Structural Class I viroporin characteristics displayed by p33.
<p>A) The TMD of p33 compared with that of three known viroporins (IAV M2, HIV-1 Vpu, and SARS-CoV E) representing the underlined TMD, the short external domains (ED) and longer cytoplasmic domains (CD), with cytoplasmic TMD-adjacent basic residues colored in red. B) Western blot of the crude...
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2025
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| _version_ | 1849927641305448448 |
|---|---|
| author | Vicken Aknadibossian (22676694) |
| author2 | Clare Stokes (816556) Roger L. Papke (685990) Hao Wei Teh (22676697) Ying Wang (11406) Svetlana Y. Folimonova (8786570) |
| author2_role | author author author author author |
| author_facet | Vicken Aknadibossian (22676694) Clare Stokes (816556) Roger L. Papke (685990) Hao Wei Teh (22676697) Ying Wang (11406) Svetlana Y. Folimonova (8786570) |
| author_role | author |
| dc.creator.none.fl_str_mv | Vicken Aknadibossian (22676694) Clare Stokes (816556) Roger L. Papke (685990) Hao Wei Teh (22676697) Ying Wang (11406) Svetlana Y. Folimonova (8786570) |
| dc.date.none.fl_str_mv | 2025-11-24T18:34:50Z |
| dc.identifier.none.fl_str_mv | 10.1371/journal.ppat.1013730.g001 |
| dc.relation.none.fl_str_mv | https://figshare.com/articles/figure/Structural_Class_I_viroporin_characteristics_displayed_by_p33_/30697722 |
| dc.rights.none.fl_str_mv | CC BY 4.0 info:eu-repo/semantics/openAccess |
| dc.subject.none.fl_str_mv | Biophysics Biochemistry Medicine Microbiology Cell Biology Ecology Infectious Diseases Plant Biology Virology Biological Sciences not elsewhere classified substantial structural similarities ion channel properties ion channel activity form ion channels closterovirus tristezae </ alphainfluenzavirus influenzae </ div >< p citrus tristeza virus lowered membrane potentials host ion homeostasis discuss additional characteristics m2 protein encoded viroporin </ p plant virus viroporin plant virus viroporins plant virus xenopus </ viroporin encoded influenza virus viral proteins using two using confocal third report study represents significantly lagged research focusing present evidence first validation favorable environments electron microscopy cytoplasmic domains associated protein >), possesses |
| dc.title.none.fl_str_mv | Structural Class I viroporin characteristics displayed by p33. |
| dc.type.none.fl_str_mv | Image Figure info:eu-repo/semantics/publishedVersion image |
| description | <p>A) The TMD of p33 compared with that of three known viroporins (IAV M2, HIV-1 Vpu, and SARS-CoV E) representing the underlined TMD, the short external domains (ED) and longer cytoplasmic domains (CD), with cytoplasmic TMD-adjacent basic residues colored in red. B) Western blot of the crude extracts of <i>N. benthamiana</i> leaves agroinfiltrated with either a p33-expressing (p33) or an empty vector (EV) construct carried out with an anti-p33 primary antibody. The p33 loaded lane displayed protein bands, which correspond to the expected sizes of p33 monomers, dimers, and tetramers. Ponceau S staining was used to display the amount of loaded protein in the p33 and EV lanes. M: Molecular marker. C) AlphaFold3 prediction of the tetrameric p33 TMD with the two amino acids on the preceding CD and succeeding ED domains. The blue color of the helices indicates a confident pIDDT score for the p33 TMD and the PAE heatmap displays the confidence of the position of the four p33 TMD monomers with respect to each other in the model. D) AlphaFold3 predicted aligned error for the residues at the binding interface between the p33 TMD monomers.</p> |
| eu_rights_str_mv | openAccess |
| id | Manara_77ab73ee947ad5663b52d9762bff3911 |
| identifier_str_mv | 10.1371/journal.ppat.1013730.g001 |
| network_acronym_str | Manara |
| network_name_str | ManaraRepo |
| oai_identifier_str | oai:figshare.com:article/30697722 |
| publishDate | 2025 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | CC BY 4.0 |
