This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zhou, G.
Right arrow Articles by Roizman, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhou, G.
Right arrow Articles by Roizman, B.

 Previous Article  |  Next Article 

Journal of Virology, November 2002, p. 11469-11475, Vol. 76, No. 22
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.22.11469-11475.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Truncated Forms of Glycoprotein D of Herpes Simplex Virus 1 Capable of Blocking Apoptosis and of Low-Efficiency Entry into Cells Form a Heterodimer Dependent on the Presence of a Cysteine Located in the Shared Transmembrane Domains

Guoying Zhou and Bernard Roizman*

The Marjorie B. Kovler Viral Oncology Laboratories, The University of Chicago, Chicago, Illinois 60637

Received 17 May 2002/ Accepted 7 August 2002

Earlier studies have shown that herpes simplex virus 1 (HSV-1) virions of mutant lacking glycoprotein D (gD) and made in either complementing (gD-/+ stocks) or noncomplementing cells (gD-/- stocks) induce apoptosis. Subsequent studies have shown that apoptosis induced by gD-/- mutant virus stocks can be blocked by in trans delivery of viral genes that encode either intact gD or a mixture of two genes encoding the glycoprotein ectodomain plus transmembrane domain (gD-B) and transmembrane domain plus the cytoplasmic carboxyl terminus of the protein (gD-D), respectively. Since the presence of the transmembrane domains was critical for precluding apoptosis in the bipartite system, the question arose whether the two components, gD-B and gD-D, form a heterodimer mediated by an unpaired cysteine located in the transmembrane domain. We report the following. (i) The substitution of the unpaired cysteine with serine in either gD-B or gD-D truncated forms of gD disabled the ability of gD-D and gD-B to block apoptosis. (ii) Immunoprecipitation of gD-D coprecipitated gD-B only from lysates of cells transduced with gD-D and gD-B containing the cysteine in the transmembrane domains. Replacement of cysteine with serine ablated coprecipitation of the components. (ii) The mixture of gD-D and gD-B complemented at a low level gD-/+ virions. We conclude that the gD-B and gD-D can form a heterodimer dependent on the presence of cysteines in the transmembrane domain and the heterodimer can substitute for intact gD but at a much reduced efficiency.


* Corresponding author. Mailing address: The Marjorie B. Kovler Viral Oncology Laboratories, The University of Chicago, 910 East 58th St., Chicago, IL 60637. Phone: (773) 702-1898. Fax: (773) 702-1631. E-mail: bernard{at}cummings.uchicago.edu.


Journal of Virology, November 2002, p. 11469-11475, Vol. 76, No. 22
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.22.11469-11475.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Sanfilippo, C. M., Chirimuuta, F. N. W., Blaho, J. A. (2004). Herpes Simplex Virus Type 1 Immediate-Early Gene Expression Is Required for the Induction of Apoptosis in Human Epithelial HEp-2 Cells. J. Virol. 78: 224-239 [Abstract] [Full Text]