WW- and SH3-domain interactions with epstein-barr virus LMP2A

Richard Longnecker*, Mark Merchant, Melissa E. Brown, Sara Fruehling, James O. Bickford, Masato Ikeda, Ronald N. Harty

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

28 Scopus citations


Epstein-Barr virus (EBV) is a human herpesvirus which establishes a lifelong latent infection in B lymphocytes. Latent membrane protein 2A (LMP2A) is expressed in both humans with EBV latent infection and EBV immortalized cell lines grown in culture. Previous studies have shown that the amino terminal domain of LMP2A, which contains eight tyrosines, associates with a variety of cellular proteins via SH2-phosphotyrosine interactions. Also contained within the LMP2A amino terminal domain are five prolinerich regions, three of which possess the PxxP core consensus sequence required for interacting with SH3 domains and two of which possess the PPxY core consensus sequence (PY motif) required for interacting with class I type WW domains. In the current study, the ability of LMP2A to interact with either modular SH3 or WW domains was investigated. The results of these studies indicate that the two LMP2A PY motifs interact strongly with representative class I WW domains, but not with representative class II WW domains. In contrast, no interactions were detected between LMP2A and any of the five different SH3 domains tested. These data demonstrate that a subset of the conserved proline-rich motifs within the amino terminus of LMP2A can potentially mediate interactions with cellular proteins and may play a role in EBV-mediated latency and/or transformation. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)332-340
Number of pages9
JournalExperimental Cell Research
Issue number2
StatePublished - Jun 15 2000

ASJC Scopus subject areas

  • Cell Biology


Dive into the research topics of 'WW- and SH3-domain interactions with epstein-barr virus LMP2A'. Together they form a unique fingerprint.

Cite this