Natural variants of the human papillomavirus type 16 E6 protein differ in their abilities to alter keratinocyte differentiation and to induce p53 degradation
| Autor: | J Icenogle, Hubert Stöppler, M C Stöppler, Richard Schlegel, K Clancy, K Ching |
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| Rok vydání: | 1996 |
| Předmět: |
Keratinocytes
Oncogene Proteins Cellular differentiation Ubiquitin-Protein Ligases Immunology Molecular Sequence Data chemistry.chemical_element Repressor Calcium Biology Microbiology Viral Proteins Virology Humans Papillomaviridae chemistry.chemical_classification Base Sequence Gene Transfer Techniques Cell Differentiation Oncogene Proteins Viral biology.organism_classification Cell Transformation Viral Molecular biology In vitro Amino acid Cell biology N-terminus Repressor Proteins chemistry Insect Science Research Article |
| Zdroj: | Journal of virology. 70(10) |
| ISSN: | 0022-538X |
| Popis: | Three naturally occurring variant human papillomavirus type 16 (HPV-16) E6 proteins, which contained amino acid substitutions predominantly near the N terminus, exhibited significant differences in their abilities to abrogate keratinocyte differentiation in response to serum and calcium and to induce the degradation of p53 in vitro. One variant surpassed the reference E6 protein in its ability to abrogate keratinocyte differentiation responses, whereas another showed a reduction in this activity. Interestingly, the biological activities of the HPV-16 E6 proteins and their abilities to induce p53 degradation in vitro were directly correlated. These results demonstrate that naturally occurring variants of HPV-16 differ in biological and biochemical properties which might result in differences in pathogenicity. |
| Databáze: | OpenAIRE |
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