Latent membrane protein 2 (LMP2)

Osman Cen, Richard Longnecker*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapter

57 Scopus citations

Abstract

LMP2A is an EBV-encoded protein with three domains: (a) an N-terminal cytoplasmic domain, which has PY motifs that bind to WW domaincontaining E3 ubiquitin ligases and an ITAM that binds to SH2 domain-containing proteins, (b) a transmembrane domain with 12 transmembrane segments that localizes LMP2A in cellular membranes, and (c) a 27-amino acid C-terminal domain which mediates homodimerization and heterodimerization of LMP2 protein isoforms. The most prominent two isoforms of the protein are LMP2A and LMP2B. The LMP2B isoform lacks the 19-amino acid N-terminal domain found in LMP2A, which modulates cellular signaling resulting in a baseline activation of B cells and degradation of cellular kinases leading to the downregulation of normal B cell signaling pathways. These two seemingly contradictory processes allow EBV to establish and maintain latency. LMP2 is expressed in many EBVassociated malignancies. While its antigenic properties may be useful in developing LMP2-specific immunity, the LMP2A N-terminal motifs also provide a basis to target LMP2A-modulated cellular kinases for the development of treatment strategies.

Original languageEnglish (US)
Title of host publicationCurrent Topics in Microbiology and Immunology
PublisherSpringer Verlag
Pages151-180
Number of pages30
DOIs
StatePublished - Oct 1 2015

Publication series

NameCurrent Topics in Microbiology and Immunology
Volume391
ISSN (Print)0070-217X
ISSN (Electronic)2196-9965

ASJC Scopus subject areas

  • Immunology and Allergy
  • Microbiology
  • Immunology
  • Microbiology (medical)

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