New insights into the role of the subnuclear structure ND10 for viral infection

被引：148

作者：

Tavalai, Nina ^{[1
]}

Stamminger, Thomas ^{[1
]}

机构：

[1] Univ Erlangen Nurnberg, Inst Clin & Mol Virol, D-91054 Erlangen, Germany

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2008年 / 1783卷 / 11期

关键词：

Nuclear domain 10; PML-bodies; PML; sp100; hDaxx; Antiviral defense; Intrinsic immunity; Interferon;

D O I：

10.1016/j.bbamcr.2008.08.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Nuclear domains 10 (ND10), alternatively termed PML nuclear bodies (PML-NBs) or PML oncogenic domains (PODs), have been discovered approximately 15 years ago as a nuclear substructure that is targeted by a variety of viruses belonging to different viral families. This review will summarize the most important structural and functional characteristics of ND10 and its major protein constituents followed by a discussion of the current view regarding the role of this subnuclear structure for various DNA and RNA viruses with an emphasis on herpesviruses. It is concluded that accumulating evidence argues for an involvement of ND10 in host antiviral defenses either via mediating an intrinsic immune response against specific viruses or via acting as a component of the cellular interferon pathway. (c) 2008 Elsevier B.V. All rights reserved.

引用

页码：2207 / 2221

页数：15

共 202 条

[21] Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies [J].

Blondel, D ;

Regad, T ;

Poisson, N ;

Pavie, B ;

Harper, F ;

Pandolfi, PP ;

de Thé, H ;

Chelbi-Alix, MK .

ONCOGENE, 2002, 21 (52) :7957-7970

[22] Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA [J].

Boisvert, FM ;

Hendzel, MJ ;

Bazett-Jones, DP .

JOURNAL OF CELL BIOLOGY, 2000, 148 (02) :283-292

[23] The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body [J].

Boisvert, FM ;

Kruhlak, MJ ;

Box, AK ;

Hendzel, MJ ;

Bazett-Jones, DP .

JOURNAL OF CELL BIOLOGY, 2001, 152 (05) :1099-1106

[24] Effects of promyelocytic leukemia protein on virus-host balance [J].

Bonilla, WV ;

Pinschewer, DD ;

Klenerman, P ;

Rousson, V ;

Gaboli, M ;

Pandolfi, PP ;

Zinkernagel, RM ;

Salvato, MS ;

Hengartner, H .

JOURNAL OF VIROLOGY, 2002, 76 (08) :3810-3818

[25] Pondering the promyelocytic leukemia protein (PML) puzzle: Possible functions for PML nuclear bodies [J].

Borden, KLB .

MOLECULAR AND CELLULAR BIOLOGY, 2002, 22 (15) :5259-5269

[26] An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm [J].

Borden, KLB ;

Dwyer, EJC ;

Salvato, MS .

JOURNAL OF VIROLOGY, 1998, 72 (01) :758-766

[27] The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation [J].

Bottomley, MJ ;

Collard, MW ;

Huggenvik, JI ;

Liu, ZH ;

Gibson, TJ ;

Sattler, M .

NATURE STRUCTURAL BIOLOGY, 2001, 8 (07) :626-633

[28] Herpes simplex virus type 1 immediate-early protein ICP0 and its isolated RING finger domain act as ubiquitin E3 ligases in vitro [J].

Boutell, C ;

Sadis, S ;

Everett, RD .

JOURNAL OF VIROLOGY, 2002, 76 (02) :841-850

[29] UL82 virion protein activates expression of immediate early viral genes in human cytomegalovirus-infected cells [J].

Bresnahan, WA ;

Shenk, TE .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (26) :14506-14511

[30] Interaction between the human cytomegalovirus UL82 gene product (pp71) and hDaxx regulates immediate-early gene expression and viral replication [J].

Cantrell, SR ;

Bresnahan, WA .

JOURNAL OF VIROLOGY, 2005, 79 (12) :7792-7802

← 1 2 3 4 5 6 7 8 9 10 →