Functional Roles of Immediate Early Proteins Encoded by the Human Cytomegalovirus UL36-38, UL115-119, TRS1/IRS1 and US3 Loci

Intervirology ◽  
1996 ◽  
Vol 39 (5-6) ◽  
pp. 350-360 ◽  
Author(s):  
Anamaris M. Colberg-Poley
Keyword(s):  
Human Cytomegalovirus ◽  
Immediate Early ◽  
Functional Roles ◽  
Early Proteins ◽  
Immediate Early Proteins

Human cytomegalovirus US3 and UL36-38 immediate-early proteins regulate gene expression.

1992 ◽  
Vol 66 (1) ◽  
pp. 95-105 ◽  
Author(s):  
A M Colberg-Poley ◽  
L D Santomenna ◽  
P P Harlow ◽  
P A Benfield ◽  
D J Tenney
Keyword(s):  
Gene Expression ◽  
Human Cytomegalovirus ◽  
Immediate Early ◽  
Regulate Gene Expression ◽  
Early Proteins ◽  
Immediate Early Proteins ◽  
Regulate Gene

scholarly journals Effects of Human Cytomegalovirus Immediate-Early Proteins on p53-mediated Apoptosis in Coronary Artery Smooth Muscle Cells

Circulation ◽  
1999 ◽  
Vol 99 (13) ◽  
pp. 1656-1659 ◽  
Author(s):  
Koichi Tanaka ◽  
Jian-Ping Zou ◽  
Kazuyo Takeda ◽  
Victor J. Ferrans ◽  
Gordon R. Sandford ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Coronary Artery ◽  
Smooth Muscle Cells ◽  
Human Cytomegalovirus ◽  
Muscle Cells ◽  
Immediate Early ◽  
Early Proteins ◽  
Immediate Early Proteins

scholarly journals The Use of Recombinant Baculoviruses for Sustained Expression of Human Cytomegalovirus Immediate Early Proteins in Fibroblasts

Virology ◽  
2001 ◽  
Vol 284 (2) ◽  
pp. 297-307 ◽  
Author(s):  
Roopashree S. Dwarakanath ◽  
Charles L. Clark ◽  
Anita K. McElroy ◽  
Deborah H. Spector
Keyword(s):  
Human Cytomegalovirus ◽  
Immediate Early ◽  
Recombinant Baculoviruses ◽  
Early Proteins ◽  
Immediate Early Proteins

scholarly journals Human cytomegalovirus immediate early proteins promote degradation of connexin 43 and disrupt gap junction communication: implications for a role in gliomagenesis

2013 ◽  
Vol 35 (1) ◽  
pp. 145-154 ◽  
Author(s):  
Zahidul Khan ◽  
Koon-Chu Yaiw ◽  
Vanessa Wilhelmi ◽  
Hoyin Lam ◽  
Afsar Rahbar ◽  
...  
Keyword(s):  
Gap Junction ◽  
Human Cytomegalovirus ◽  
Connexin 43 ◽  
Immediate Early ◽  
Gap Junction Communication ◽  
Early Proteins ◽  
Immediate Early Proteins

scholarly journals Analysis of Human Cytomegalovirus-Encoded SUMO Targets and Temporal Regulation of SUMOylation of the Immediate-Early Proteins IE1 and IE2 during Infection

PLoS ONE ◽  
2014 ◽  
Vol 9 (7) ◽  
pp. e103308 ◽  
Author(s):  
Eui Tae Kim ◽  
Young-Eui Kim ◽  
Ye Ji Kim ◽  
Myoung Kyu Lee ◽  
Gary S. Hayward ◽  
...  
Keyword(s):  
Human Cytomegalovirus ◽  
Immediate Early ◽  
Temporal Regulation ◽  
Early Proteins ◽  
Immediate Early Proteins

Human cytomegalovirus immediate early proteins and cell growth control

Gene ◽  
2002 ◽  
Vol 290 (1-2) ◽  
pp. 19-34 ◽  
Author(s):  
Jonathan P Castillo ◽  
Timothy F Kowalik
Keyword(s):  
Cell Growth ◽  
Human Cytomegalovirus ◽  
Growth Control ◽  
Immediate Early ◽  
Early Proteins ◽  
Immediate Early Proteins ◽  
Cell Growth Control

scholarly journals The ND10 Component Promyelocytic Leukemia Protein Acts as an E3 Ligase for SUMOylation of the Major Immediate Early Protein IE1 of Human Cytomegalovirus

2017 ◽  
Vol 91 (10) ◽  
Author(s):  
Nina Reuter ◽  
Eva-Maria Schilling ◽  
Myriam Scherer ◽  
Regina Müller ◽  
Thomas Stamminger
Keyword(s):  
Immune Response ◽  
Human Cytomegalovirus ◽  
E3 Ligase ◽  
Promyelocytic Leukemia ◽  
Immediate Early ◽  
Promyelocytic Leukemia Protein ◽  
Sumo Modification ◽  
Early Proteins ◽  
Immediate Early Proteins ◽  
Sumo E3 Ligase

ABSTRACT Previous studies identified the nuclear domain 10 (ND10) components promyelocytic leukemia protein (PML), hDaxx, and Sp100 as factors of an intrinsic immune response against human cytomegalovirus (HCMV). This antiviral function of ND10, however, is antagonized by viral effector proteins like IE1p72, which induces dispersal of ND10. Furthermore, we have shown that both major immediate early proteins of HCMV, IE1p72 and IE2p86, transiently colocalize with ND10 subnuclear structures and undergo modification by the covalent attachment of SUMO. Since recent reports indicate that PML acts as a SUMO E3 ligase, we asked whether the SUMOylation of IE1p72 and IE2p86 is regulated by PML. To address this, PML-depleted fibroblasts, as well as cells overexpressing individual PML isoforms, were infected with HCMV. Western blot experiments revealed a clear correlation between the degree of IE1p72 SUMO conjugation and the abundance of PML. On the other hand, the SUMOylation of IE2p86 was not affected by PML. By performing in vitro SUMOylation assays, we were able to provide direct evidence that IE1p72 is a substrate for PML-mediated SUMOylation. Interestingly, disruption of the RING finger domain of PML, which is proposed to confer SUMO E3 ligase activity, abolished PML-induced SUMOylation of IE1p72. In contrast, IE1p72 was still efficiently SUMO modified by a SUMOylation-defective PML mutant, indicating that intact ND10 bodies are not necessary for this effect. Thus, this is the first report that the E3 ligase PML is capable of stimulating the SUMOylation of a viral protein which is supposed to serve as a cellular mechanism to compromise specific functions of IE1p72. IMPORTANCE The major immediate early proteins of human cytomegalovirus, termed IE1p72 and IE2p86, have previously been shown to undergo posttranslational modification by covalent coupling to SUMO moieties at specific lysine residues. However, the enzymatic activities that are responsible for this modification have not been identified. Here, we demonstrate that the PML protein, which mediates an intrinsic immune response against HCMV, specifically serves as an E3 ligase for SUMO modification of IE1p72. Since SUMO modification of IE1p72 has previously been shown to interfere with STAT factor binding, thus compromising the interferon-antagonistic function of this viral effector protein, our finding highlights an additional mechanism through which PML is able to restrict viral infections.

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