Biochemical investigation of wild-type and processed RNG2.
<p><b>(A)</b> Representation of the RNG2 constructs expressed in SF9 insect cells. <b>(B)</b> Insect cell protein expression and solubility of the RNG2 truncation variants, as assessed by Coomassie blue staining. <b>(C)</b> Protein expression and solubility...
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| _version_ | 1849927642213515264 |
|---|---|
| author | Romuald Haase (22339777) |
| author2 | Bingjian Ren (22676577) Albert Tell i Puig (22676580) Alessandro Bonavoglia (19415718) Jean-Baptiste Marq (375239) Rémy Visentin (22676583) Nicolas Dos Santos Pacheco (22676586) Bohumil Maco (383443) Ricardo Mondragón-Flores (10737057) Oscar Vadas (2416228) Dominique Soldati-Favre (79026) |
| author2_role | author author author author author author author author author author |
| author_facet | Romuald Haase (22339777) Bingjian Ren (22676577) Albert Tell i Puig (22676580) Alessandro Bonavoglia (19415718) Jean-Baptiste Marq (375239) Rémy Visentin (22676583) Nicolas Dos Santos Pacheco (22676586) Bohumil Maco (383443) Ricardo Mondragón-Flores (10737057) Oscar Vadas (2416228) Dominique Soldati-Favre (79026) |
| author_role | author |
| dc.creator.none.fl_str_mv | Romuald Haase (22339777) Bingjian Ren (22676577) Albert Tell i Puig (22676580) Alessandro Bonavoglia (19415718) Jean-Baptiste Marq (375239) Rémy Visentin (22676583) Nicolas Dos Santos Pacheco (22676586) Bohumil Maco (383443) Ricardo Mondragón-Flores (10737057) Oscar Vadas (2416228) Dominique Soldati-Favre (79026) |
| dc.date.none.fl_str_mv | 2025-11-24T18:31:05Z |
| dc.identifier.none.fl_str_mv | 10.1371/journal.pbio.3003506.g002 |
| dc.relation.none.fl_str_mv | https://figshare.com/articles/figure/Biochemical_investigation_of_wild-type_and_processed_RNG2_/30697353 |
| dc.rights.none.fl_str_mv | CC BY 4.0 info:eu-repo/semantics/openAccess |
| dc.subject.none.fl_str_mv | Biophysics Biochemistry Microbiology Cell Biology Physiology Infectious Diseases Environmental Sciences not elsewhere classified Biological Sciences not elsewhere classified Physical Sciences not elsewhere classified toxoplasma gondii </ remains apically anchored heterologous expression systems div >< p apical polar ring biochemical analysis revealed proper conoid anchorage ensures conoid functionality less parasites revealed host cell invasion enable parasite motility controlling parasite motility although rng2 depletion intact conoid organelle organelle traverses intact protein conditional depletion biochemical properties detached conoid gliding motility unstable protein undergoes extrusion two structures strong candidate striking detachment still unclear rng2 tethers rng2 led rng2 emerges rhoptries follow resilient bridge protein localized plasma membrane pivotal protein likely facilitate large coiled immunoelectron microscopy functional activity enabling rng2 electron tomography dependent extrusion critical role concatenated assemblies comprehensive mutagenesis coil domains calcium waves |
| dc.title.none.fl_str_mv | Biochemical investigation of wild-type and processed RNG2. |
| dc.type.none.fl_str_mv | Image Figure info:eu-repo/semantics/publishedVersion image |
| description | <p><b>(A)</b> Representation of the RNG2 constructs expressed in SF9 insect cells. <b>(B)</b> Insect cell protein expression and solubility of the RNG2 truncation variants, as assessed by Coomassie blue staining. <b>(C)</b> Protein expression and solubility of RNG2 truncation variants were assessed via western blotting. <b>(D)</b> Size-exclusion chromatography (SEC) chromatogram of the affinity-purified RNG2-ΔN+CTer variant obtained via Strep-tactin purification. A Coomassie-stained gel of the protein-containing fractions of the SEC is shown on the right. The data underlying this figure can be found in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003506#pbio.3003506.s008" target="_blank">S2 Data</a>. <b>(E)</b> Co-purification assays using metal-affinity chromatography of cells co-infected with RNG2 fragments assessed by western blot analysis and Coomassie blue staining. All fragments have a C-terminal STREP-tag.</p> |
| eu_rights_str_mv | openAccess |
| id | Manara_85ad9e0200721b12f2efcc07bedceb22 |
| identifier_str_mv | 10.1371/journal.pbio.3003506.g002 |
| network_acronym_str | Manara |
| network_name_str | ManaraRepo |
| oai_identifier_str | oai:figshare.com:article/30697353 |
| publishDate | 2025 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | CC BY 4.0 |
