A Kaykas

AB Rickinson

AG Eliopoulos

Amanda Emery

B Clausse

B Nyfeler

BA Mainou

CP Kung

CW Dawson

D Liu

D Wang

David N Everly

DN Everly Jr

E Paine

ED Kieff

G Mosialos

H Ardila-Osorio

I Remy

J Lee

J Piehler

JE Floettmann

K Hennessy

KD Brown

KM Izumi

KM Kaye

L Young

LE Huye

LS Young

M Higuchi

ML Roberts

N Raab-Traub

NJ Thornburg

O Devergne

P Brennan

Pooja Talaty

RK Moorthy

S Ning

SM Hiatt

T Yasui

TK Kerppola

U Schultheiss

V Soni

VR Baichwal

WE Miller

WL Yang

YJ Shyu

YJ Song

Z Ding

ZP Xia

Virology Journal

English

PubMed

Springer - Publisher Connector

Characterization of the latent membrane protein 1 signaling complex of Epstein-Barr virus in the membrane of mammalian cells with bimolecular fluorescence complementation

Abstract
          
            Background
            Bimolecular fluorescence complementation (BiFC) is a novel technique to examine protein-protein interaction through the assembly of fluorescent proteins. In the present study, BiFC was used to study the assembly of the Epstein-Barr virus latent membrane protein 1 (LMP1) signaling complex within the membrane of mammalian cells. LMP1 signaling requires oligomerization, localization to lipid rafts, and association of the cytoplasmic domain to adaptor proteins, such as the tumor necrosis factor receptor associated factors (TRAFs).
          
          
            Methods
            LMP1-TRAF and LMP1-LMP1 interactions were assayed by BiFC using fluorescence microscopy and flow cytometry. Function of LMP1 BiFC contructs were confirmed by transformation assays and nuclear factor- κB (NF-κB) reporter assays.
          
          
            Results
            BiFC was observed between LMP1 and TRAF2 or TRAF3 and mutation of the LMP1 signaling domains reduced complementation. Fluorescence was observed in previously described LMP1 signaling locations. Oligomerization of LMP1 with itself induced complementation and BiFC. LMP1-BiFC constructs were fully functional in rodent fibroblast transformation assays and activation of NF-κB reporter activity. The BiFC domain partially suppressed some LMP1 mutant phenotypes.
          
          
            Conclusions
            Together these data suggest that BiFC is a unique and novel platform to identify and characterize proteins recruited to the LMP1-signaling complex.
          </jats:sec

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Characterization of the latent membrane protein 1 signaling complex of Epstein-Barr virus in the membrane of mammalian cells with bimolecular fluorescence complementation

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