Human hepatitis B virus X protein augments the DNA binding of nuclear factor for IL-6 through its basic-leucine zipper domain.

Abstract:

:The X gene product of human hepatitis B virus, HBx, transactivates the expression of viral and cellular genes through a wide variety of cis elements, including the nuclear factor for IL-6 (NF-IL6) binding sites, although HBx does not appear to bind DNA directly. We previously reported that HBx transactivated the interleukin 8 promoter through NF-kappaB binding site and C/EBP-like binding site (NF-IL6 binding site). In this study, the interactions were examined between NF-IL6 and HBx using recombinant proteins. In a DNA-protein binding assay, the formation of a specific complex between NF-IL6 and a DNA probe harboring an NF-IL6 binding site was increased by the addition of either the full or the C-terminal 104 amino acids of HBx. A direct protein-protein binding assay (far-Western blot) revealed the direct interaction between the C-terminal 104 amino acids of HBx and the basic region-leucine zipper domain of NF-IL6. These results indicate that HBx alters the DNA-binding affinity of NF-IL6 through the direct interaction between the C-terminal domain of HBx and the basic region-leucine zipper domain of NF-IL6.

journal_name

J Med Virol

authors

Ohno H,Kaneko S,Lin Y,Kobayashi K,Murakami S

doi

10.1002/(sici)1096-9071(199905)58:1<11::aid-jmv2>3

keywords:

subject

Has Abstract

pub_date

1999-05-01 00:00:00

pages

11-8

issue

1

eissn

0146-6615

issn

1096-9071

pii

10.1002/(SICI)1096-9071(199905)58:1<11::AID-JMV2>3

journal_volume

58

pub_type

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