The latent membrane protein-1 in Epstein-Barr virus-transformed lymphoblastoid cells is found with ubiquitin-protein conjugates and heat-shock protein 70 in lysosomes oriented around the microtubule organizing centre

J Pathol. 1991 Jul;164(3):203-14. doi: 10.1002/path.1711640305.

Abstract

Immunofluorescence studies on Epstein-Barr virus (EBV)-transformed lymphoblastoid cells have previously shown that the latent membrane transforming protein (LMP-1) is found in patch-like inclusions which also immunostain for vimentin. We now show that EBV transformation causes a major reorganization of intermediate filaments, microtubules, mitochondria, and lysosomal elements, which generally become oriented around the microtubule organizing centre. Immunogold electron microscopy shows that LMP-1 is primarily concentrated in secondary lysosomes together with ubiquitin-protein conjugates and heat-shock protein 70. Intermediate filament inclusion formation with the above characteristics may be a general response triggered by other membrane glycoproteins; as seen, for example, in major human neurodegenerative diseases such as diffuse Lewy body disease.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, Viral / analysis*
  • B-Lymphocytes / chemistry*
  • B-Lymphocytes / ultrastructure
  • Cell Line, Transformed
  • Heat-Shock Proteins / analysis*
  • Herpesvirus 4, Human*
  • Humans
  • Immunohistochemistry
  • Intermediate Filaments / ultrastructure
  • Lysosomes / chemistry*
  • Microscopy, Electron
  • Microtubules / chemistry
  • Microtubules / ultrastructure*
  • Ubiquitins / analysis
  • Vimentin / analysis
  • Viral Envelope Proteins / analysis*
  • Viral Matrix Proteins*

Substances

  • Antigens, Viral
  • EBV-associated membrane antigen, Epstein-Barr virus
  • Heat-Shock Proteins
  • Ubiquitins
  • Vimentin
  • Viral Envelope Proteins
  • Viral Matrix Proteins