Open AccessKaposi's Sarcoma-Associated Herpesvirus/Human Herpesvirus 8 RTA Reactivates Murine Gammaherpesvirus 68 from Latency
Author(s) -
Tammy M. Rickabaugh,
Helen Brown,
Ting Wu,
Mee Hyun Song,
Seungmin Hwang,
Hongyu Deng,
Katherine Mitsouras,
Ren Sun
Publication year - 2005
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.79.5.3217-3222.2005
Subject(s) - biology , human herpesvirus , virology , latency (audio) , human herpesvirus 6 , gammaherpesvirinae , herpesviridae infections , herpesviridae , kaposi's sarcoma associated herpesvirus , simplexvirus , virus latency , herpesvirus hominis , immunology , virus , viral disease , viral replication , electrical engineering , engineering
Murine gammaherpesvirus 68 (MHV-68), Kaposi's sarcoma-associated herpesvirus (HHV-8), and Epstein-Barr virus (EBV) are all members of the gammaherpesvirus family, characterized by their ability to establish latency in lymphocytes. The RTA protein, conserved in all gammaherpesviruses, is known to play a critical role in reactivation from latency. Here we report that HHV-8 RTA, not EBV RTA, was able to induce MHV-68 lytic viral proteins and DNA replication and processing and produce viable MHV-68 virions from latently infected cells at levels similar to those for MHV-68 RTA. HHV-8 RTA was also able to activate two MHV-68 lytic promoters, whereas EBV RTA was not. In order to define the domains of RTA responsible for their functional differences in viral promoter activation and initiation of the MHV-68 lytic cycle, chimeric RTA proteins were constructed by exchanging the N-terminal and C-terminal domains of the RTA proteins. Our data suggest that the species specificity of MHV-68 RTA resides in the N-terminal DNA binding domain.