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Hydrodynamic, electron-microscopic, and ligand-binding analysis of the epstein-barr virus c3dg receptor (cr-2)

Academic Article
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Overview

authors

  • Moore, M. D.
  • Discipio, R. G.
  • Cooper, N. R.
  • Nemerow, Glen

publication date

  • December 1989

journal

  • Journal of Biological Chemistry  Journal

abstract

  • The interaction of the Epstein-Barr virus/45-kDa proteolytic fragment of C3 (C3dg) receptor (CR2) with its viral ligand, the Epstein-Barr virus glycoprotein gp350/220, initiates the sequence of events leading to virus internalization and B lymphocyte transformation. Soluble recombinant receptor (rCR2) and gp350/220 as well as the natural ligand, C3dg, were subjected to a number of analytical techniques including gel permeation chromatography, density gradient ultracentrifugation, circular dichroism, and electron microscopy in order to determine their hydrodynamic, structural, and binding properties. Both rCR2 and gp350/220 were found to be highly extended proteins (f/fo = 2.1 and 2.4/2.2, respectively). C3dg, in contrast to the viral ligand, is only somewhat elongated (f/fo = 1.5). Soluble rCR2, visualized by high resolution electron microscopy, was shown to be an extended, highly flexible molecule comprised of ringlet domains, each approximately 24.1 A in length, which likely correspond to the short consensus repeat motif deduced from the CR2 cDNA nucleotide sequence. Ligand-binding studies carried out under physiological conditions indicated that gp350/220 binding to rCR2 was saturable and univalent, with a dissociation constant of 3.2 nM. In contrast, monomeric C3dg did not bind to rCR2 under physiological conditions; however, at reduced ionic strength, monomeric C3dg binding could be measured. These studies indicate that the affinity of the C3dg monomer for rCR2 under physiologic conditions is approximately 10(4)-fold less than that of the viral ligand. The molecular properties of rCR2 revealed in these studies provide essential information for future studies of the biologic functions of the Epstein-Barr virus/C3dg receptor.

subject areas

  • Antigens, CD
  • Antigens, Differentiation, B-Lymphocyte
  • Antigens, Viral
  • Circular Dichroism
  • Complement C3d
  • Enzyme-Linked Immunosorbent Assay
  • Herpesvirus 4, Human
  • Humans
  • Kinetics
  • Ligands
  • Microscopy, Electron
  • Protein Binding
  • Protein Conformation
  • Receptors, Complement
  • Receptors, Complement 3d
  • Viral Matrix Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 2555366
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Additional Document Info

start page

  • 20576

end page

  • 20582

volume

  • 264

issue

  • 34

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