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Interaction of the Human Papillomavirus E6 Oncoprotein with Sorting Nexin 27 Modulates Endocytic Cargo Transport Pathways

Ganti, Ketaki, Massimi, Paola, Manzo-Merino, Joaquin, Tomaić, Vjekoslav, Pim, David, Playford, Martin P., Lizano, Marcela, Roberts, Sally, Kranjec, Christian, Doorbar, John, Banks, Lawrence·2016·PLOS Pathogens
DOI 10.1371/journal.ppat.1005854PMC PMC5029876
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Fig 1 SNX27 interacts with multiple high-risk HPV E6 proteins. Panel A: SNX27 and MAGI-1 were translated and radio-labelled in vitro using the TNT Coupled Reticulocyte Lysate System (Promega). The translated proteins were then incubated with purified GST-tagged HPV E6s as indicated. The arrows indicate the position of MAGI-1 and SNX27 on the autoradiograms, which show the levels of bound and input proteins. The Coomassie Blue staining shows loading of the purified GST proteins, with the arrows indicating the position of GST and the GST tagged E6s. Panel B: SNX27 was translated and radio-labelled in vitro using the TNT Coupled Reticulocyte Lysate System (Promega). The translated proteins were then incubated with purified GST alone, GST-HPV18 E6 or GST-HPV11 E6 as indicated, with the upper panel showing the autoradiogram of bound and input SNX27. The Coomassie Blue staining shows loading of the purified GST proteins. Arrows indicate the position of GST and the GST-tagged E6s. Panel C: SNX27 was translated and radio-labelled in vitro using the TNT Coupled Reticulocyte Lysate System (Promega). The translated proteins were then incubated with purified GST alone, GST-HPV16 E6, GST-HPV18 E6 or the GST-HPV18 E6 T156E mutant as indicated. The upper panel shows the autoradiogram of bound and input proteins with the arrows indicating the position of SNX27. The Coomassie Blue staining shows loading of the purified GST proteins, with the arrows indicating the position of GST and the GST-tagged E6s.
Fig 1 SNX27 interacts with multiple high-risk HPV E6 proteins. Panel A: SNX27 and MAGI-1 were translated and radio-labelled in vitro using the TNT Coupled Reticulocyte Lysate System (Promega). The translated proteins were then incubated with purified GST-tagged HPV E6s as indicated. The arrows indicate the position of MAGI-1 and SNX27 on the autoradiograms, which show the levels of bound and input proteins. The Coomassie Blue staining shows loading of the purified GST proteins, with the arrows indicating the position of GST and the GST tagged E6s. Panel B: SNX27 was translated and radio-labelled in vitro using the TNT Coupled Reticulocyte Lysate System (Promega). The translated proteins were then incubated with purified GST alone, GST-HPV18 E6 or GST-HPV11 E6 as indicated, with the upper panel showing the autoradiogram of bound and input SNX27. The Coomassie Blue staining shows loading of the purified GST proteins. Arrows indicate the position of GST and the GST-tagged E6s. Panel C: SNX27 was translated and radio-labelled in vitro using the TNT Coupled Reticulocyte Lysate System (Promega). The translated proteins were then incubated with purified GST alone, GST-HPV16 E6, GST-HPV18 E6 or the GST-HPV18 E6 T156E mutant as indicated. The upper panel shows the autoradiogram of bound and input proteins with the arrows indicating the position of SNX27. The Coomassie Blue staining shows loading of the purified GST proteins, with the arrows indicating the position of GST and the GST-tagged E6s.CC0 · PubMed Central
Fig 2 Interaction between HPV-18 E6 and SNX27 involves PBM-PDZ recognition. Panel A: The C-terminal HPV 18E6 mutants were translated and radio-labelled in vitro using the TNT Coupled Reticulocyte Lysate System (Promega). The translated proteins were then incubated with purified GST alone or GST-tagged SNX27 as indicated. The top panel shows input levels of the different HPV E6 mutants. The lower pairs of panels show the Coomassie stained gels of input GST and GST-SNX27 (lower panel in each pair) and the autoradiograms of the bound E6 (upper panel in each pair). Panel B: Wild type SNX27 and the various SNX27 deletion mutants was translated in vitro in rabbit reticulocyte lysate and radio labelled using the TNT Coupled Reticulocyte Lysate System (Promega). The translated proteins were then incubated with purified GST alone, GST-HPV18 E6 or the GST-HPV18 E6ΔPBM mutant as indicated. The arrows indicate the position of SNX27 on the autoradiograms, showing the levels of input and bound proteins. The Coomaasie Blue staining shows loading of the purified GST proteins.
