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Journal of Virology, June 2008, p. 5198-5211, Vol. 82, No. 11
0022-538X/08/$08.00+0     doi:10.1128/JVI.02681-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Simultaneous Tracking of Capsid, Tegument, and Envelope Protein Localization in Living Cells Infected with Triply Fluorescent Herpes Simplex Virus 1{triangledown}

Ken Sugimoto,1 Masashi Uema,1 Hiroshi Sagara,2 Michiko Tanaka,3 Tetsutaro Sata,3 Yasuhiro Hashimoto,4 and Yasushi Kawaguchi1*

Division of Viral Infection, Department of Infectious Disease Control, International Research Center for Infectious Diseases,1 Fine Morphology Laboratory, Department of Basic Medical Science, The Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo 108-8639,2 Department of Pathology, National Institute of Infectious Disease, Shinjuku-ku, Tokyo 162-8640,3 Glyco-Chain Functions Laboratory, Supra-Biomolecular System Group, Frontier Research System, RIKEN, Wako-shi, Saitama 351-0198, Japan4

Received 18 December 2007/ Accepted 10 March 2008

We report here the construction of a triply fluorescent-tagged herpes simplex virus 1 (HSV-1) expressing capsid protein VP26, tegument protein VP22, and envelope protein gB as fusion proteins with monomeric yellow, red, and cyan fluorescent proteins, respectively. The recombinant virus enabled us to monitor the dynamics of these capsid, tegument, and envelope proteins simultaneously in the same live HSV-1-infected cells and to visualize single extracellular virions with three different fluorescent emissions. In Vero cells infected by the triply fluorescent virus, multiple cytoplasmic compartments were found to be induced close to the basal surfaces of the infected cells (the adhesion surfaces of the infected cells on the solid growth substrate). Major capsid, tegument, and envelope proteins accumulated and colocalized in the compartments, as did marker proteins for the trans-Golgi network (TGN) which has been implicated to be the site of HSV-1 secondary envelopment. Moreover, formation of the compartments was correlated with the dynamic redistribution of the TGN proteins induced by HSV-1 infection. These results suggest that HSV-1 infection causes redistribution of TGN membranes to form multiple cytoplasmic compartments, possibly for optimal secondary envelopment. This is the first real evidence for the assembly of all three types of herpesvirus proteins—capsid, tegument, and envelope membrane proteins—in TGN.

* Corresponding author. Mailing address: Division of Viral Infection, Department of Infectious Disease Control, International Research Center for Infectious Diseases, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan. Phone: 81 3 6409 2070. Fax: 81 3 6409 2072. E-mail: ykawagu{at}ims.u-tokyo.ac.jp

{triangledown} Published ahead of print on 19 March 2008.

Journal of Virology, June 2008, p. 5198-5211, Vol. 82, No. 11
0022-538X/08/$08.00+0     doi:10.1128/JVI.02681-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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