![]() |
CiteULike | ![]() |
pauldobson's CiteULike | ![]() |
![]() |
|
![]() |
Register | ![]() |
Log in | ![]() |
EpsteinâBarr virus and virus human protein interaction mapsby: Michael A. Calderwood, Kavitha Venkatesan, Li Xing, Michael R. Chase, Alexei Vazquez, Amy M. Holthaus, Alexandra E. Ewence, Ning Li, Tomoko Hirozane-Kishikawa, David E. Hill, Marc Vidal, Elliott Kieff, Eric Johannsen
Proceedings of the National Academy of Sciences, Vol. 104, No. 18. (1 May 2007), pp. 7606-7611.
|
Reviews
[Write a review of this article]
Find related articles from these CiteULike users
Find related articles with these CiteULike tags
Posting History
Abstract10.1073/pnas.0702332104 A comprehensive mapping of interactions among EpsteinâBarr virus (EBV) proteins and interactions of EBV proteins with human proteins should provide specific hypotheses and a broad perspective on EBV strategies for replication and persistence. Interactions of EBV proteins with each other and with human proteins were assessed by using a stringent high-throughput yeast two-hybrid system. Overall, 43 interactions between EBV proteins and 173 interactions between EBV and human proteins were identified. EBVâEBV and EBVâhuman protein interaction, or âinteractomeâ maps provided a framework for hypotheses of protein function. For example, LF2, an EBV protein of unknown function interacted with the EBV immediate early R transactivator (Rta) and was found to inhibit Rta transactivation. From a broader perspective, EBV genes can be divided into two evolutionary classes, âcoreâ genes, which are conserved across all herpesviruses and subfamily specific, or ânoncoreâ genes. Our EBVâEBV interactome map is enriched for interactions among proteins in the same evolutionary class. Furthermore, human proteins targeted by EBV proteins were enriched for highly connected or âhubâ proteins and for proteins with relatively short paths to all other proteins in the human interactome network. Targeting of hubs might be an efficient mechanism for EBV reorganization of cellular processes.
BibTeX record
RIS record