Fig 2 Interaction between HPV-18 E6 and SNX27 involves PBM-PDZ recognition. Panel A: The C-terminal HPV 18E6 mutants were translated and radio-labelled in vitro using the TNT Coupled Reticulocyte Lysate System (Promega). The translated proteins were then incubated with purified GST alone or GST-tagged SNX27 as indicated. The top panel shows input levels of the different HPV E6 mutants. The lower pairs of panels show the Coomassie stained gels of input GST and GST-SNX27 (lower panel in each pair) and the autoradiograms of the bound E6 (upper panel in each pair). Panel B: Wild type SNX27 and the various SNX27 deletion mutants was translated in vitro in rabbit reticulocyte lysate and radio labelled using the TNT Coupled Reticulocyte Lysate System (Promega). The translated proteins were then incubated with purified GST alone, GST-HPV18 E6 or the GST-HPV18 E6ΔPBM mutant as indicated. The arrows indicate the position of SNX27 on the autoradiograms, showing the levels of input and bound proteins. The Coomaasie Blue staining shows loading of the purified GST proteins.CC0 · PubMed Central
Fig 3 HPV-18 E6 resides primarily within the membrane fraction of HeLa cells. The stably transfected HeLa S4 shSNX27 cells were treated with Doxycycline (DOX) or DMSO for 72 hours. The cells were then treated with the proteosome inhibitor MG132 or control DMSO, as indicated, for a further 3 hours. The cells were then harvested and cytoplasmic, membrane, nuclear and cytoskeletal fractions were prepared using the ProteoExtract Cell Fractionation Kit (Calbiochem). The fractions were run on SDS polyacrylamide gels and HPV-18 E6 and SNX27 detected by western blotting. The arrows indicate the position of SNX27, HPV-18 E6, and the markers of the different fractions: α-Tubulin (cytoplasmic), Transferrin Receptor (membrane), p84 (nuclear) and Vimentin (cytoskeletal).
Fig 3 HPV-18 E6 resides primarily within the membrane fraction of HeLa cells. The stably transfected HeLa S4 shSNX27 cells were treated with Doxycycline (DOX) or DMSO for 72 hours. The cells were then treated with the proteosome inhibitor MG132 or control DMSO, as indicated, for a further 3 hours. The cells were then harvested and cytoplasmic, membrane, nuclear and cytoskeletal fractions were prepared using the ProteoExtract Cell Fractionation Kit (Calbiochem). The fractions were run on SDS polyacrylamide gels and HPV-18 E6 and SNX27 detected by western blotting. The arrows indicate the position of SNX27, HPV-18 E6, and the markers of the different fractions: α-Tubulin (cytoplasmic), Transferrin Receptor (membrane), p84 (nuclear) and Vimentin (cytoskeletal).CC0 · PubMed Central
Fig 4 SNX27 accumulates in close proximity to retromer components in the absence of E6. HeLa cells were transfected with siRNA against Luciferase (siLuc), HPV-18 E6 (siE6), HPV-18 E6/E7 (siE6/E7) or E6AP (siE6AP) for 72 hours and the cells were then fixed using 4% Paraformaldehyde followed by permeabilization with PBS containing 0.1% Triton X-100. The cells were then stained for Vps35 (red) SNX27 (green) and p53 (blue) by indirect immunofluorescence. The images were acquired using the LSM 510 META Confocal Microscope (Carl Zeiss) and co-localisation between Vps35 and SNX27 was quantified by Velocity Software, with PCC values shown at the right hand side. Note the marked increase in co-localisation between SNX27 and Vps35 (given as Pearson’s Correlation Coefficient (PCC)) following ablation of E6, E6/E7 and E6AP.
