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<ArticleSet>
<Article>
<Journal>
				<PublisherName>University of Tehran</PublisherName>
				<JournalTitle>Journal of Sciences, Islamic Republic of Iran</JournalTitle>
				<Issn>1016-1104</Issn>
				<Volume>17</Volume>
				<Issue>1</Issue>
				<PubDate PubStatus="epublish">
					<Year>2006</Year>
					<Month>03</Month>
					<Day>01</Day>
				</PubDate>
			</Journal>
<ArticleTitle>In vitro Interaction of HSV-1 ORF P with Both Thymidine Kinase (TK) and an Unidentified Cellular Protein</ArticleTitle>
<VernacularTitle>-</VernacularTitle>
			<FirstPage></FirstPage>
			<LastPage></LastPage>
			<ELocationID EIdType="pii">31688</ELocationID>
			
			
			<Language>EN</Language>
<AuthorList>
</AuthorList>
				<PublicationType>Journal Article</PublicationType>
		    <Abstract>Herpes simplex virus type-1 (HSV-1) is a neurotropic pathogen of humans that establishes latent infection in the sensory ganglia innervating the site of primary infection. A number of genes control HSV-1 pathogenicity and latency. Open reading frame P (ORF P) is one of these genes that might have a role in latency and pathogenesis. A complication in the analysis of the role of ORF P in the HSV-1 life-cycle is an antisense overlapping gene, ICP34.5. ORF P is also deleted in ICP34.5 negative mutants and to date, no definite function is attributed to it. An approach to analyze the function of a viral gene such as ORF P is to determine if this gene interacts with any of the cellular and viral proteins both in vitro and in vivo. Therefore, in this work, using GST pulldown assay and Western-blotting, it was investigated that with which cellular and viral gene products ORF P interacts. Our results showed that ORF P interacted with Thymidine kinase (TK) and also with an unidentified cellular protein. Conclusively the results of these works to-gether suggest possible role for ORF P in both splicing and replication of HSV-1.</Abstract>
<ArchiveCopySource DocType="pdf">https://jsciences.ut.ac.ir/article_31688_7d1fb6b4eec12bee96b88020c7afadb8.pdf</ArchiveCopySource>
</Article>
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