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Transcript
Oral Presentation Jacob Marsh Genetics Program Department of Microbiology and Immunology Dr. John Wills Packaging Requirements for the UL21 Tegument Protein of Herpes Simplex Virus Jacob A. Marsh, Amy L. Harper, Nicholas L. Baird, David G. Meckes, Pei-Chun Yeh, John W. Wills The UL21 gene of herpes simplex virus (HSV) encodes a 535-amino-acid tegument protein that is located throughout the cytoplasm and nuclei of infected cells. Little is known of the function of this protein, but studies of pseudorabies virus (PRV) suggest a role in viral DNA processing in the nucleus (J Virol. 66:7096-103, Vet Res. 32:47-54). It has also been suggested that UL21 from HSV may be associated with microtubules (Genes Cells. 6:955-66). Mutants that lack this gene exhibit slow plaque formation and a ten-fold reduction in virus titer. In PRV, UL21 forms a complex with UL16, another tegument protein. In this study, we confirmed this interaction in HSV-1 by using immunopreciptation and GST pull-down assays. In addition, we determined that the C-terminal half of UL21 is both necessary and sufficient for the UL21-UL16 interaction. Using a transfection/infection-based assay, we found this same half of UL21 is necessary and sufficient for packaging into the virion, both in the presence and absence of full-length UL21. Analysis of knock-out mutants of each protein revealed that the interaction of UL21 and UL16 is not required for the packaging of either protein into the virion. Taken together, these data indicate that the C-terminal domain of UL21 is responsible for binding to both UL16 and some other protein needed for association with capsids and subsequently for packaging into the virion. Herpes simplex virus, tegument, assembly, egress, protein-protein interaction National Institute of Health, National Heart Association