved in the absence of partner ligands.

Statistical Information

P-Value

p<0.05

Statistical Significance

p<0.05

Digital Object Identifier (DOI)

10.1186/1743-422X-8-422

Want to read the original?

Access the complete publication on the publisher's website

View Original Publication