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Updated: Mar 8, 2026
RNAscope for In situ Detection of Transcriptionally Active Human Papillomavirus in Head and Neck Squamous Cell Carcinoma
Published on: March 11, 2014
Monitoring HPV-16 E7 phosphorylation events
Marcela O Nogueira1, Tomáš Hošek1, Eduardo O Calçada1
1Magnetic Resonance Center (CERM) and Department of Chemistry "Ugo Schiff", University of Florence, via Luigi Sacconi 6, Sesto Fiorentino, Italy.
Abstract:
HPV-16 E7 is one of the key proteins that, by interfering with the host metabolism through many protein-protein interactions, hijacks cell regulation and contributes to malignancy. Here we report the high resolution investigation of the CR3 region of HPV-16 E7, both as an isolated domain and in the full-length protein. This opens the way to the atomic level study of the many interactions in which HPV-16 E7 is involved. Along these lines we show here the effect of one of the key post-translational modifications of HPV-16 E7, the phosphorylation by casein kinase II.
Insights
High-resolution investigation of the Human Papillomavirus-16 (HPV-16) E7 protein
Area of Science:
- Structural biology
- Oncogenic protein research
- Molecular mechanisms of cancer
Background:
- Human Papillomavirus-16 (HPV-16) E7 protein is crucial in hijacking host cell regulation and promoting malignancy.
- Understanding HPV-16 E7's protein-protein interactions is key to studying its role in cancer development.
Purpose of the Study:
- To investigate the CR3 region of the HPV-16 E7 protein at high resolution.
- To explore the impact of phosphorylation by casein kinase II on HPV-16 E7.
Main Methods:
- High-resolution structural investigation of the CR3 region of HPV-16 E7.
- Analysis of both isolated domain and full-length HPV-16 E7 protein.
- Study of post-translational modifications, specifically phosphorylation by casein kinase II.
Main Results:
- Detailed high-resolution structural data of the HPV-16 E7 CR3 region was obtained.
- The study provides a foundation for atomic-level analysis of HPV-16 E7 interactions.
- The effect of casein kinase II phosphorylation on HPV-16 E7 was demonstrated.
Conclusions:
- High-resolution structural insights into HPV-16 E7, particularly the CR3 region, are now available.
- This work facilitates detailed atomic-level studies of HPV-16 E7's interactions.
- The study highlights the significance of post-translational modifications like phosphorylation in HPV-16 E7 function.