Fig 4 SNX27 accumulates in close proximity to retromer components in the absence of E6. HeLa cells were transfected with siRNA against Luciferase (siLuc), HPV-18 E6 (siE6), HPV-18 E6/E7 (siE6/E7) or E6AP (siE6AP) for 72 hours and the cells were then fixed using 4% Paraformaldehyde followed by permeabilization with PBS containing 0.1% Triton X-100. The cells were then stained for Vps35 (red) SNX27 (green) and p53 (blue) by indirect immunofluorescence. The images were acquired using the LSM 510 META Confocal Microscope (Carl Zeiss) and co-localisation between Vps35 and SNX27 was quantified by Velocity Software, with PCC values shown at the right hand side. Note the marked increase in co-localisation between SNX27 and Vps35 (given as Pearson’s Correlation Coefficient (PCC)) following ablation of E6, E6/E7 and E6AP.CC0 · PubMed Central
Fig 5 HPV-16 E6 modulation of SNX27 localisation is PBM-dependent. Control NIKS, NIKS expressing HPV-16 E6 and NIKS expressing the HPV-16 E6 ΔPBM mutant were fixed using 4% Paraformaldehyde followed by permeabilization with PBS containing 0.1% Triton X-100. The cells were then stained for Vps35 (red), SNX27 (green) and p53 (red) by indirect immunofluorescence. The images were acquired using the LSM 510 META Confocal Microscope (Carl Zeiss) and co-localisation between Vps35 and SNX27 quantified by Velocity Software, with PCC values shown at the right hand side. Note the marked increase in co-localisation between SNX27 and Vps35 in the control NIKS and NIKS containing E6ΔPBM.
Fig 5 HPV-16 E6 modulation of SNX27 localisation is PBM-dependent. Control NIKS, NIKS expressing HPV-16 E6 and NIKS expressing the HPV-16 E6 ΔPBM mutant were fixed using 4% Paraformaldehyde followed by permeabilization with PBS containing 0.1% Triton X-100. The cells were then stained for Vps35 (red), SNX27 (green) and p53 (red) by indirect immunofluorescence. The images were acquired using the LSM 510 META Confocal Microscope (Carl Zeiss) and co-localisation between Vps35 and SNX27 quantified by Velocity Software, with PCC values shown at the right hand side. Note the marked increase in co-localisation between SNX27 and Vps35 in the control NIKS and NIKS containing E6ΔPBM.CC0 · PubMed Central
Fig 6 HPV-18 E6 exists in a complex with SNX27 and the retromer in HeLa cells. Panel A Left. HeLa cell extracts were incubated with anti-HPV-18 E6 monoclonal antibody or anti-HA monoclonal antibody as a negative control and the immune complexes were precipitated using Protein A Sepharose beads. The beads were washed and then loaded onto SDS polyacrylamide gels and co-immunoprecipitating proteins detected by SDS-PAGE followed by western blotting. The arrows indicate the position of SNX27, E6 and Vps35, with the upper three panels showing the levels of input proteins and the lower panels showing the immunoprecipitates. Panel A Right. HeLa cells were treated with siRNA against Luciferase as control or against HPV-18 E6 for 72 hours. Membrane fractions were prepared using the ProteoExtract Cell Fractionation Kit (Calbiochem) and then incubated with anti-SNX27 antibody and immune complexes were precipitated using Protein A Sepharose beads. The beads were washed, loaded onto SDS polyacrylamide gels and immunoprecipitating proteins detected by western blotting. The arrows indicate the position of SNX27 andVps35, with the upper two panels showing protein inputs and the two lower panels showing the immunoprecipitation. Panel B. HeLa cells were transfected with siE6/E7 or scrambled siRNA (siScr) and after 72hrs cells were harvested and immunoprecipitated using non-specific antibody or anti-SNX27. Complexes were then analysed by western blotting for HPV-18 E6 (anti-18 E6) and SNX27. Arrows indicate the positions of SNX27 and E6 together with the IgG heavy chain and a short and long exposure of the anti-18E6 western blot is provided for further clarity. Input proteins are also shown.
