Title of article :
Cryo-EM Reconstruction of Dengue Virus in Complex with the Carbohydrate Recognition Domain of DC-SIGN
Author/Authors :
Zhang، Ying نويسنده , , Pokidysheva، Elena نويسنده , , Battisti، Anthony J. نويسنده , , Bator-Kelly، Carol M. نويسنده , , Chipman، Paul R. نويسنده , , Xiao، Chuan نويسنده , , Gregorio، G. Glenn نويسنده , , Hendrickson، Wayne A. نويسنده , , Kuhn، Richard J. نويسنده , , Rossmann، Michael G. نويسنده ,
Issue Information :
هفته نامه با شماره پیاپی سال 2006
Pages :
-484
From page :
485
To page :
0
Abstract :
Dengue virus (DENV) is a significant human pathogen that causes millions of infections and results in about 24,000 deaths each year. Dendritic cell-specific ICAM3 grabbing nonintegrin (DC-SIGN), abundant in immature dendritic cells, was previously reported as being an ancillary receptor interacting with the surface of DENV. The structure of DENV in complex with the carbohydrate recognition domain (CRD) of DC-SIGN was determined by cryo-electron microscopy at 25 (angstrom) resolution. One CRD monomer was found to bind to two glycosylation sites at Asn67 of two neighboring glycoproteins in each icosahedral asymmetric unit, leaving the third Asn67 residue vacant. The vacancy at the third Asn67 site is a result of the nonequivalence of the glycoprotein environments, leaving space for the primary receptor binding to domain III of E. The use of carbohydrate moieties for receptor binding sites suggests a mechanism for avoiding immune surveillance.
Keywords :
DIGLYPHUS ISAEA , Abamectin compatibility , Biological control , IPM , Greenhouse , Liriomyza trifolii
Journal title :
CELL
Serial Year :
2006
Journal title :
CELL
Record number :
102405
Link To Document :
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