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Journal of Virology, August 2009, p. 8082-8089, Vol. 83, No. 16
0022-538X/09/$08.00+0     doi:10.1128/JVI.00777-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Time-Dependent Transformation of the Herpesvirus Tegument{triangledown}

William W. Newcomb and Jay C. Brown*

Department of Microbiology and Cancer Center, University of Virginia Health System, Charlottesville, Virginia 22908

Received 16 April 2009/ Accepted 28 May 2009

All herpesviruses have a layer of protein called the tegument that lies between the virion membrane and the capsid. The tegument consists of multiple, virus-encoded protein species that together can account for nearly half the total virus protein. To clarify the structure of the tegument and its attachment to the capsid, we used electron microscopy and protein analysis to examine the tegument of herpes simplex virus type 1 (HSV-1). Electron microscopic examination of intact virions revealed that whereas the tegument was asymmetrically distributed around the capsid in extracellular virions, it was symmetrically arranged in cell-associated virus. Examination of virions after treatment with nonionic detergent demonstrated that: (i) in extracellular virus the tegument was resistant to removal with Triton X-100 (TX-100), whereas it was lost nearly completely when cell-associated virus was treated in the same way; (ii) the tegument in TX-100-treated extracellular virions was asymmetrically distributed around the capsid as it is in unextracted virus; and (iii) in some images, tegument was seen to be linked to the capsid by short, regularly spaced connectors. Further analysis was carried out with extracellular virus harvested from cells at different times after infection. It was observed that while the amount of tegument present in virions was not affected by time of harvest, the amount remaining after TX-100 treatment increased markedly as the time of harvest was increased from 24 h to 64 h postinfection. The results support the view that HSV-1 virions undergo a time-dependent change in which the tegument is transformed from a state in which it is symmetrically organized around the capsid and extractable with TX-100 to a state where it is asymmetrically arranged and resistant to extraction.


* Corresponding author. Mailing address: Department of Microbiology Box 800734, University of Virginia Health System, 1300 Jefferson Park Ave., Charlottesville, VA 22908. Phone: (434) 924-1814. Fax: (434) 982-1071. E-mail: jcb2g{at}virginia.edu

{triangledown} Published ahead of print on 3 June 2009.


Journal of Virology, August 2009, p. 8082-8089, Vol. 83, No. 16
0022-538X/09/$08.00+0     doi:10.1128/JVI.00777-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.