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PMID: 2422399 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Purification of the Epstein-Barr virus/C3d complement receptor of human B lymphocytes: antigenic and functional properties of the purified protein.

Journal of virology ·Vol. 58 ·No. 2 ·1986-05-00 ·Pages 709-12

Nemerow GR, Siaw MF, Cooper NR

Abstract

The Epstein-Barr virus/C3d receptor (CR2) of human B lymphocytes was purified to homogeneity from Raji cells by immunoaffinity chromatography. The average yield of the 145-kilodalton receptor was 400 pmol (50 micrograms) per 10(10) cells, representing an approximate 75% recovery. The isolated 145-kilodalton protein was antigenically and functionally intact as it reacted with several anti-CR2 monoclonal antibodies and bound purified Epstein-Barr virus and C3d,g. These findings with the purified molecule provide an unequivocal demonstration of the dual receptor functions of this protein.

MeSH Terms
B-Lymphocytes/analysis,immunology Cell Line Chromatography, Affinity Complement C3 Complement C3d Enzyme-Linked Immunosorbent Assay Epitopes Herpesvirus 4, Human/metabolism Humans Molecular Weight Receptors, Complement/immunology,isolation & purification,metabolism Receptors, Complement 3d Receptors, Virus/immunology,isolation & purification,metabolism
Chemicals
Complement C3 Epitopes Receptors, Complement Receptors, Complement 3d Receptors, Virus Complement C3d
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Nemerow G R
Siaw M F
Cooper N R
References (18)
18 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1986-05-00
Pages
709-12
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC252969
Subset
IM
Grants
NIAID NIH HHS · AI-17354 · United States
NCI NIH HHS · CA-14692 · United States
NCI NIH HHS · CA-36204 · United States
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