Different Isoforms of HPV-16 E7 Protein are Present in Cytoplasm and Nucleus

The E7 protein of high risk HPV types has been found with different molecular weights, mainly because of phosphorylation, an event that changes protein charge and mobility in SDS-PAGE. Distribution of E7 protein in the cellular compartments has also been subject of debate as some groups report the p...

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Detalles Bibliográficos
Autores principales: Valdovinos-Torres, H, Orozco-Morales, M, Pedroza-Saavedra, A, Padilla-Noriega, L, Esquivel-Guadarrama, F, Gutierrez-Xicotencatl, L
Formato: Texto
Lenguaje:English
Publicado: Bentham Science Publishers Ltd. 2008
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2678815/
https://www.ncbi.nlm.nih.gov/pubmed/19440460
http://dx.doi.org/10.2174/1874357900802010015
Descripción
Sumario:The E7 protein of high risk HPV types has been found with different molecular weights, mainly because of phosphorylation, an event that changes protein charge and mobility in SDS-PAGE. Distribution of E7 protein in the cellular compartments has also been subject of debate as some groups report the protein in nucleus and others in cytoplasm. The different subcellular distribution and molecular weights reported for the E7 protein suggest the presence of isoforms. We examined this possibility by using several antibodies that recognize different epitopes on the HPV-16 E7 protein. We showed that E7 is processed in 3 isoforms with different molecular weights and isoelectric points (IEP), and described as E7a1 (17.5 kDa, IEP 4.68), E7a (17 kDa, IEP 6.18) and E7b (16 kDa, IEP 6.96). The immunofluorescense results also showed that E7 is distributed into different compartments (ER, Golgi and nucleus), which suggest the presence of other posttranslational modifications, besides phosphorylation.

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