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Journal of Virology, June 2005, p. 6947-6956, Vol. 79, No. 11
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.11.6947-6956.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Herpes Simplex Virus Type 1 UL51 Protein Is Involved in Maturation and Egress of Virus Particles

Naoki Nozawa,1,2 Yasushi Kawaguchi,1,2 Michiko Tanaka,3 Akihisa Kato,1 Ai Kato,1 Hiroshi Kimura,4 and Yukihiro Nishiyama1*

Department of Virology, Nagoya University Graduate School of Medicine Tsurumai-cho 65, Showa-ku, Nagoya 466-8550, Japan,1 PRESTO, Japan Science and Technology Agency, Honcho 4-1-8, Kawaguchi, Saitama 332-0012, Japan,2 Department of Pathology, National Institute of Infectious Disease, Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan,3 Department of Pediatrics, Nagoya University Graduate School of Medicine Tsurumai-cho 65, Showa-ku, Nagoya 466-8550, Japan4

Received 4 August 2004/ Accepted 25 January 2005

The UL51 gene of herpes simplex virus type 1 (HSV-1) encodes a phosphoprotein whose homologs are conserved throughout the herpes virus family. Recently, we reported that UL51 protein colocalizes with Golgi marker proteins in transfected cells and that targeting of UL51 protein to the Golgi apparatus depends on palmitoylation of its N-terminal cysteine at position 9 (N. Nozawa, T. Daikoku, T. Koshizuka, Y. Yamauchi, T. Yoshikawa, and Y. Nishiyama, J. Virol. 77:3204-3216, 2003). However, its role in the HSV replication cycle was unknown. Here, we generated UL51-null mutants (FDL51) in HSV-1 to uncover the function of UL51 protein. We show that the mutant plaques were much smaller in size and that maximal titers were reduced nearly 100-fold compared to wild-type virus. Electron microscopy indicated that the formation of nucleocapsids was not affected by the deletion of UL51 but that viral egress from the perinuclear space was severely compromised. In FDL51-infected cells, a large number of enveloped nucleocapsids were observed in the perinuclear space, but enveloped mature virions in the cytoplasm, as well as extracellular mature virions, were rarely detected. These defects were fully rescued by reinsertion of the UL51 gene. These results indicate that UL51 protein is involved in the maturation and egress of HSV-1 virus particles downstream of the initial envelopment step.

* Corresponding author. Mailing address: Department of Virology, Nagoya University Graduate School of Medicine Tsurumai-cho 65, Showa-ku, Nagoya 466-8550, Japan. Phone: 81-52-744-2451. Fax: 81-52-744-2452. E-mail: ynishiya{at}med.nagoya-u.ac.jp.

Journal of Virology, June 2005, p. 6947-6956, Vol. 79, No. 11
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.11.6947-6956.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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