| spelling | Structural Class I viroporin characteristics displayed by p33.Vicken Aknadibossian (22676694)Clare Stokes (816556)Roger L. Papke (685990)Hao Wei Teh (22676697)Ying Wang (11406)Svetlana Y. Folimonova (8786570)BiophysicsBiochemistryMedicineMicrobiologyCell BiologyEcologyInfectious DiseasesPlant BiologyVirologyBiological Sciences not elsewhere classifiedsubstantial structural similaritiesion channel propertiesion channel activityform ion channelsclosterovirus tristezae </alphainfluenzavirus influenzae </div >< pcitrus tristeza viruslowered membrane potentialshost ion homeostasisdiscuss additional characteristicsm2 protein encodedviroporin </ pplant virus viroporinplant virus viroporinsplant virusxenopus </viroporin encodedinfluenza virusviral proteinsusing twousing confocalthird reportstudy representssignificantly laggedresearch focusingpresent evidencefirst validationfavorable environmentselectron microscopycytoplasmic domainsassociated protein>), possesses<p>A) The TMD of p33 compared with that of three known viroporins (IAV M2, HIV-1 Vpu, and SARS-CoV E) representing the underlined TMD, the short external domains (ED) and longer cytoplasmic domains (CD), with cytoplasmic TMD-adjacent basic residues colored in red. B) Western blot of the crude extracts of <i>N. benthamiana</i> leaves agroinfiltrated with either a p33-expressing (p33) or an empty vector (EV) construct carried out with an anti-p33 primary antibody. The p33 loaded lane displayed protein bands, which correspond to the expected sizes of p33 monomers, dimers, and tetramers. Ponceau S staining was used to display the amount of loaded protein in the p33 and EV lanes. M: Molecular marker. C) AlphaFold3 prediction of the tetrameric p33 TMD with the two amino acids on the preceding CD and succeeding ED domains. The blue color of the helices indicates a confident pIDDT score for the p33 TMD and the PAE heatmap displays the confidence of the position of the four p33 TMD monomers with respect to each other in the model. D) AlphaFold3 predicted aligned error for the residues at the binding interface between the p33 TMD monomers.</p>2025-11-24T18:34:50ZImageFigureinfo:eu-repo/semantics/publishedVersionimage10.1371/journal.ppat.1013730.g001https://figshare.com/articles/figure/Structural_Class_I_viroporin_characteristics_displayed_by_p33_/30697722CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/306977222025-11-24T18:34:50Z |
| spellingShingle | Structural Class I viroporin characteristics displayed by p33. Vicken Aknadibossian (22676694) Biophysics Biochemistry Medicine Microbiology Cell Biology Ecology Infectious Diseases Plant Biology Virology Biological Sciences not elsewhere classified substantial structural similarities ion channel properties ion channel activity form ion channels closterovirus tristezae </ alphainfluenzavirus influenzae </ div >< p citrus tristeza virus lowered membrane potentials host ion homeostasis discuss additional characteristics m2 protein encoded viroporin </ p plant virus viroporin plant virus viroporins plant virus xenopus </ viroporin encoded influenza virus viral proteins using two using confocal third report study represents significantly lagged research focusing present evidence first validation favorable environments electron microscopy cytoplasmic domains associated protein >), possesses |
| status_str | publishedVersion |
| title | Structural Class I viroporin characteristics displayed by p33. |
| title_full | Structural Class I viroporin characteristics displayed by p33. |
| title_fullStr | Structural Class I viroporin characteristics displayed by p33. |
| title_full_unstemmed | Structural Class I viroporin characteristics displayed by p33. |
| title_short | Structural Class I viroporin characteristics displayed by p33. |
| title_sort | Structural Class I viroporin characteristics displayed by p33. |
| topic | Biophysics Biochemistry Medicine Microbiology Cell Biology Ecology Infectious Diseases Plant Biology Virology Biological Sciences not elsewhere classified substantial structural similarities ion channel properties ion channel activity form ion channels closterovirus tristezae </ alphainfluenzavirus influenzae </ div >< p citrus tristeza virus lowered membrane potentials host ion homeostasis discuss additional characteristics m2 protein encoded viroporin </ p plant virus viroporin plant virus viroporins plant virus xenopus </ viroporin encoded influenza virus viral proteins using two using confocal third report study represents significantly lagged research focusing present evidence first validation favorable environments electron microscopy cytoplasmic domains associated protein >), possesses |