Proteomic analysis of the gamma human papillomavirus type 197 E6 and E7 associated cellular proteins

Abstract Gamma HPV197 was the most frequently identified HPV when human skin cancer specimens were analyzed by deep sequencing (Arroyo Muhr et al., Int. J. Cancer 136: 2546-55, 2015). To gain insight into the biological activities of HPV197, we investigated the cellular interactomes of HPV197 E6 and...

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Veröffentlicht in:	Virology (New York, N.Y.) N.Y.), 2017-01, Vol.500, p.71-81
Hauptverfasser:	Grace, Miranda, Munger, Karl
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Gammapapillomavirus - chemistry Gammapapillomavirus - classification Gammapapillomavirus - genetics Gammapapillomavirus - metabolism Human Papillomavirus Humans Infectious Disease Molecular Sequence Data Oncogene Proteins, Viral - chemistry Oncogene Proteins, Viral - genetics Oncogene Proteins, Viral - metabolism p53 tumor suppressor Papillomavirus E7 Proteins - chemistry Papillomavirus E7 Proteins - genetics Papillomavirus E7 Proteins - metabolism Papillomavirus Infections - genetics Papillomavirus Infections - metabolism Papillomavirus Infections - virology Protein Binding Proteomics Sequence Alignment Skin Cancer Transcription Factors - genetics Transcription Factors - metabolism Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism
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Zusammenfassung:	Abstract Gamma HPV197 was the most frequently identified HPV when human skin cancer specimens were analyzed by deep sequencing (Arroyo Muhr et al., Int. J. Cancer 136: 2546-55, 2015). To gain insight into the biological activities of HPV197, we investigated the cellular interactomes of HPV197 E6 and E7. HPV197 E6 protein interacts with a broad spectrum of cellular LXXLL domain proteins, including UBE3A and MAML1. HPV197 E6 also binds and inhibits the TP53 tumor suppressor and interacts with the CCR4-NOT ubiquitin ligase and deadenylation complex. Despite lacking a canonical retinoblastoma (RB1) tumor suppressor binding site, HPV197 E7 binds RB1 and activates E2F transcription. Hence, HPV197 E6 and E7 proteins interact with a similar set of cellular proteins as E6 and E7 proteins encoded by HPVs that have been linked to human carcinogenesis and/or have transforming activities in vitro.
ISSN:	0042-6822 1096-0341
DOI:	10.1016/j.virol.2016.10.010