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Journal of Virology, July 2008, p. 6272-6287, Vol. 82, No. 13
0022-538X/08/$08.00+0     doi:10.1128/JVI.02345-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Multimerization of Tegument Protein pp28 within the Assembly Compartment Is Required for Cytoplasmic Envelopment of Human Cytomegalovirus{triangledown}

Jun-Young Seo1 and William J. Britt1,2,3*

Departments of Microbiology,1 Pediatrics,2 Neurobiology, School of Medicine, University of Alabama in Birmingham, Birmingham, Alabama 352333

Received 30 October 2007/ Accepted 25 March 2008

Human cytomegalovirus (HCMV) UL99-encoded pp28 is an essential tegument protein required for envelopment and production of infectious virus. Nonenveloped virions accumulate in the cytoplasm of cells infected with recombinant viruses with the UL99 gene deleted. Previous results have suggested that a key function of pp28 in the envelopment of infectious HCMV is expressed after the protein localizes in the assembly compartment (AC). In this study, we investigated the potential role of pp28 multimerization in the envelopment of the infectious virion. Our results indicated that pp28 multimerized during viral infection and that interacting domains responsible for self-interaction were localized in the amino terminus of the protein (amino acids [aa] 1 to 43). The results from transient-expression and/or infection assays indicated that the self-interaction took place in the AC. A mutant pp28 molecule containing only the first 35 aa failed to accumulate in the AC, did not interact with pp28 in the AC, and could not support virus replication. In contrast, the first 50 aa of pp28 was sufficient for the self-interaction within the AC and the assembly of infectious virus. Recombinant viruses encoding an in-frame deletion of aa 26 to 33 of pp28 were replication competent, whereas infectious virus was not recovered from HCMV BACs lacking aa 26 to 43. These findings suggested that the accumulation of pp28 was a prerequisite for multimerization of pp28 within the AC and that pp28 multimerization in the AC represented an essential step in the envelopment and production of infectious virions.

* Corresponding author. Mailing address: Department of, Pediatrics, Room 107, Harbor Bldg., Children's Hospital, 1600 7th Ave. South, Birmingham, AL 35233. Phone: (205) 996-7762. Fax: (205) 975-6549. E-mail: wbritt{at}peds.uab.edu

{triangledown} Published ahead of print on 2 April 2008.

Journal of Virology, July 2008, p. 6272-6287, Vol. 82, No. 13
0022-538X/08/$08.00+0     doi:10.1128/JVI.02345-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Buchkovich, N. J., Maguire, T. G., Paton, A. W., Paton, J. C., Alwine, J. C. (2009). The Endoplasmic Reticulum Chaperone BiP/GRP78 Is Important in the Structure and Function of the Human Cytomegalovirus Assembly Compartment. J. Virol. 83: 11421-11428 [Abstract] [Full Text]  


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