Different Isoforms of HPV-16 E7 Protein are Present in Cytoplasm and Nucleus
H Valdovinos-Torres1, M Orozco-Morales1, A Pedroza-Saavedra1, L Padilla-Noriega3, F Esquivel-Guadarrama2, L Gutierrez-Xicotencatl*, 1
Identifiers and Pagination:Year: 2008
First Page: 15
Last Page: 23
Publisher Id: TOVJ-2-15
Article History:Received Date: 29/1/2008
Revision Received Date: 14/2/2008
Acceptance Date: 5/3/2008
Electronic publication date: 26/3/2008
Collection year: 2008
open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.5/), which permits unrestrictive use, distribution, and reproduction in any medium, provided the original work is properly cited.
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.