Literature DB >> 11369891

Epstein-Barr virus-encoded protein kinase BGLF4 mediates hyperphosphorylation of cellular elongation factor 1delta (EF-1delta): EF-1delta is universally modified by conserved protein kinases of herpesviruses in mammalian cells.

Kentaro Kato1,2, Yasushi Kawaguchi2, Michiko Tanaka2, Mie Igarashi2, Akihiko Yokoyama2, Go Matsuda2, Mikiko Kanamori2, Kaori Nakajima2, Yorihiro Nishimura1, Masayuki Shimojima1, Hang T T Phung1, Eiji Takahashi1, Kanji Hirai2.   

Abstract

Translation elongation factor 1delta (EF-1delta) is hyperphosphorylated in various mammalian cells infected with alpha-, beta- and gammaherpesviruses and EF-1delta modification is mediated by viral protein kinases, including UL13 of herpes simplex virus type 1 and UL97 of human cytomegalovirus. In this study, the following is reported. (i) BGLF4 encoded by the prototype gammaherpesvirus Epstein-Barr virus was purified as a fusion protein that was labelled with [gamma-(32)P]ATP and labelling was eliminated by phosphatase. (ii) The ratio of the hyperphosphorylated form of human EF-1delta was increased both in Sf9 cells after infection with baculoviruses expressing GST-BGLF4 fusion proteins and in COS-7 cells after transfection with a BGLF4 expression plasmid. These results indicate that purified BGLF4 possesses protein kinase activity and mediates EF-1delta hyperphosphorylation. These data also support the hypothesis that the protein kinases that are conserved by herpesviruses universally mediate EF-1delta modification in mammalian cells.

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Year:  2001        PMID: 11369891     DOI: 10.1099/0022-1317-82-6-1457

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


  35 in total

1.  Phosphorylation of the Epstein-Barr virus (EBV) DNA polymerase processivity factor EA-D by the EBV-encoded protein kinase and effects of the L-riboside benzimidazole 1263W94.

Authors:  Edward Gershburg; Joseph S Pagano
Journal:  J Virol       Date:  2002-02       Impact factor: 5.103

Review 2.  Role of ICP0 in the strategy of conquest of the host cell by herpes simplex virus 1.

Authors:  Ryan Hagglund; Bernard Roizman
Journal:  J Virol       Date:  2004-03       Impact factor: 5.103

3.  Epstein-Barr virus protein kinase BGLF4 targets the nucleus through interaction with nucleoporins.

Authors:  Chou-Wei Chang; Chung-Pei Lee; Yu-Hao Huang; Pei-Wen Yang; Jiin-Tarng Wang; Mei-Ru Chen
Journal:  J Virol       Date:  2012-05-23       Impact factor: 5.103

Review 4.  Viral serine/threonine protein kinases.

Authors:  Thary Jacob; Céline Van den Broeke; Herman W Favoreel
Journal:  J Virol       Date:  2010-11-17       Impact factor: 5.103

5.  Hyperphosphorylation of EBNA2 by Epstein-Barr virus protein kinase suppresses transactivation of the LMP1 promoter.

Authors:  Wei Yue; Edward Gershburg; Joseph S Pagano
Journal:  J Virol       Date:  2005-05       Impact factor: 5.103

6.  Identification of proteins phosphorylated directly by the Us3 protein kinase encoded by herpes simplex virus 1.

Authors:  Akihisa Kato; Mayuko Yamamoto; Takashi Ohno; Hiroshi Kodaira; Yukihiro Nishiyama; Yasushi Kawaguchi
Journal:  J Virol       Date:  2005-07       Impact factor: 5.103

7.  Epstein-Barr virus-encoded protein kinase (BGLF4) is involved in production of infectious virus.

Authors:  Edward Gershburg; Salvatore Raffa; Maria Rosaria Torrisi; Joseph S Pagano
Journal:  J Virol       Date:  2007-03-14       Impact factor: 5.103

8.  Phosphorylation of p27Kip1 by Epstein-Barr virus protein kinase induces its degradation through SCFSkp2 ubiquitin ligase actions during viral lytic replication.

Authors:  Satoko Iwahori; Takayuki Murata; Ayumi Kudoh; Yoshitaka Sato; Sanae Nakayama; Hiroki Isomura; Teru Kanda; Tatsuya Tsurumi
Journal:  J Biol Chem       Date:  2009-05-18       Impact factor: 5.157

9.  Protein array identification of substrates of the Epstein-Barr virus protein kinase BGLF4.

Authors:  Jian Zhu; Gangling Liao; Liang Shan; Jun Zhang; Mei-Ru Chen; Gary S Hayward; S Diane Hayward; Prashant Desai; Heng Zhu
Journal:  J Virol       Date:  2009-02-25       Impact factor: 5.103

10.  Direct Substrate Identification with an Analog Sensitive (AS) Viral Cyclin-Dependent Kinase (v-Cdk).

Authors:  Angie C Umaña; Satoko Iwahori; Robert F Kalejta
Journal:  ACS Chem Biol       Date:  2017-12-19       Impact factor: 5.100

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