PMID- 24760738
OWN - NLM
STAT- MEDLINE
DCOM- 20150126
LR  - 20140604
IS  - 1096-9071 (Electronic)
IS  - 0146-6615 (Linking)
VI  - 86
IP  - 8
DP  - 2014 Aug
TI  - High expression of beta2-glycoprotein I is associated significantly with the 
      earliest stages of hepatitis B virus infection.
PG  - 1296-306
LID - 10.1002/jmv.23961 [doi]
AB  - Human beta2-glycoprotein I (beta2-GPI) binds to recombinant hepatitis B surface 
      antigen (rHBsAg) and can bind specifically to annexin II, which is located on the 
      cell membrane of human hepatoma SMMC-7721 cells. Viral envelope proteins are 
      essential for mediating cellular entry. The aim of this study was to investigate 
      the role of beta2-GPI in the early stages of hepatitis B virus (HBV) infection. 
      Western blot and qRT-PCR analyses revealed that beta2-GPI expression was 
      upregulated in HepG2.2.15 cells at both the mRNA and protein level and was almost 
      non-existent in 293T and CHO cells. Furthermore, annexin II was expressed at 
      lower levels in HepG2.2.15 cells compared to L02, HepG2, and SMMC-7721 cells. 
      Additionally, ELISA analyses demonstrated that beta2-GPI enhanced the ability of 
      HBsAg to bind to cell surfaces, and there was differential adhesion to L02, 
      HepG2, HepG2.2.15, and 293T cells. Western blot and ELISA were then performed to 
      assess the effects of HBV and the HBsAg domain on beta2-GPI expression in 
      co-transfected 293T cells. This study revealed that HBV and the large HBV 
      envelope protein increased beta2-GPI expression. Further investigation indicated 
      that beta2-GPI colocalized with HBsAg in the cytosol of HepG2.2.15 cells, with 
      sodium taurocholate co-transporting polypeptide (NTCP) on the cell membrane in 
      NTCP-complemented HepG2 cells, and with annexin II in the cytosol of HepG2 and 
      HepG2.2.15 cells. These data suggest that high expression of beta2-GPI enhances 
      HBsAg binding to cell surfaces, thus contributing to virus particle transfer to 
      the NTCP receptor and interaction with annexin II for viral membrane fusion.
CI  - (c) 2014 Wiley Periodicals, Inc.
FAU - Liu, Ya-Ming
AU  - Liu YM
AD  - Department of Hepatology, First Hospital of Jilin University, Changchun, Jilin, 
      China.
FAU - Zhang, Wen-Yan
AU  - Zhang WY
FAU - Wang, Zhong-Feng
AU  - Wang ZF
FAU - Yan, Chao-Ying
AU  - Yan CY
FAU - Gao, Pu-Jun
AU  - Gao PJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20140424
PL  - United States
TA  - J Med Virol
JT  - Journal of medical virology
JID - 7705876
RN  - 0 (beta 2-Glycoprotein I)
SB  - IM
MH  - Blotting, Western
MH  - Cell Line
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Hepatitis B virus/*physiology
MH  - Hepatocytes/*physiology/*virology
MH  - *Host-Pathogen Interactions
MH  - Humans
MH  - Real-Time Polymerase Chain Reaction
MH  - *Virus Attachment
MH  - beta 2-Glycoprotein I/*biosynthesis
OTO - NOTNLM
OT  - annexin II
OT  - beta2-GPI
OT  - hepatitis B surface antigen
OT  - hepatitis B virus
OT  - hepatocyte
OT  - sodium taurocholate co-transporting polypeptide
EDAT- 2014/04/25 06:00
MHDA- 2015/01/27 06:00
CRDT- 2014/04/25 06:00
PHST- 2014/03/25 00:00 [accepted]
PHST- 2014/04/25 06:00 [entrez]
PHST- 2014/04/25 06:00 [pubmed]
PHST- 2015/01/27 06:00 [medline]
AID - 10.1002/jmv.23961 [doi]
PST - ppublish
SO  - J Med Virol. 2014 Aug;86(8):1296-306. doi: 10.1002/jmv.23961. Epub 2014 Apr 24.