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Journal of Virology, August 2001, p. 7506-7516, Vol. 75, No. 16
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.16.7506-7516.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

E1B 19K Blocks Bax Oligomerization and Tumor Necrosis Factor Alpha-Mediated Apoptosis

Ramya Sundararajan1 and Eileen White2,3,4,*

Howard Hughes Medical Institute,2 Center for Advanced Biotechnology and Medicine,1 Department of Molecular Biology and Biochemistry,3 and Cancer Institute of New Jersey,4 Rutgers University, Piscataway, New Jersey 08854

Received 27 February 2001/Accepted 4 May 2001

Tumor necrosis factor alpha (TNF-alpha )-mediated death signaling causes the recruitment of monomeric pro- apoptotic Bax into a 500-kDa protein complex. The adenovirus Bcl-2 homologue, E1B 19K, inhibits TNF-alpha -mediated apoptosis, interacts with Bax, and blocked the formation of the 500-kDa Bax complex. TNF-alpha and truncated Bid induced Bax-Bax cross-linking, indicative of oligomerization, and E1B 19K expression during infection inhibited this TNF-alpha -mediated Bax oligomerization. TNF-alpha signaled conformation changes at the Bax amino and carboxy termini. Exposure of the Bax amino terminus facilitates E1B 19K-Bax binding, which prevented exposure of the carboxy-terminal Bax Bcl-2 homology region 2 epitope. Inhibition of Bax oligomerization by E1B 19K is an activity that bears striking similarity to the means by which bacterial immunity proteins block pore formation by bacterial toxins which have structural homology to Bax.

* Corresponding author. Mailing address: Center for Advanced Biotechnology and Medicine, Howard Hughes Medical Institute, 679 Hoes Lane, Room 140, Piscataway, NJ 08854. Phone: (732) 235-5329. Fax: (732) 235-5795. E-mail: ewhite{at}cabm.rutgers.edu.

Journal of Virology, August 2001, p. 7506-7516, Vol. 75, No. 16
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.16.7506-7516.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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