Literature DB >> 3029301

DNA-binding proteins of herpes simplex virus type 1-infected BHK cell nuclear matrices.

M F Pinard, R Simard, V Bibor-Hardy.   

Abstract

The nuclear matrix is involved in the replicative cycle of herpes simplex virus type 1 (HSV-1) and in at least some cases viral DNA has been shown to be closely associated with this structure. In this communication, we report the presence of five DNA-binding proteins in the nuclear matrix of HSV-1-infected BHK cells. These proteins (p114, p89, p77, p37 and p29) were detected by probing with 32P-labelled HSV DNA after Western blotting of nuclear matrix proteins. Three were identified as virion components: p89 as VP12, p77 as VP13 and p37 as the capsid protein VP22a. These polypeptides were detected in cells and nuclei and found to be associated with the nuclear matrix late during the lytic cycle, long after the onset of viral DNA replication. The nuclear matrix-binding capacity of VP22a depended on viral DNA replication, since after DNA polymerase inhibition it was still synthesized and transported into the nucleus but was no longer associated with the nuclear matrix. After inhibition of viral DNA synthesis, VP13 was no longer found in cells, nuclei or nuclear matrices. These results suggest a possible involvement in anchoring viral progeny DNA to the nuclear matrix.

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Year:  1987        PMID: 3029301     DOI: 10.1099/0022-1317-68-3-727

Source DB:  PubMed          Journal:  J Gen Virol        ISSN: 0022-1317            Impact factor:   3.891


  14 in total

1.  Cytoplasm-to-nucleus translocation of a herpesvirus tegument protein during cell division.

Authors:  G Elliott; P O'Hare
Journal:  J Virol       Date:  2000-03       Impact factor: 5.103

2.  Nuclear localization and shuttling of herpes simplex virus tegument protein VP13/14.

Authors:  M Donnelly; G Elliott
Journal:  J Virol       Date:  2001-03       Impact factor: 5.103

3.  The pseudorabies virus VP22 homologue (UL49) is dispensable for virus growth in vitro and has no effect on virulence and neuronal spread in rodents.

Authors:  T del Rio; H C Werner; L W Enquist
Journal:  J Virol       Date:  2002-01       Impact factor: 5.103

4.  The product of the UL31 gene of herpes simplex virus 1 is a nuclear phosphoprotein which partitions with the nuclear matrix.

Authors:  Y E Chang; B Roizman
Journal:  J Virol       Date:  1993-11       Impact factor: 5.103

5.  Nuclear localization of Semliki Forest virus-specific nonstructural protein nsP2.

Authors:  J Peränen; M Rikkonen; P Liljeström; L Kääriäinen
Journal:  J Virol       Date:  1990-05       Impact factor: 5.103

6.  Characterization of a UL49-null mutant: VP22 of herpes simplex virus type 1 facilitates viral spread in cultured cells and the mouse cornea.

Authors:  Carol Duffy; Jennifer H Lavail; Andrew N Tauscher; Elizabeth G Wills; John A Blaho; Joel D Baines
Journal:  J Virol       Date:  2006-09       Impact factor: 5.103

7.  VP16 interacts via its activation domain with VP22, a tegument protein of herpes simplex virus, and is relocated to a novel macromolecular assembly in coexpressing cells.

Authors:  G Elliott; G Mouzakitis; P O'Hare
Journal:  J Virol       Date:  1995-12       Impact factor: 5.103

8.  Temporal regulation of herpes simplex virus type 2 VP22 expression and phosphorylation.

Authors:  B J Geiss; J E Tavis; L M Metzger; D A Leib; L A Morrison
Journal:  J Virol       Date:  2001-11       Impact factor: 5.103

9.  Herpes simplex virus type 1 UL46 and UL47 deletion mutants lack VP11 and VP12 or VP13 and VP14, respectively, and exhibit altered viral thymidine kinase expression.

Authors:  Y Zhang; J L McKnight
Journal:  J Virol       Date:  1993-03       Impact factor: 5.103

10.  The terminal regions of adenovirus and minute virus of mice DNAs are preferentially associated with the nuclear matrix in infected cells.

Authors:  J W Bodnar; P I Hanson; M Polvino-Bodnar; W Zempsky; D C Ward
Journal:  J Virol       Date:  1989-10       Impact factor: 5.103

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