Tetrameric ring formation of Epstein-Barr virus polymerase processivity factor is crucial for viral replication

Sanae Nakayama, Takayuki Murata, Yoshihiro Yasui, Kazutaka Murayama, Hiroki Isomura, Teru Kanda, Tatsuya Tsurumi

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14 Citations (Scopus)


The Epstein-Barr virus BMRF1 DNA polymerase processivity factor, which is essential for viral genome replication, exists mainly as a C-shaped head-to-head homodimer but partly forms a ring-shaped tetramer through tail-to-tail association. Based on its molecular structure, several BMRF1 mutant viruses were constructed to examine their influence on viral replication. The R256E virus, which has a severely impaired capacity for DNA binding and polymerase processivity, failed to form replication compartments, resulting in interference of viral replication, while the C95E mutation, which impairs head-to-head contact in vitro, unexpectedly hardly affected the viral replication. Also, surprisingly, replication of the C206E virus, which is expected to have impairment of tail-to-tail contact, was severely restricted, although the mutant protein possesses the same in vitro biochemical activities as the wild type. Since the tail-to-tail contact surface is smaller than that of the head-to-head contact area, its contribution to ring formation might be essential for viral replication.

Original languageEnglish
Pages (from-to)12589-12598
Number of pages10
JournalJournal of Virology
Issue number24
Publication statusPublished - 12-2010
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Immunology
  • Insect Science
  • Virology


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