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Establishment of Epstein-Barr Virus Growth-transformed Lymphoblastoid Cell Lines

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Published on: November 8, 2011

Epstein-Barr virus BDLF2-BMRF2 complex affects cellular morphology.

Jens-Bernhard Loesing^1,2, Stefano Di Fiore³, Klaus Ritter²

¹Fraunhofer Institute for Molecular Biology and Applied Ecology (IME), Forckenbeckstr. 6, 52074 Aachen, Germany.

The Journal of General Virology

|March 7, 2009

Summary

This summary is machine-generated.

Epstein-Barr virus (EBV) envelope proteins BMRF2 and BDLF2 form a heterodimer. This complex alters cell shape by reorganizing the actin cytoskeleton, potentially aiding virus spread.

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Area of Science:

Virology
Cell Biology
Molecular Biology

Background:

Herpesvirus glycoproteins often form heterodimers to perform unique functions.
Epstein-Barr virus (EBV) is a human herpesvirus implicated in various cancers.

Purpose of the Study:

To investigate the interaction between EBV BMRF2 and BDLF2.
To determine the functional consequences of this interaction on protein trafficking and cellular morphology.

Main Methods:

Transient expression of BMRF2 and BDLF2 in mammalian cells.
Analysis of protein localization using cell imaging techniques.
Investigation of cellular morphology changes and the role of RhoA signaling.

Main Results:

BMRF2 and BDLF2 individually localized to the ER and Golgi.
Co-expression led to co-trafficking to the plasma membrane.
Complex formation induced significant cellular morphological changes, including membrane protrusions.
The RhoA GTPase pathway was identified as central to the observed cytoskeleton reorganization.

Conclusions:

EBV BMRF2 and BDLF2 form a functional glycoprotein heterodimer.
This heterodimer alters cellular morphology via actin cytoskeleton reorganization.
The BMRF2-BDLF2 complex may facilitate EBV virion spread between cells.