Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0042-6822(03)00261-7
Title: Characterization of a 105-kDa plasma membrane associated glycoprotein that is involved in West Nile virus binding and infection
Authors: Chu, J.J.H.
Ng, M.L. 
Keywords: Flavivirus
Kunjin virus
Mannose residues
N-linked sugars
Receptor
Virus entry
West Nile virus
Issue Date: 2003
Source: Chu, J.J.H., Ng, M.L. (2003). Characterization of a 105-kDa plasma membrane associated glycoprotein that is involved in West Nile virus binding and infection. Virology 312 (2) : 458-469. ScholarBank@NUS Repository. https://doi.org/10.1016/S0042-6822(03)00261-7
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, α-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 β-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. © 2003 Elsevier Science (USA). All rights reserved.
Source Title: Virology
URI: http://scholarbank.nus.edu.sg/handle/10635/31274
ISSN: 00426822
DOI: 10.1016/S0042-6822(03)00261-7
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