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Journal of Virology, September 2002, p. 8939-8952, Vol. 76, No. 17
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.17.8939-8952.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Ultrastructural Localization of the Herpes Simplex Virus Type 1 UL31, UL34, and US3 Proteins Suggests Specific Roles in Primary Envelopment and Egress of Nucleocapsids

Ashley E. Reynolds,1 Elizabeth G. Wills,1 Richard J. Roller,2 Brent J. Ryckman,2 and Joel D. Baines1*

Department of Microbiology and Immunology, Cornell University, Ithaca, New York 14853,1 Department of Microbiology, University of Iowa, Iowa City, Iowa 522422

Received 1 April 2002/ Accepted 4 June 2002

The wild-type UL31, UL34, and US3 proteins localized on nuclear membranes and perinuclear virions; the US3 protein was also on cytoplasmic membranes and extranuclear virions. The UL31 and UL34 proteins were not detected in extracellular virions. US3 deletion caused (i) virion accumulation in nuclear membrane invaginations, (ii) delayed virus production onset, and (iii) reduced peak virus titers. These data support the herpes simplex virus type 1 deenvelopment-reenvelopment model of virion egress and suggest that the US3 protein plays an important, but nonessential, role in the egress pathway.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Cornell University, Veterinary Medical Center (VMC) C5 131, Ithaca, NY 14853. Phone: (607) 253-3385. Fax: (607) 253-3384. E-mail: jdb11{at}cornell.edu.

Journal of Virology, September 2002, p. 8939-8952, Vol. 76, No. 17
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.17.8939-8952.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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