Abstract
Murine gammaherpesvirus 68 (MHV-68), Kaposi's sarcoma-associated herpesvirus (HHV-8), and Epsiein-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 gammaherpesvinises, 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.
| Original language | English |
|---|---|
| Pages (from-to) | 3217-3222 |
| Number of pages | 6 |
| Journal | Journal of Virology |
| Volume | 79 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 2005 Mar 1 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Immunology
Cite this
Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 RTA reactivates murine gammaherpesvirus 68 from latency. / Rickabaugh, Tammy M.; Brown, Helen J.; Wu, Ting Ting; Song, Moon Jung; Hwang, Seungmin; Deng, Hongyu; Mitsouras, Katherine; Sun, Ren.
In: Journal of Virology, Vol. 79, No. 5, 01.03.2005, p. 3217-3222.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 RTA reactivates murine gammaherpesvirus 68 from latency
AU - Rickabaugh, Tammy M.
AU - Brown, Helen J.
AU - Wu, Ting Ting
AU - Song, Moon Jung
AU - Hwang, Seungmin
AU - Deng, Hongyu
AU - Mitsouras, Katherine
AU - Sun, Ren
PY - 2005/3/1
Y1 - 2005/3/1
N2 - Murine gammaherpesvirus 68 (MHV-68), Kaposi's sarcoma-associated herpesvirus (HHV-8), and Epsiein-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 gammaherpesvinises, 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.
AB - Murine gammaherpesvirus 68 (MHV-68), Kaposi's sarcoma-associated herpesvirus (HHV-8), and Epsiein-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 gammaherpesvinises, 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.
UR - http://www.scopus.com/inward/record.url?scp=13844324384&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=13844324384&partnerID=8YFLogxK
U2 - 10.1128/JVI.79.5.3217-3222.2005
DO - 10.1128/JVI.79.5.3217-3222.2005
M3 - Article
C2 - 15709045
AN - SCOPUS:13844324384
VL - 79
SP - 3217
EP - 3222
JO - Journal of Virology
JF - Journal of Virology
SN - 0022-538X
IS - 5
ER -