Premium
Hepatitis B spliced protein (HBSP) generated by a spliced hepatitis B virus RNA participates in abnormality of fibrin formation and functions by binding to fibrinogen γ chain
Author(s) -
Chen JinYan,
Chen WanNan,
Liu LingLing,
Lin WanSong,
Jiao BoYan,
Wu YunLi,
Lin JianYin,
Lin Xu
Publication year - 2010
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/jmv.21918
Subject(s) - hepatitis b virus , fibrinogen , virology , immunoprecipitation , biology , microbiology and biotechnology , hepatitis b , virus , gene , biochemistry
Hepatitis B spliced protein (HBSP) encoded by a 2.2 kb singly spliced hepatitis B virus (HBV) pre‐genomic RNA (spliced between positions 2447 and 489 nt) is involved in the pathogenesis of HBV infection, whereas the exact mechanism is far from being fully elucidated. In this study, a yeast two‐hybrid system using HBSP as bait was employed to screen binding partners for HBSP from a human liver cDNA library. The interaction between HBSP and fibrinogen γ chain (FGG) was further confirmed in vitro using a GST pull‐down assay and confirmed in vivo using a mammalian two‐hybrid assay and co‐immunoprecipitation. It was identified that this interaction is mediated by the N terminal 47 amino acid residues of HBSP. HBSP could inhibit fibrin polymerization, factor XIIIa‐mediated fibrin cross‐linking, adhesion of platelets to fibrinogen and ADP‐stimulated platelet aggregation. However, the interaction‐mediating fragment 1–47 of HBSP is not sufficient for the inhibitory activity on fibrinogen function. The findings suggested that HBSP may participate in the hemostatic abnormality in patients with HBV‐related liver diseases. J. Med. Virol. 82:2019–2026, 2010. © 2010 Wiley‐Liss, Inc.