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Virology. 2017 Jan 27;504:12-24. doi: 10.1016/j.virol.2017.01.013. [Epub ahead of print]

Normal human cell proteins that interact with the adenovirus type 5 E1B 55kDa protein.

Author information

  • 1Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
  • 2Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA. Electronic address: sjflint@princeton.edu.

Abstract

Several of the functions of the human adenovirus type 5 E1B 55kDa protein are fulfilled via the virus-specific E3 ubiquitin ligase it forms with the viral E4 Orf6 protein and several cellular proteins. Important substrates of this enzyme have not been identified, and other functions, including repression of transcription of interferon-sensitive genes, do not require the ligase. We therefore used immunoaffinity purification and liquid chromatography-mass spectrometry of lysates of normal human cells infected in parallel with HAdV-C5 and E1B 55kDa protein-null mutant viruses to identify specifically E1B 55kDa-associated proteins. The resulting set of >90 E1B-associated proteins contained the great majority identified previously, and was enriched for those associated with the ubiquitin-proteasome system, RNA metabolism and the cell cycle. We also report very severe inhibition of viral genome replication when cells were exposed to both specific or non-specific siRNAs and interferon prior to infection.

KEYWORDS:

E1B 55kDa protein; Human adenovirus type 5 (HAdV-C5); Mass spectrometry; Normal human cells; RNA metabolism; Type I interferons; Ubiquitin-proteasome system

PMID:
28135605
DOI:
10.1016/j.virol.2017.01.013
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