Physical and functional interaction between the HCMV IE2 protein and the Wilms' tumor suppressor WT1

Jong Mook Kim, Youngtae Hong, Kentaro Senba, Sunyoung Kim

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Human cytomegalovirus (HCMV) is a major renal pathogen in congenitally infected infants and renal allograft recipients. It has been shown that human kidney cells of glomerular, tubular, and vascular origin were all infected by HCMV in vitro. It has previously been demonstrated that the IE2 protein of HCMV directly associates with the zinc finger domain of Egr-1. The zinc finger region of WT1 is a sequence-specific DNA-binding domain which also recognizes the consensus DNA binding site (5'-CGCCCCCGC-3') of Egr-1, thus suggesting a possible interaction between WT1 and IE2. Here we demonstrate that HCMV IE2 binds to the C-terminal region of WT1 containing zinc finger domain in vivo as well as in vitro and that WT1 can inhibit IES-driven transactivation of the responsive promoter. Our results suggest that WT1 may be able to regulate the functional activity of HCMV IE2. Furthermore, these data may provide new insights into the possible involvement of HCMV in WT1-related pathogeneses. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)59-63
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume267
Issue number1
DOIs
Publication statusPublished - 2000 Jan 7
Externally publishedYes

Fingerprint

Wilms Tumor
Zinc
Tumors
Cytomegalovirus
Zinc Fingers
DNA
Pathogens
Kidney
Allografts
Binding Sites
Human Activities
Transcriptional Activation
Blood Vessels
Cytomegalovirus IE2 protein
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Physical and functional interaction between the HCMV IE2 protein and the Wilms' tumor suppressor WT1. / Kim, Jong Mook; Hong, Youngtae; Senba, Kentaro; Kim, Sunyoung.

In: Biochemical and Biophysical Research Communications, Vol. 267, No. 1, 07.01.2000, p. 59-63.

Research output: Contribution to journalArticle

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