Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
HBV infection of cell culture: evidence for multivalent and cooperative attachment
Autore:
Paran, N; Geiger, B; Shaul, Y;
Indirizzi:
Weizmann Inst Sci, Dept Mol Genet, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 enet, IL-76100 Rehovot, Israel Weizmann Inst Sci, Dept Mol Cell Biol, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 Biol, IL-76100 Rehovot, Israel
Titolo Testata:
EMBO JOURNAL
fascicolo: 16, volume: 20, anno: 2001,
pagine: 4443 - 4453
SICI:
0261-4189(20010815)20:16<4443:HIOCCE>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEPATITIS-B VIRUS; HUMAN HEPATOCYTES; DUCK HEPATOCYTES; PRE-S1 DOMAIN; PROTEIN; RECEPTOR; PARTICLES; BINDING; IDENTIFICATION; GP180;
Keywords:
endocytosis; HBsAg proteins; HBV infection; QLDPAF motif; virus attachment;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Shaul, Y Weizmann Inst Sci, Dept Mol Genet, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 76100 Rehovot, Israel
Citazione:
N. Paran et al., "HBV infection of cell culture: evidence for multivalent and cooperative attachment", EMBO J, 20(16), 2001, pp. 4443-4453

Abstract

Hepadnaviruses do not infect cultured cells, therefore our knowledge of the mechanism of the early stages of virus-cell interaction is rather poor. In this study, we show that dimethylsulfoxide (DMSO)-treated HepG2 hepatoblastoma cells are infected efficiently by serum-derived hepatitis B virus (HBV) as monitored by viral gene expression and replication markers. To measure virus attachment, a variety of HBV surface proteins (HBsAgs) were conjugated to polystyrene beads and their capacity to attach cells was visualized and quantified by light microscopy at a single-cell resolution. Remarkably,DMSO increases the attachment efficiency by > 200-fold. We further identify the QLDPAF sequence within preS1 as the receptor-binding viral domain epitope. Interestingly, a similar sequence is shared by several cellular, bacterial and viral proteins involved in cell adhesion, attachment and fusion. We also found that the small HBsAg contains a secondary attachment site that recognizes a distinct receptor on the cell membrane. Furthermore, we provide evidence in support of multivalent HBV attachment with synergistic interplay. Our data depict a mechanistic view of virus attachment and ingestion.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 10:12:11