Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Biochemical and antigenic analysis of the epstein-barr virus/c3d receptor (cr-2)

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Siaw, M. F. E.
  • Nemerow, Glen
  • Cooper, N. R.

publication date

  • June 1986

journal

  • Journal of Immunology  Journal

abstract

  • Four monoclonal antibodies (OKB7, HB-5, AB-1, and anti-B2) that recognize a 145-kDa B cell-specific membrane structure have markedly different abilities to 1) inhibit C3d and EBV binding to B cells, 2) immunoprecipitate a 145-kDa B cell protein, and 3) stimulate B cell proliferation and differentiation into Ig-secreting cells. This study was initiated to determine whether these four monoclonal antibodies (MoAb) react with the same protein; a related goal was to determine whether the structure(s) recognized by these antibodies constitutes an antigenically related family of structurally distinct molecules. In the studies presented here, the four MoAb were found to fully immunoprecipitate the purified 145-kDa B cell molecule isolated by immunoaffinity chromatography on either OKB7, HB-5, or AB-1 columns, findings that show conclusively that the antibodies all react with the same B cell protein. The variable ability to immunoprecipitate this B cell membrane protein was found to result from differences in exposure or accessibility of the relevant antigenic epitopes in the detergent extract. The 145-kDa molecule immunoprecipitated with the four MoAb was equivalently sensitive to endoglycosidase F and yielded the same banding pattern after digestion with endoglycosidase F and after partial digestion with either S. aureus V8 protease or with trypsin. Within the limits of the sensitivity of these techniques, therefore, there is no evidence for carbohydrate or protein differences in the EBV/C3d receptor (CR2) molecule recognized by the four MoAb. Additional studies showed that the four MoAb react with distinct and nonoverlapping antigenic epitopes on the 145-kDa molecule. The variable abilities of the four MoAb to inhibit CR2 function and EBV binding and to trigger B cell activation, together with the other findings noted above, indicates that the 145-kDa EBV/C3d receptor possesses discretely localized functional domains.

subject areas

  • Antibodies, Monoclonal
  • Antigen-Antibody Reactions
  • Antigens, Viral
  • B-Lymphocytes
  • Cell Extracts
  • Cell Line
  • Endopeptidases
  • Glycoside Hydrolases
  • Herpesvirus 4, Human
  • Humans
  • Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
  • Membrane Proteins
  • Molecular Weight
  • Precipitin Tests
  • Receptors, Complement
  • Receptors, Complement 3d
  • Receptors, Virus
  • Serine Endopeptidases
  • Trypsin
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0022-1767

PubMed ID

  • 3009616
scroll to property group menus

Additional Document Info

start page

  • 4146

end page

  • 4151

volume

  • 136

issue

  • 11

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support