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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Faudry, Eric Eric, Faudry Sylvie, Elsen Caroline, Gébus Bohn, Yu-sing Tammy Elsen, Sylvie Attree, Ina Gébus, Caroline |
| Description | Author Affiliation: Gébus C ( Laboratoire de Biochimie et Biophysique des Systèmes Intégrés (Unité mixte de recherche 5092), CNRS, Université Joseph Fourier, Commissariat à l'Energie Atomique, DSV, iRTSV, 17 rue des Martyrs, Grenoble, France.) |
| Abstract | Protective antigens of Pseudomonas aeruginosa (PcrV) and Yersinia pestis (LcrV) are key elements of specialized machinery, the type III secretion system (T3SS), which enables the injection of effector molecules into eukaryotic cells. Being positioned at the injectisome extremity, V proteins participate in the translocation process across the host cell plasma membrane. In this study, we demonstrate the assembly of V proteins into oligomeric doughnut-like complexes upon controlled refolding of the proteins in vitro. The oligomeric nature of refolded PcrV was revealed by size exclusion chromatography, native gel electrophoresis, and native mass spectrometry, which ascertain the capacity of the protein to multimerize into higher-order species. Furthermore, transmission electron microscopy performed on oligomers of both PcrV and LcrV revealed the presence of distinct structures with approximate internal and external diameters of 3-4 and 8-10 nm, respectively. The C-terminal helix, alpha12, of PcrV and notably the hydrophobic residues Val(255), Leu(262), and Leu(276) located within this helix, were shown to be crucial for oligomerization. Moreover, the corresponding mutant proteins produced in P. aeruginosa were found to be non-functional in in vivo type III-dependent cytotoxicity assays by directly affecting the correct assembly of PopB/D translocon within the host cell membranes. The detailed understanding of structure-function relationships of T3SS needle tip proteins will be of value in further developments of new vaccines and antimicrobials. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 35 |
| Volume Number | 283 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2008-08-29 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Antigens, Bacterial Chemistry Bacterial Toxins Multiprotein Complexes Pore Forming Cytotoxic Proteins Pseudomonas Aeruginosa Yersinia Pestis Animals Anti-Infective Agents Immunology Bacterial Vaccines Drug Design Hydrophobic And Hydrophilic Interactions Macrophages Mice Ultrastructure Mutation Plague Protein Folding Protein Structure, Quaternary Protein Structure, Secondary Pseudomonas Infections Structure-Activity Relationship Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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