Accumulation of Virion Tegument and Envelope Proteins in a Stable Cytoplasmic Compartment during Human Cytomegalovirus Replication: Characterization of a Potential Site of Virus Assembly

doi:10.1128/JVI.74.2.975-986.2000

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Journal of Virology, January 2000, p. 975-986, Vol. 74, No. 2
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Accumulation of Virion Tegument and Envelope Proteins in a Stable Cytoplasmic Compartment during Human Cytomegalovirus Replication: Characterization of a Potential Site of Virus Assembly

Veronica Sanchez,¹^, Kenneth D. Greis,²^, Elizabeth Sztul,³ and William J. Britt¹^,⁴^,^*

Departments of Pediatrics,¹ Biochemistry and Molecular Genetics,² Cell Biology,³ and Microbiology,⁴ The University of Alabama at Birmingham, Birmingham, Alabama 35233

Received 3 August 1999/Accepted 11 October 1999

The assembly of human cytomegalovirus (HCMV) is thought to be similar to that which has been proposed for alphaherpesvirusesand involve envelopment of tegumented subviral particles at thenuclear membrane followed by export from the cell by a poorlydefined pathway. However, several studies have shown that at leasttwo tegument virion proteins remain in the cytoplasm during theHCMV replicative cycle, thereby suggesting that HCMV cannot acquireits final envelope at the nuclear envelope. We investigated theassembly of HCMV by determining the intracellular traffickingof the abundant tegument protein pp150 (UL32) in productivelyinfected human fibroblasts. Our results indicated that pp150 remainedwithin the cytoplasm throughout the replicative cycle of HCMVand accumulated in a stable, juxtanuclear structure late in infection.Image analysis using a variety of cell protein-specific antibodiesindicated that the pp150-containing structure was not a componentof the endoplasmic reticulum, (ER), ER-Golgi intermediate compartment,cis or medial Golgi, or lysosomes. Partial colocalization of thestructure was noted with the trans-Golgi network, and it appearedto lie in close proximity to the microtubule organizing center.Two additional tegument proteins (pp28 and pp65) and three envelopeglycoproteins (gB, gH, and gp65) localized in this same structurelate infection. This compartment appeared to be relatively stablesince pp150, pp65, and the processed form of gB could be coisolatedfollowing cell fractionation. Our findings indicated that pp150was expressed exclusively within the cytoplasm throughout theinfectious cycle of HCMV and that the accumulation of the pp150in this cytoplasmic structure was accompanied by at least fiveother virion proteins. These results suggested the possibilitythat this virus-induced structure represented a cytoplasmic siteof virusassembly.

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

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

Present address: Procter and Gamble Pharmaceuticals, Mason,Ohio.

Journal of Virology, January 2000, p. 975-986, Vol. 74, No. 2
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

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