Lysine-independent ubiquitination of Epstein-Barr virus LMP2A

Masato Ikeda, Akiko Ikeda, Richard Longnecker*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

52 Scopus citations

Abstract

Latent membrane protein 2A (LMP2A) of latent Epstein-Barr virus (EBV) specifically associates with HECT domain-containing Nedd4-family ubiquitin-protein ligases (E3s). Here we demonstrate that LMP2A is specifically ubiquitinated by the HECT domains of AIP4 and WWP2. Deletion and site-specific mutation of LMP2A indicates that LMP2A is ubiquitinated at its amino-terminus and is not ubiquitinated on lysine residues. LMP2A and LMP1, also encoded by EBV, are two of only four proteins that have been identified that are ubiquitinated at the amino-terminus, indicating that EBV may specifically target and utilize this host cell protein modification.

Original languageEnglish (US)
Pages (from-to)153-159
Number of pages7
JournalVirology
Volume300
Issue number1
DOIs
StatePublished - 2002

ASJC Scopus subject areas

  • Virology

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