Involvement of Crm 1 in hepatitis B virus X protein-induced aberrant centriole replication and abnormal mitotic spindles

Authors:
Forgues M, Difilippantonio MJ, Linke SP, Ried T, Nagashima K, Feden, J, Valerie K, Fukasawa K and Wang XW
In:
Source: Mol Cell Biol
Publication Date: (2003)
Issue: 23(15): 5282-5292
Experiment
Hepatitis B Virus (HBV) includes an X gene (HBx gene) necessary for establishment of viral infection that plays a critical role in liver carcinogenesis. Because centrosome abnormalities are associated with genomic instability in most human cancer cells, the authors examined the effect of HBx on centrosomes. HepG2 cells (hepatoma cell line) were transfected with an expression vector encoding either the wild-type HBV (pHBV) genome or the HBV genome without HBx expression due to a point mutation at codon 7 of HBx (pHBV(-HBx)). pHBV replicated efficiently in HepG2 cells whereas pHBV(-HBx) did not. There was a significant increase in mitototic HepG2 cells with supernumerary centrosomes in pHBV, but not in pHBV(-HBx) transfected cells. These data indicate that induction of supernumerary centrosomes in HepG2 cells by HBV depends on a physiological expression of HBx during HBV replication.
Abstract
Hepatitis B virus (HBV) includes an X gene (HBx gene) that plays a critical role in liver carcinogenesis. Because centrosome abnormalities are associated with genomic instability in most human cancer cells, we examined the effect of HBx on centrosomes. We found that HBx induced supernumerary centrosomes and multipolar spindles. This effect was independent of mutations in the p21 gene. Furthermore, the ability of HBV to induce supernumerary centrosomes was dependent on the presence of physiological HBx expression. We recently showed that HBx induces cytoplasmic sequestration of Crm1, a nuclear export receptor that binds to Ran GTPase, thereby inducing nuclear localization of NF-kappaB. Consistently, supernumerary centrosomes were observed in cells treated with a Crm1-specific inhibitor but not with an HBx mutant that lacked the ability to sequester Crm1 in the cytoplasm. Moreover, a fraction of Crm1 was found to be localized at the centrosomes. Immunocytochemical and ultrastructural examination of these supernumerary centrosomes revealed that inactivation of Crm1 was associated with abnormal centrioles. The presence of more than two centrosomes led to an increased frequency of defective mitoses and chromosome transmission errors. Based on this evidence, we suggest that Crm1 is actively involved in maintaining centrosome integrity and that HBx disrupts this process by inactivating Crm1 and thus contributes to HBV-mediated carcinogenesis.