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PMID: 3035211 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Posttranslational processing of the Epstein-Barr virus-encoded p63/LMP protein.

Journal of virology ·Vol. 61 ·No. 7 ·1987-07-00 ·Pages 2100-8

Mann KP, Thorley-Lawson D

Abstract

In this paper we describe the posttranslational processing of the p63/LMP (latent membrane protein) encoded by Epstein-Barr virus in transformed B cells. Specifically, we show that after synthesis, free LMP disappeared with a half-life of about 0.5 h. This was caused by the association of LMP with an insoluble complex. All detectable LMP in the plasma membrane was insoluble. This interaction was resistant to nondenaturing detergents but readily dissociated with 8 M urea or by boiling in 0.5% sodium dodecyl sulfate, suggesting that LMP may be associated with cytoskeletal elements. Most of the Nonidet P-40-insoluble LMP was phosphorylated (ppLMP) primarily on serine but also on threonine residues. No phosphotyrosine was detected. Furthermore, greater than 90% of the ppLMP resided in the Nonidet P-40-insoluble fraction, suggesting a strong correlation between complexing and phosphorylation. Additionally, ppLMP was found to be associated with a 53,000-molecular-weight phosphoprotein (pp53) of unknown origin. Finally, LMP turned over extremely rapidly, with a half-life of about 2 h. Taken together, these properties suggest that although LMP falls broadly within the category of phosphorylated, cytoskeleton-associated oncoproteins, it is nevertheless clearly different from any previously described member of this family.

MeSH Terms
Amino Acids/analysis Antibodies, Monoclonal/immunology Antibodies, Viral/immunology Cell Line Cell Membrane/analysis Cytoskeleton/analysis Detergents Half-Life Herpesvirus 4, Human/immunology,metabolism Humans Isoelectric Focusing Lymphocytes/analysis Membrane Proteins/biosynthesis,immunology,isolation & purification Protein Processing, Post-Translational Solubility Viral Proteins/biosynthesis,immunology,isolation & purification
Chemicals
Amino Acids Antibodies, Monoclonal Antibodies, Viral Detergents Membrane Proteins Viral Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Mann K P
Thorley-Lawson D
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.61.7.2100-2108.1987
Published
1987-07-00
Pages
2100-8
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC254230
Subset
IM
Grants
NIAID NIH HHS · AI 00549 · United States
NIAID NIH HHS · AI 15310 · United States
NCI NIH HHS · CA 28737 · United States
External Links
PubMed source DOI: 10.1128/JVI.61.7.2100-2108.1987 PMC Full Text View journal details
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