Fig 6 HPV-18 E6 exists in a complex with SNX27 and the retromer in HeLa cells. Panel A Left. HeLa cell extracts were incubated with anti-HPV-18 E6 monoclonal antibody or anti-HA monoclonal antibody as a negative control and the immune complexes were precipitated using Protein A Sepharose beads. The beads were washed and then loaded onto SDS polyacrylamide gels and co-immunoprecipitating proteins detected by SDS-PAGE followed by western blotting. The arrows indicate the position of SNX27, E6 and Vps35, with the upper three panels showing the levels of input proteins and the lower panels showing the immunoprecipitates. Panel A Right. HeLa cells were treated with siRNA against Luciferase as control or against HPV-18 E6 for 72 hours. Membrane fractions were prepared using the ProteoExtract Cell Fractionation Kit (Calbiochem) and then incubated with anti-SNX27 antibody and immune complexes were precipitated using Protein A Sepharose beads. The beads were washed, loaded onto SDS polyacrylamide gels and immunoprecipitating proteins detected by western blotting. The arrows indicate the position of SNX27 andVps35, with the upper two panels showing protein inputs and the two lower panels showing the immunoprecipitation. Panel B. HeLa cells were transfected with siE6/E7 or scrambled siRNA (siScr) and after 72hrs cells were harvested and immunoprecipitated using non-specific antibody or anti-SNX27. Complexes were then analysed by western blotting for HPV-18 E6 (anti-18 E6) and SNX27. Arrows indicate the positions of SNX27 and E6 together with the IgG heavy chain and a short and long exposure of the anti-18E6 western blot is provided for further clarity. Input proteins are also shown.CC0 · PubMed Central
Fig 7 Loss of HPV-18 E6 alters GLUT-1 levels in HeLa cells. HeLa S4 cells were treated with siRNA against Luciferase, HPV-18 E6/E7 or DOX to induce SNX27 shRNA for 72 hours. The cells were then harvested and levels of GLUT-1 expression analysed by western blotting. Slower migrating forms of GLUT-1 are indicated by the brackets. Knock down of E6 and SNX27 were verified by western blotting for p53 and SNX27 respectively. The lower panel shows γ-tubulin as the loading control.
Fig 7 Loss of HPV-18 E6 alters GLUT-1 levels in HeLa cells. HeLa S4 cells were treated with siRNA against Luciferase, HPV-18 E6/E7 or DOX to induce SNX27 shRNA for 72 hours. The cells were then harvested and levels of GLUT-1 expression analysed by western blotting. Slower migrating forms of GLUT-1 are indicated by the brackets. Knock down of E6 and SNX27 were verified by western blotting for p53 and SNX27 respectively. The lower panel shows γ-tubulin as the loading control.CC0 · PubMed Central
Fig 8 The loss of HPV-18 E6 in HeLa cells leads to an altered distribution of SNX27 and GLUT-1 cargo within endocytic compartments. HeLa cells were treated with siRNA against Luciferase or E6 for 72 hours and post nuclear extracts were loaded onto 5–25% OptiPrep gradients. The collected fractions were loaded on 12% SDS polyacrylamide gels followed by Western Blotting. The arrows indicate the position of GLUT-1, SNX27, p53 as a control for E6 knock down, but which was undetectable in the siLuc transfected cells, Rab4, Vps35 and LAMP2. The upper white arrows indicates the higher molecular weight forms of GLUT-1 that are absent following the loss of E6.
Fig 8 The loss of HPV-18 E6 in HeLa cells leads to an altered distribution of SNX27 and GLUT-1 cargo within endocytic compartments. HeLa cells were treated with siRNA against Luciferase or E6 for 72 hours and post nuclear extracts were loaded onto 5–25% OptiPrep gradients. The collected fractions were loaded on 12% SDS polyacrylamide gels followed by Western Blotting. The arrows indicate the position of GLUT-1, SNX27, p53 as a control for E6 knock down, but which was undetectable in the siLuc transfected cells, Rab4, Vps35 and LAMP2. The upper white arrows indicates the higher molecular weight forms of GLUT-1 that are absent following the loss of E6.CC0 · PubMed Central
Fig 9 GLUT-1 distribution is modulated by E6 in a PBM-dependent manner. Panel A. Control NIKS, NIKS expressing HPV-16 E6 and NIKS expressing the HPV-16 E6ΔPBM mutant were fixed using 4% paraformaldehyde followed by permeabilization with PBS containing 0.1% Triton X-100. The cells were then stained for p53 (blue), Vps35 (red) and GLUT-1 (green) by indirect immunofluorescence. Co-localisation between Vps35 and GLUT-1 was measured using Velocity software and POC values are shown at the right. Panel B: HeLa and SiHa cells were transfected with siRNA against Luciferase, HPV-18 E6 or E6AP as indicated for 72 hours and the cells were then fixed using 4% paraformaldehyde followed by permeabilization with PBS containing 0.1% Triton X-100. The cells were then stained for Vps35 (red), GLUT-1 (green) and p53 (blue) by indirect immunofluorescence. The images were acquired using the LSM 510 META Confocal Microscope (Carl Zeiss). Co-localisation between GLUT1 and Vps35 was measured using Velocity software and PCC values are shown at the right hand side. Panel C: HeLa cells were transfected with siRNA against Luciferase or HPV-18 E6/E7 or E6AP for 72 hours and the cells were then fixed using 4% Paraformaldehyde followed by permeabilization with PBS containing 0.1% Triton X-100. The cells were then stained for Vps35 (red), Rab4 (green) and p53 (blue) by indirect immunofluorescence. The images were acquired using the LSM 510 META Confocal Microscope (Carl Zeiss). Co-localisation between GLUT-1 and Rab4 was measured using Velocity software and PCC values are shown at the right hand side.
