scholarly journals Interaction between the cellular E3 ubiquitin ligase SIAH-1 and the viral immediate-early protein ICP0 enables efficient replication of Herpes Simplex Virus type 2 in vivo

PLoS ONE ◽  
2018 ◽  
Vol 13 (8) ◽  
pp. e0201880 ◽  
Author(s):  
Julia S. Czechowicz ◽  
Claus-Henning Nagel ◽  
Maike Voges ◽  
Michael Spohn ◽  
Martha M. Eibl ◽  
...  
2009 ◽  
Vol 84 (3) ◽  
pp. 1637-1640 ◽  
Author(s):  
Mark G. Delboy ◽  
Carlos R. Siekavizza-Robles ◽  
Anthony V. Nicola

ABSTRACT Herpes simplex virus (HSV) immediate-early (IE) protein ICP0 is a multifunctional regulator of HSV infection. ICP0 that is present in the tegument layer has not been well characterized. Protein compositions of wild-type and ICP0 null virions were similar, suggesting that the absence of ICP0 does not grossly impair virion assembly. ICP0 has a RING finger domain with E3 ubiquitin ligase activity that is necessary for IE functions. Virions with mutations in this domain contained greatly reduced levels of tegument ICP0, suggesting that the domain influences the incorporation of ICP0. Virion ICP0 was resistant to removal by detergent and salt and was associated with capsids, features common to inner tegument proteins.


Virology ◽  
1992 ◽  
Vol 190 (1) ◽  
pp. 256-268 ◽  
Author(s):  
Yukihiro Nishiyama ◽  
Yoshinari Yamada ◽  
Ryutaro Kurachi ◽  
Tohru Daikoku

1999 ◽  
Vol 42 (3) ◽  
pp. 219-226 ◽  
Author(s):  
Krystyn Z. Bourne ◽  
Nigel Bourne ◽  
Shirley F. Reising ◽  
Lawrence R. Stanberry

2001 ◽  
Vol 75 (11) ◽  
pp. 5357-5362 ◽  
Author(s):  
Jane Parkinson ◽  
Roger D. Everett

ABSTRACT Herpes simplex virus type 1 immediate early protein ICP0 influences virus infection by inducing the degradation of specific cellular proteins via a mechanism requiring its RING finger and the ubiquitin-proteasome pathway. Many RING finger proteins, by virtue of their RING finger domain, interact with E2 ubiquitin-conjugating enzymes and act as a component of an E3 ubiquitin ligase. We have recently shown that ICP0 induces the accumulation of colocalizing, conjugated ubiquitin, suggesting that ICP0 can act as or contribute to an E3 ubiquitin ligase. In this report we demonstrate that the ICP0-related RING finger proteins encoded by other alphaherpesviruses also induce colocalizing, conjugated ubiquitin, thereby suggesting that they act by similar biochemical mechanisms.


2010 ◽  
Vol 86 (1) ◽  
pp. A65 ◽  
Author(s):  
Debra Quenelle ◽  
Robert Glazer ◽  
Aquilur Rahman ◽  
Deborah Collins ◽  
Terri Rice

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