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Journal of Virology, September 2005, p. 11837-11847, Vol. 79, No. 18
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.18.11837-11847.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Deletion of gpUL132, a Structural Component of Human Cytomegalovirus, Results in Impaired Virus Replication in Fibroblasts

Simone Spaderna,1,{dagger} Barbara Kropff,1 Yvonne Ködel,1 Siyuan Shen,2 Scott Coley,2 Shan Lu,2 William Britt,3 and Michael Mach1*

Institut für Klinische und Molekulare Virologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany,1 Department of Medicine, University of Massachusetts Medical School, Worcester, Massachusetts,2 Department of Pediatrics, University of Alabama School of Medicine, Birmingham, Alabama3

Received 7 April 2005/ Accepted 24 June 2005

The coding capacity of human cytomegalovirus (HCMV) for glycoproteins by far exceeds that of other herpesviruses. Few of these proteins have been characterized so far. We have investigated the gene product of reading frame UL132. The putative protein product of UL132 is a glycoprotein with a theoretical mass of 29.8 kDa. Transcription analysis revealed that the gene is transcribed with a true late kinetics from the laboratory-adapted strain AD169 and the low-passage isolate TB40E. Two proteins of 22 to 28 kDa and 45 to 60 kDa were detected in virus-infected cells as well as in extracellular virions. The larger protein carried N-linked carbohydrates. Both protein forms were present in laboratory-adapted strains as well as in low-passage isolates of HCMV. Recombinant viruses with the UL132 gene deleted were constructed in the low-passage HCMV isolate PAN as well as the high-passage isolate AD169. Deletion of UL132 from either genome resulted in a pronounced replication deficit with a reduction of approximately 100-fold for HCMV strain AD169. Thus, the protein product of the UL132 reading frame represents a structural viral glycoprotein of HCMV that has an important function for viral replication in tissue culture.

* Corresponding author. Mailing address: Institut für Klinische und Molekulare Virologie, Universität Erlangen-Nürnberg, Schlossgarten 4, 91054 Erlangen, Germany. Phone: 49 9131 8522107. Fax: 49 9131 8522101. E-mail: mlmach{at}viro.med.uni-erlangen.de.

{dagger} Present address: Pathologisch-Anatomisches Institut, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany.

Journal of Virology, September 2005, p. 11837-11847, Vol. 79, No. 18
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.18.11837-11847.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Ryckman, B. J., Jarvis, M. A, Drummond, D. D., Nelson, J. A., Johnson, D. C. (2006). Human Cytomegalovirus Entry into Epithelial and Endothelial Cells Depends on Genes UL128 to UL150 and Occurs by Endocytosis and Low-pH Fusion. J. Virol. 80: 710-722 [Abstract] [Full Text]  


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