Fig 9 GLUT-1 distribution is modulated by E6 in a PBM-dependent manner. Panel A. Control NIKS, NIKS expressing HPV-16 E6 and NIKS expressing the HPV-16 E6ΔPBM mutant were fixed using 4% paraformaldehyde followed by permeabilization with PBS containing 0.1% Triton X-100. The cells were then stained for p53 (blue), Vps35 (red) and GLUT-1 (green) by indirect immunofluorescence. Co-localisation between Vps35 and GLUT-1 was measured using Velocity software and POC values are shown at the right. Panel B: HeLa and SiHa cells were transfected with siRNA against Luciferase, HPV-18 E6 or E6AP as indicated for 72 hours and the cells were then fixed using 4% paraformaldehyde followed by permeabilization with PBS containing 0.1% Triton X-100. The cells were then stained for Vps35 (red), GLUT-1 (green) and p53 (blue) by indirect immunofluorescence. The images were acquired using the LSM 510 META Confocal Microscope (Carl Zeiss). Co-localisation between GLUT1 and Vps35 was measured using Velocity software and PCC values are shown at the right hand side. Panel C: HeLa cells were transfected with siRNA against Luciferase or HPV-18 E6/E7 or E6AP for 72 hours and the cells were then fixed using 4% Paraformaldehyde followed by permeabilization with PBS containing 0.1% Triton X-100. The cells were then stained for Vps35 (red), Rab4 (green) and p53 (blue) by indirect immunofluorescence. The images were acquired using the LSM 510 META Confocal Microscope (Carl Zeiss). Co-localisation between GLUT-1 and Rab4 was measured using Velocity software and PCC values are shown at the right hand side.CC0 · PubMed Central
Fig 10 Modulation of glucose uptake and cell proliferation by E6 and SNX27. Panel A. HeLa cells were treated with siRNA against Luciferase or HPV-18 E6 for 72 hours and glucose uptake was analyzed using the glucose analog 2-deoxyglucose (2-DG) using the Colorimetric Glucose Uptake Assay Kit (Abcam) according to the manufacturer’s instructions. The graph shows the cumulative results of three independent experiments, with 2-DG uptake measured in pmol/μl. Error bars represent standard deviations with a p-value < 0.05. Panel B. Control HeLa cells and HeLa S4 DOX inducible shRNA SNX27 cells were plated in medium containing low or high glucose in the presence and absence of DOX as indicated. Cells were then counted over a period of 4 days and the numbers represent the means from three independent assays. Standard deviations are shown.
Fig 10 Modulation of glucose uptake and cell proliferation by E6 and SNX27. Panel A. HeLa cells were treated with siRNA against Luciferase or HPV-18 E6 for 72 hours and glucose uptake was analyzed using the glucose analog 2-deoxyglucose (2-DG) using the Colorimetric Glucose Uptake Assay Kit (Abcam) according to the manufacturer’s instructions. The graph shows the cumulative results of three independent experiments, with 2-DG uptake measured in pmol/μl. Error bars represent standard deviations with a p-value < 0.05. Panel B. Control HeLa cells and HeLa S4 DOX inducible shRNA SNX27 cells were plated in medium containing low or high glucose in the presence and absence of DOX as indicated. Cells were then counted over a period of 4 days and the numbers represent the means from three independent assays. Standard deviations are shown.CC0 · PubMed Central

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Cited by

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Metadata

Authors
Ganti, K., Massimi, P., Manzo-Merino, J., Tomaić, V., Pim, D., Playford, M. P., Lizano, M., Roberts, S., Kranjec, C., Doorbar, J., & Banks, L.
Venue
PLOS Pathogens
Publisher
Public Library of Science (PLoS)
Published
2016-09-20
Volume
12
Issue
9
Pages
e1005854
ISSN
1553-7374
DOI
10.1371/journal.ppat.1005854
PMC
PMC5029876
Cited by
50
References
5
Language
en
Licence
creativecommons.org/publicdomain/zero/1.0/ (vor)
Funders
  • Associazione Italiana per la Ricerca sul Cancro (0923450/Z10/Z)
  • Wellcome Trust (09345/B/10/Z)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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