Linked Life Data

7706299

Source:http://linkedlifedata.com/resource/pubmed/id/7706299

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1995-5-10
pubmed:abstractText
CD22, a B cell-specific receptor of the immunoglobulin superfamily, has been demonstrated to bind to oligosaccharides containing alpha 2-6-linked sialic acid (Sia) residues. Previously, we demonstrated that the minimal structure recognized by this lectin is the trisaccharide Sia alpha 2-6Gal beta 1-4GlcNAc, as found on N-linked, O-linked, or glycolipid structures (Powell, L., and Varki, A. (1994) J. Biol. Chem. 269, 10628-10636). Here we utilize a soluble immunoglobulin fusion construct (CD22Rg) to determine directly by equilibrium dialysis the stoichiometry (2:1) and dissociation constant (32 microM) for Neu5Ac alpha 2-6Gal beta 1-4Glc binding. Inhibition assays performed with over 30 different natural and synthetic sialylated and/or sulfated compounds are utilized to define in greater detail specific structural features involved in oligosaccharide-protein binding. Specifically, the critical features required for binding include the exocyclic hydroxylated side chain of the Sia residue and the alpha 2-6 linkage position to the underlying Gal unit. Surprisingly, alterations of the 2-, 3-, and 4-positions of the latter residue have limited effect on the binding. The nature of the residue to which the Gal is attached may affect binding. Bi(alpha 2-6)-sialylated biantennary oligosaccharides are capable of simultaneously interacting with both lectin sites present on the dimeric CD22Rg fusion construct, giving a marked improvement in binding over monosialylated compounds. Furthermore, data are presented indicating that full-length native CD22, expressed on the surface of Chinese hamster ovary cells, is structurally and functionally a multimeric protein, demonstrating a higher apparent affinity for multiply sialylated compounds over monosialylated compounds. These observations provide a mechanism for strong CD22-dependent cell adhesion despite the relatively low Kd for protein-sugar binding.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7523-32
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:7706299-Animals, pubmed-meshheading:7706299-Antigens, CD, pubmed-meshheading:7706299-Antigens, CD22, pubmed-meshheading:7706299-Antigens, Differentiation, B-Lymphocyte, pubmed-meshheading:7706299-B-Lymphocytes, pubmed-meshheading:7706299-Binding Sites, pubmed-meshheading:7706299-Carbohydrate Conformation, pubmed-meshheading:7706299-Carbohydrate Sequence, pubmed-meshheading:7706299-Cattle, pubmed-meshheading:7706299-Cell Adhesion Molecules, pubmed-meshheading:7706299-Fibrinogen, pubmed-meshheading:7706299-Humans, pubmed-meshheading:7706299-Kinetics, pubmed-meshheading:7706299-Lectins, pubmed-meshheading:7706299-Mice, pubmed-meshheading:7706299-Models, Structural, pubmed-meshheading:7706299-Molecular Sequence Data, pubmed-meshheading:7706299-Oligosaccharides, pubmed-meshheading:7706299-Recombinant Proteins, pubmed-meshheading:7706299-Structure-Activity Relationship
pubmed:year
1995
pubmed:articleTitle
Characterization of sialyloligosaccharide binding by recombinant soluble and native cell-associated CD22. Evidence for a minimal structural recognition motif and the potential importance of multisite binding.
pubmed:affiliation
Department of Medicine, University of California at San Diego, La Jolla 92093, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't