| spelling | Biochemical investigation of wild-type and processed RNG2.Romuald Haase (22339777)Bingjian Ren (22676577)Albert Tell i Puig (22676580)Alessandro Bonavoglia (19415718)Jean-Baptiste Marq (375239)Rémy Visentin (22676583)Nicolas Dos Santos Pacheco (22676586)Bohumil Maco (383443)Ricardo Mondragón-Flores (10737057)Oscar Vadas (2416228)Dominique Soldati-Favre (79026)BiophysicsBiochemistryMicrobiologyCell BiologyPhysiologyInfectious DiseasesEnvironmental Sciences not elsewhere classifiedBiological Sciences not elsewhere classifiedPhysical Sciences not elsewhere classifiedtoxoplasma gondii </remains apically anchoredheterologous expression systemsdiv >< papical polar ringbiochemical analysis revealedproper conoid anchorageensures conoid functionalityless parasites revealedhost cell invasionenable parasite motilitycontrolling parasite motilityalthough rng2 depletionintact conoid organelleorganelle traversesintact proteinconditional depletionbiochemical propertiesdetached conoidgliding motilityunstable proteinundergoes extrusiontwo structuresstrong candidatestriking detachmentstill unclearrng2 tethersrng2 ledrng2 emergesrhoptries followresilient bridgeprotein localizedplasma membranepivotal proteinlikely facilitatelarge coiledimmunoelectron microscopyfunctional activityenabling rng2electron tomographydependent extrusioncritical roleconcatenated assembliescomprehensive mutagenesiscoil domainscalcium waves<p><b>(A)</b> Representation of the RNG2 constructs expressed in SF9 insect cells. <b>(B)</b> Insect cell protein expression and solubility of the RNG2 truncation variants, as assessed by Coomassie blue staining. <b>(C)</b> Protein expression and solubility of RNG2 truncation variants were assessed via western blotting. <b>(D)</b> Size-exclusion chromatography (SEC) chromatogram of the affinity-purified RNG2-ΔN+CTer variant obtained via Strep-tactin purification. A Coomassie-stained gel of the protein-containing fractions of the SEC is shown on the right. The data underlying this figure can be found in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003506#pbio.3003506.s008" target="_blank">S2 Data</a>. <b>(E)</b> Co-purification assays using metal-affinity chromatography of cells co-infected with RNG2 fragments assessed by western blot analysis and Coomassie blue staining. All fragments have a C-terminal STREP-tag.</p>2025-11-24T18:31:05ZImageFigureinfo:eu-repo/semantics/publishedVersionimage10.1371/journal.pbio.3003506.g002https://figshare.com/articles/figure/Biochemical_investigation_of_wild-type_and_processed_RNG2_/30697353CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/306973532025-11-24T18:31:05Z |
| spellingShingle | Biochemical investigation of wild-type and processed RNG2. Romuald Haase (22339777) Biophysics Biochemistry Microbiology Cell Biology Physiology Infectious Diseases Environmental Sciences not elsewhere classified Biological Sciences not elsewhere classified Physical Sciences not elsewhere classified toxoplasma gondii </ remains apically anchored heterologous expression systems div >< p apical polar ring biochemical analysis revealed proper conoid anchorage ensures conoid functionality less parasites revealed host cell invasion enable parasite motility controlling parasite motility although rng2 depletion intact conoid organelle organelle traverses intact protein conditional depletion biochemical properties detached conoid gliding motility unstable protein undergoes extrusion two structures strong candidate striking detachment still unclear rng2 tethers rng2 led rng2 emerges rhoptries follow resilient bridge protein localized plasma membrane pivotal protein likely facilitate large coiled immunoelectron microscopy functional activity enabling rng2 electron tomography dependent extrusion critical role concatenated assemblies comprehensive mutagenesis coil domains calcium waves |
| status_str | publishedVersion |
| title | Biochemical investigation of wild-type and processed RNG2. |
| title_full | Biochemical investigation of wild-type and processed RNG2. |
| title_fullStr | Biochemical investigation of wild-type and processed RNG2. |
| title_full_unstemmed | Biochemical investigation of wild-type and processed RNG2. |
| title_short | Biochemical investigation of wild-type and processed RNG2. |
| title_sort | Biochemical investigation of wild-type and processed RNG2. |
| topic | Biophysics Biochemistry Microbiology Cell Biology Physiology Infectious Diseases Environmental Sciences not elsewhere classified Biological Sciences not elsewhere classified Physical Sciences not elsewhere classified toxoplasma gondii </ remains apically anchored heterologous expression systems div >< p apical polar ring biochemical analysis revealed proper conoid anchorage ensures conoid functionality less parasites revealed host cell invasion enable parasite motility controlling parasite motility although rng2 depletion intact conoid organelle organelle traverses intact protein conditional depletion biochemical properties detached conoid gliding motility unstable protein undergoes extrusion two structures strong candidate striking detachment still unclear rng2 tethers rng2 led rng2 emerges rhoptries follow resilient bridge protein localized plasma membrane pivotal protein likely facilitate large coiled immunoelectron microscopy functional activity enabling rng2 electron tomography dependent extrusion critical role concatenated assemblies comprehensive mutagenesis coil domains calcium waves |