Biochemical investigation of wild-type and processed RNG2.

(A) Representation of the RNG2 constructs expressed in SF9 insect cells. (B) Insect cell protein expression and solubility of the RNG2 truncation variants, as assessed by Coomassie blue staining. (C) Protein expression and solubility...

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Glavni avtor:	Romuald Haase (22339777) (author)
Drugi avtorji:	Bingjian Ren (22676577) (author), Albert Tell i Puig (22676580) (author), Alessandro Bonavoglia (19415718) (author), Jean-Baptiste Marq (375239) (author), Rémy Visentin (22676583) (author), Nicolas Dos Santos Pacheco (22676586) (author), Bohumil Maco (383443) (author), Ricardo Mondragón-Flores (10737057) (author), Oscar Vadas (2416228) (author), Dominique Soldati-Favre (79026) (author)
Izdano:	2025
Teme:	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
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Izvleček:	<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>

Biochemical investigation of wild-type and processed RNG2.

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