Linked Life Data

17925391

Source:http://linkedlifedata.com/resource/pubmed/id/17925391

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
50
pubmed:dateCreated
2007-12-10
pubmed:abstractText
Complement receptor type 2 (CR2/CD21) is essential for the attachment of Epstein-Barr virus (EBV) to the surface of B-lymphocytes in an interaction mediated by the viral envelope glycoprotein gp350. The heavily glycosylated structure of EBV gp350 has recently been elucidated by x-ray crystallography, and the CR2 binding site on this protein has been characterized. To identify the corresponding gp350 binding site on CR2, we have undertaken a site-directed mutagenesis study targeting regions of CR2 that have previously been implicated in the binding of CR2 to the C3d/C3dg fragments of complement component C3. Wild-type or mutant forms of CR2 were expressed on K562 cells, and the ability of these CR2-expressing cells to bind gp350 was measured using flow cytometry. Mutations directed toward the two N-terminal extracellular domains of CR2 (SCR1-2) reveal that a large contiguous surface of CR2 SCR1-2 is involved in gp350 binding, including a number of positively charged residues (Arg-13, (Arg-28, (Arg-36, Lys-41, Lys-57, Lys-67, and Arg-83). These data appear to complement the CR2 binding site on gp350, which is characterized by a preponderance of negative charge. In addition to identifying the importance of charge in the formation of a CR2-gp350 complex, we also provide evidence that both SCR1 and SCR2 make contact with gp350. Specifically, two anti-CR2 monoclonal antibodies, designated as monoclonal antibodies 171 and 1048 whose primary epitopes are located within SCR2, inhibit binding of wild-type CR2 to EBV gp350; with regard to SCR1, both K562 cells expressing an S15P mutation and recombinant S15P CR2 proteins exhibit diminished gp350 binding.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
282
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
36614-25
pubmed:meshHeading
pubmed-meshheading:17925391-Amino Acid Substitution, pubmed-meshheading:17925391-Antibodies, Monoclonal, pubmed-meshheading:17925391-B-Lymphocytes, pubmed-meshheading:17925391-Binding Sites, pubmed-meshheading:17925391-Complement C3b, pubmed-meshheading:17925391-Complement C3d, pubmed-meshheading:17925391-Crystallography, X-Ray, pubmed-meshheading:17925391-Glycoproteins, pubmed-meshheading:17925391-Herpesvirus 4, Human, pubmed-meshheading:17925391-Humans, pubmed-meshheading:17925391-K562 Cells, pubmed-meshheading:17925391-Mutagenesis, Site-Directed, pubmed-meshheading:17925391-Mutation, Missense, pubmed-meshheading:17925391-Peptide Fragments, pubmed-meshheading:17925391-Protein Binding, pubmed-meshheading:17925391-Protein Structure, Tertiary, pubmed-meshheading:17925391-Receptors, Complement 3d, pubmed-meshheading:17925391-Recombinant Proteins, pubmed-meshheading:17925391-Viral Envelope Proteins, pubmed-meshheading:17925391-Virus Attachment
pubmed:year
2007
pubmed:articleTitle
Isolating the Epstein-Barr virus gp350/220 binding site on complement receptor type 2 (CR2/CD21).
pubmed:affiliation
Department of Medicine and Immunology, University of Colorado at Denver and Health Sciences Center, Aurora, Colorado 80045, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural