ArticleScientific reports2018
Felis catus papillomavirus type-2 E6 binds to E6AP, promotes E6AP/p53 binding and enhances p53 proteasomal degradation.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 41 citations in OpenAlex.
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- Feline oral squamous cell carcinoma: recent advances and future perspectives.Frontiers in veterinary science · 2025Review
- Papillomaviruses and Papillomaviral Disease in Dogs and Cats: A Comprehensive Review.Pathogens (Basel, Switzerland) · 2024Review
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- Feline papillomavirus-associated Merkel cell carcinoma: a comparative review with human Merkel cell carcinoma.The Journal of veterinary medical science · 2023Review
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- Feline oral squamous cell carcinoma andFrontiers in veterinary science · 2023Article
- Effectiveness of the Fungal Metabolite 3-Antibiotics (Basel, Switzerland) · 2022Article
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- Feline Oral Squamous Cell Carcinoma: A Critical Review of Etiologic Factors.Veterinary sciences · 2022Review
- Papillomaviral skin diseases of humans, dogs, cats and horses: A comparative review. Part 2: Pre-neoplastic and neoplastic diseases.Veterinary journal (London, England : 1997) · 2022Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
E6 from high risk human papillomaviruses (HR HPVs) promotes ubiquitination and degradation of p53 tumour suppressor by mediating its binding to ubiquitin ligase E6AP in a ternary complex, contributing to cell transformation in cervical cancer. We have previously shown that Felis catus papillomavirus type -2 (FcaPV-2) E6 is expressed in feline squamous cell carcinoma (SCC) and displays the ability to bind p53 and decrease its protein levels in transfected CRFK cells. However, the mechanism of p53 downregulation has not yet been characterized. Here we show that FcaPV-2 E6 bound to E6AP, which in turn was bound by p53 exclusively in cells expressing the viral oncoprotein (CRFKE6). Furthermore, p53 was highly poly-ubiquitinated and underwent accumulation upon E6AP gene knockdown in CRFKE6. Half-life experiments and proteasome inhibition treatments indicated that down-regulation of p53 protein in CRFKE6 was due to accelerated proteasomal degradation. E6AP/p53 binding was also demonstrated in two feline SCC cell lines expressing FcaPV-2 E6, where p53 protein levels and poly-ubiquitination degree were proportional to E6 mRNA levels. The data obtained in both artificial and spontaneous in vitro models suggest that FcaPV-2 E6 degrades p53 through a molecular mechanism similar to HR HPVs, possibly contributing to the development of feline SCC.
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