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Characterization of a 105-kDa plasma membrane associated glycoprotein that is involved in West Nile virus binding and infection.

Abstract：

:This study attempts to isolate and characterize West Nile virus-binding molecules on the plasma membrane of Vero and murine neuroblastoma cells that is responsible for virus entry. Pretreatment of Vero cells with proteases, glycosidases (endoglycosidase H, alpha-mannosidase), and sodium periodate strongly inhibited West Nile virus infection, whereas treatments with phospholipases and heparinases had no effect. The virus overlay protein blot detected a 105-kDa molecule on the plasma membrane extract of Vero and murine neuroblastoma cells that bind to WN virus. Treatment of the 105-kDa molecules with beta-mercaptoethanol resulted in the virus binding to a series of lower molecular weight bands ranging from 30 to 40 kDa. The disruption of disulfide-linked subunits did not affect virus binding. N-linked sugars with mannose residues on the 105-kDa membrane proteins were found to be important in virus binding. Specific antibodies against the 105-kDa glycoprotein were highly effective in blocking virus entry. These results strongly supported the possibility that the 105-kDa protease-sensitive glycoprotein with complex N-linked sugars could be the putative receptor for WN virus.

journal_name

Virology

journal_title

Virology

authors

Chu JJ,Ng ML

doi

10.1016/s0042-6822(03)00261-7

subject

Has Abstract

pub_date

2003-08-01 00:00:00

pages

458-69

issue

2

eissn

0042-6822

issn

1096-0341

pii

S0042682203002617

journal_volume

312

pub_type

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