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Identification of gp350 as the viral glycoprotein mediating attachment of epstein-barr-virus (ebv) to the ebv/c3d receptor of b-cells - sequence homology of gp350 and c3-complement fragment c3d

Academic Article
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Overview

authors

  • Nemerow, Glen
  • Mold, C.
  • Schwend, V. K.
  • Tollefson, V.
  • Cooper, N. R.

publication date

  • May 1987

journal

  • Journal of Virology  Journal

abstract

  • The major Epstein-Barr virus (EBV) envelope glycoprotein, gp350, was purified from the B95-8 cell line and analyzed for its ability to mediate virus attachment to the isolated EBV/C3d receptor (CR2) of human B lymphocytes. Purified gp350 and EBV, but not cytomegalovirus, exhibited dose-dependent binding to purified CR2 in dot blot immunoassays. Binding was inhibited by certain monoclonal antibodies to CR2 and to gp350. Liposomes bearing incorporated gp350 bound to CR2-positive B-cell lines but not to CR2-negative lines. Liposome binding was also inhibited by the OKB7 anti-CR2 monoclonal antibody. A computer-generated comparison of the deduced gp350 amino acid sequence with that of the human C3d complement fragment revealed two regions of significant primary sequence homology, a finding which suggests that a common region on these two unrelated proteins may be involved in CR2 binding.

subject areas

  • Amino Acid Sequence
  • Antibodies, Monoclonal
  • B-Lymphocytes
  • Cell Line
  • Complement C3
  • Complement C3d
  • Glycoproteins
  • Herpesvirus 4, Human
  • Humans
  • Liposomes
  • Receptors, Complement
  • Receptors, Complement 3d
  • Receptors, Virus
  • Viral Envelope Proteins
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Identity

PubMed Central ID

  • PMC254117

International Standard Serial Number (ISSN)

  • 0022-538X

PubMed ID

  • 3033269
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Additional Document Info

start page

  • 1416

end page

  • 1420

volume

  • 61

issue

  • 5

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