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- W2026842365 abstract "Infected cell protein (ICP) 27 is an essential herpes simplex virus type 1 (HSV-1) phosphoprotein required for optimal viral DNA and early or late gene synthesis. Three slow-migrating immunoreactive species were detected using multiple anti-ICP27 antibodies following HSV-1 infection of HEp-2 and Vero cells in the presence of cycloheximide (CHX). Generation of the protein triplet moieties required transcription of the α27 gene. These forms were observed following infection with a series of recombinant viruses that produce truncated ICP27 polypeptides, suggesting that alternative splicing is not involved in the process. These ICP27 species were not observed following translation inhibition by puromycin (PUR). Synthesis of the triplet occurred by 6 hpi and CHX addition as late as 3 hpi still enabled their production. That the ICP27 species were detected in uninfected ICP27-expressing cells without CHX, but not in its presence, suggests a mechanism in which virus infection is required to produce the forms when ribosomal aminoacyl-transfer RNA (tRNA) translocation is blocked." @default.
- W2026842365 created "2016-06-24" @default.
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- W2026842365 date "2004-07-01" @default.
- W2026842365 modified "2023-09-27" @default.
- W2026842365 title "Herpes simplex virus 1 infection is required to produce ICP27 immunoreactive triplet forms when ribosomal aminoacyl-tRNA translocation is blocked by cycloheximide" @default.
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- W2026842365 doi "https://doi.org/10.1016/j.virol.2004.04.011" @default.
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