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Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN.
Cell. 2006 Feb 10; 124(3):485-93.Cell

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 A 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.

Authors+Show Affiliations

Pokidysheva E
Department of Biological Sciences, Lilly Hall, 915 W. State Street, Purdue University, West Lafayette, IN 47907, USA.
Zhang Y
No affiliation info available
Battisti AJ
No affiliation info available
Bator-Kelly CM
No affiliation info available
Chipman PR
No affiliation info available
Xiao C
No affiliation info available
Gregorio GG
No affiliation info available
Hendrickson WA
No affiliation info available
Kuhn RJ
No affiliation info available
Rossmann MG
No affiliation info available

MeSH

Binding SitesCarbohydratesCell Adhesion MoleculesCryoelectron MicroscopyDendritic CellsDengue VirusHumansImage Processing, Computer-AssistedLectins, C-TypeModels, MolecularMultiprotein ComplexesProtein Structure, TertiaryReceptors, Cell SurfaceReceptors, VirusRecombinant Proteins

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16469696

Citation

Pokidysheva, Elena, et al. "Cryo-EM Reconstruction of Dengue Virus in Complex With the Carbohydrate Recognition Domain of DC-SIGN." Cell, vol. 124, no. 3, 2006, pp. 485-93.
Pokidysheva E, Zhang Y, Battisti AJ, et al. Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN. Cell. 2006;124(3):485-93.
Pokidysheva, E., Zhang, Y., Battisti, A. J., Bator-Kelly, C. M., Chipman, P. R., Xiao, C., Gregorio, G. G., Hendrickson, W. A., Kuhn, R. J., & Rossmann, M. G. (2006). Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN. Cell, 124(3), 485-93.
Pokidysheva E, et al. Cryo-EM Reconstruction of Dengue Virus in Complex With the Carbohydrate Recognition Domain of DC-SIGN. Cell. 2006 Feb 10;124(3):485-93. PubMed PMID: 16469696.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN. AU - Pokidysheva,Elena, AU - Zhang,Ying, AU - Battisti,Anthony J, AU - Bator-Kelly,Carol M, AU - Chipman,Paul R, AU - Xiao,Chuan, AU - Gregorio,G Glenn, AU - Hendrickson,Wayne A, AU - Kuhn,Richard J, AU - Rossmann,Michael G, PY - 2005/08/22/received PY - 2005/10/06/revised PY - 2005/11/11/accepted PY - 2006/2/14/pubmed PY - 2006/3/21/medline PY - 2006/2/14/entrez SP - 485 EP - 93 JF - Cell JO - Cell VL - 124 IS - 3 N2 - 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 A 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. SN - 0092-8674 UR - https://www.unboundmedicine.com/medline/citation/16469696/Cryo_EM_reconstruction_of_dengue_virus_in_complex_with_the_carbohydrate_recognition_domain_of_DC_SIGN_ DB - PRIME DP - Unbound Medicine ER -