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http://purl.uniprot.org/citations/14970226http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14970226http://www.w3.org/2000/01/rdf-schema#comment"DC-SIGN is a C-type lectin that binds to endogenous adhesion molecules ICAM-2 and ICAM-3 as well as the viral envelope glycoprotein human immunodeficiency virus, type 1, glycoprotein (gp) 120. We wished to determine whether DC-SIGN binds differently to its endogenous ligands ICAM-2 and ICAM-3 versus HIV-1 gp120. We found that recombinant soluble DC-SIGN bound to gp120-Fc more than 100- and 50-fold better than ICAM-2-Fc and ICAM-3-Fc, respectively. This relative difference was maintained using DC-SIGN expressed on three different CD4-negative cell lines. Although the cell surface affinity for gp120 varied by up to 4-fold on the cell lines examined, the affinity for gp120 was not a correlate of the ability of the cell line to transfer virus. Monosaccharides with equatorial 4-OH groups competed as well as D-mannose for gp120 binding to DC-SIGN, regardless of how the other hydroxyl groups were positioned. Disaccharide competitors and glycan chip analysis showed that DC-SIGN has a preference for oligosaccharides linked in an alpha-anomeric configuration. Alanine-scanning mutagenesis of DC-SIGN revealed that highly conserved residues that coordinate calcium (Asp-366) and/or are involved in both calcium and specific carbohydrate interactions (Glu-347, Asn-349, Glu-354, and Asp-355) significantly compromised binding to all three ligands. Mutating non-conserved residues (Asn-311, Arg-345, Val-351, Gly-352, Glu-353, Ser-360, Gly-361, and Asn-362) minimally affected binding except for the Asp-367 mutant, which enhanced gp120 binding but diminished ICAM-2 and ICAM-3 binding. Conversely, mutating the moderately conserved residue (Gly-346) abrogated gp120 binding but enhanced ICAM-2 and ICAM-3 binding. Thus, DC-SIGN appears to bind in a distinct but overlapping manner to gp120 when compared with ICAM-2 and ICAM-3."xsd:string
http://purl.uniprot.org/citations/14970226http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m400184200"xsd:string
http://purl.uniprot.org/citations/14970226http://purl.uniprot.org/core/author"Lee B."xsd:string
http://purl.uniprot.org/citations/14970226http://purl.uniprot.org/core/author"Negrete O.A."xsd:string
http://purl.uniprot.org/citations/14970226http://purl.uniprot.org/core/author"Su S.V."xsd:string
http://purl.uniprot.org/citations/14970226http://purl.uniprot.org/core/author"Hong P."xsd:string
http://purl.uniprot.org/citations/14970226http://purl.uniprot.org/core/author"Baik S."xsd:string
http://purl.uniprot.org/citations/14970226http://purl.uniprot.org/core/author"Gurney K.B."xsd:string
http://purl.uniprot.org/citations/14970226http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14970226http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/14970226http://purl.uniprot.org/core/pages"19122-19132"xsd:string
http://purl.uniprot.org/citations/14970226http://purl.uniprot.org/core/title"DC-SIGN binds to HIV-1 glycoprotein 120 in a distinct but overlapping fashion compared with ICAM-2 and ICAM-3."xsd:string
http://purl.uniprot.org/citations/14970226http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/14970226http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14970226
http://purl.uniprot.org/citations/14970226http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/14970226
http://purl.uniprot.org/uniprot/#_A0A0H4PIN7-mappedCitation-14970226http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14970226
http://purl.uniprot.org/uniprot/#_A0A0H4PJU2-mappedCitation-14970226http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14970226
http://purl.uniprot.org/uniprot/#_A0A0H4PJU9-mappedCitation-14970226http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14970226
http://purl.uniprot.org/uniprot/#_A0A0H4PMS7-mappedCitation-14970226http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14970226
http://purl.uniprot.org/uniprot/#_A0A0H4Q180-mappedCitation-14970226http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14970226
http://purl.uniprot.org/uniprot/#_B2R907-mappedCitation-14970226http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14970226
http://purl.uniprot.org/uniprot/#_A8KAP5-mappedCitation-14970226http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14970226
http://purl.uniprot.org/uniprot/#_B2R736-mappedCitation-14970226http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14970226
http://purl.uniprot.org/uniprot/#_B4E2A8-mappedCitation-14970226http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14970226