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Journal of Virology, November 2005, p. 13442-13453, Vol. 79, No. 21
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.21.13442-13453.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Identification, Subviral Localization, and Functional Characterization of the Pseudorabies Virus UL17 Protein

Barbara G. Klupp,1 Harald Granzow,2 Axel Karger,1 and Thomas C. Mettenleiter1*

Institutes of Molecular Biology,1 Infectology, Friedrich-Loeffler-Institut, D-17493 Greifswald-Insel Riems, Germany2

Received 24 January 2005/ Accepted 8 August 2005

Homologs of the UL17 gene of the alphaherpesvirus herpes simplex virus 1 (HSV-1) are conserved in all three subfamilies of herpesviruses. However, only the HSV-1 protein has so far been characterized in any detail. To analyze UL17 of pseudorabies virus (PrV) the complete 597-amino-acid protein was expressed in Escherichia coli and used for rabbit immunization. The antiserum recognized a 64-kDa protein in PrV-infected cell lysates and purified virions, identifying PrV UL17 as a structural virion component. In indirect immunofluorescence analyses of PrV-infected cells the protein was predominantly found in the nucleus. In electron microscopic studies after immunogold labeling of negatively stained purified virion preparations, UL17-specific label was detected on single, mostly damaged capsids, whereas complete virions and the majority of capsids were free of label. In ultrathin sections of infected cells, label was primarily found dispersed around scaffold-containing B-capsids, whereas on DNA-filled C-capsids it was located in the center. Empty intranuclear A-capsids were free of label, as were extracellular capsid-less L-particles. Functional characterization of PrV-{Delta}UL17F, a deletion mutant lacking codons 23 to 444, demonstrated that cleavage of viral DNA into unit-length genomes was inhibited in the absence of UL17. In electron microscopic analyses of PrV-{Delta}UL17F-infected RK13 cells, DNA-containing capsids were not detected, while numerous capsidless L-particles were observed. In summary, our data indicate that the PrV UL17 protein is an internal nucleocapsid protein necessary for DNA cleavage and packaging but suggest that the protein is not a prominent part of the tegument.

* Corresponding author. Mailing address: Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Boddenblick 5A, D-17493 Greifswald—Insel Riems, Germany. Phone: 49 38351 7250. Fax: 49 38351 7151. E-mail: Mettenleiter{at}rie.bfav.de.

Journal of Virology, November 2005, p. 13442-13453, Vol. 79, No. 21
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.21.13442-13453.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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