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Journal of Virology, April 2000, p. 3842-3851, Vol. 74, No. 8
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Human Cytomegalovirus pp28 (UL99) Localizes to a Cytoplasmic Compartment Which Overlaps the Endoplasmic Reticulum-Golgi-Intermediate Compartment

Veronica Sanchez,1,dagger Elizabeth Sztul,2 and William J. Britt1,3,*

Departments of Pediatrics,1 Cell Biology,2 and Microbiology,3 The University of Alabama at Birmingham, Birmingham, Alabama

Received 9 November 1999/Accepted 18 January 2000

Although the assembly of herpesviruses has remained an active area of investigation, considerable controversy continues to surround the cellular location of tegument and envelope acquisition. This controversy is particularly evident when the proposed pathways for alpha - and beta -herpesvirus assembly are compared. We have approached this aspect of human cytomegalovirus (HCMV) assembly, specifically, envelopment, by investigating the intracellular trafficking of viral tegument proteins which localize in the cytoplasms of infected cells. In this study we have demonstrated that the virion tegument protein pp28 (UL99), a true late protein, was membrane associated as a result of myristoylation. A mutation in this protein which prevented incorporation of [3H]myristic acid also altered the detergent solubility and intracellular distribution of the protein when it was expressed in transfected cells. Using a panel of markers for intracellular compartments, we could localize the expression of wild-type pp28 to an intracellular compartment which colocalized with the endoplasmic reticulum-Golgi-intermediate compartment (ERGIC), a dynamic compartment of the secretory pathway which interfaces with both the ER and Golgi apparatus. The localization of this viral tegument protein within an early secretory compartment of the cell provided further evidence that the assembly of the HCMV tegument likely includes a cytoplasmic phase. Because pp28 has been shown to be localized to a cytoplasmic assembly compartment in HCMV-infected cells, our findings also suggested that viral tegument protein interactions within the secretory pathway may have an important role in the assembly of the virion.

* Corresponding author. Mailing address: Department of Pediatrics, 1600 7th Ave. South, Suite 752, Birmingham, AL 35233. Phone: (205) 939-9590. Fax: (205) 975-6549. E-mail: wbritt{at}peds.uab.edu.

dagger Present address: Department of Biology, University of California, San Diego, La Jolla, Calif.

Journal of Virology, April 2000, p. 3842-3851, Vol. 74, No. 8
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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