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Ngondo, P.

Publications and source records attributed to Ngondo, P..

3 recordsLinked to original sources

SPATEs promote the survival of Shigella to the plasma complement system upon hemorrhage and bacteremia

Shigella spp. are the causative agents of shigellosis, which remains a leading cause of death in children under the age of five. Shigellosis is characterized by fever and results in hemorrhagic diarrhea; in more severe cases, Shigella bacteremia has been reported. These clinical features strongly suggest that Shigella survive exposure to plasma, although this has not yet been studied at the molecular level. In this report, we confirmed in a guinea pig model of shigellosis that local hemorrhages were induced by S. flexneri 5a and S. sonnei, and we demonstrated that Shigella reached mucosal CD31+/CD34+ blood vessels during the late stages of infection and further disseminated in the bloodstream. These results confirmed the exposure of Shigella to plasma components within the hemorrhagic colonic mucosa and in the bloodstream. We demonstrated that all the tested Shigella strains survived plasma exposure in vitro, and we showed that Serine Protease Autotransporters of Enterobacteriaceae (SPATEs) are essential for Shigella dissemination within the colonic mucosa. We have confirmed that SPATEs are expressed and secreted in poorly oxygenated environments encountered by Shigella from hypoxic foci of infection to the bloodstream. We further demonstrated that SPATEs promoted Shigella survival in plasma, by cleaving complement component 3 (C3), thereby impairing complement system activation. We have shown here that the ability of Shigella to survive plasma exposure is a key factor in its virulence, both within primary foci and systemically. Significance StatementIn this study we aimed to better understand the significance of the ability of Shigella to survive plasma exposure, as we observed that non-pathogenic E. coli rapidly lysed upon exposure. Indeed, we reported that Shigella was already exposed to plasma components within the colonic mucosa, as we reported in a guinea pig model of shigellosis that hemorrhages were induced, that were associated with local diffusion of plasma components in the infected colonic mucosa. Shigella was obviously exposed to plasma during bacteremia. The ability of Shigella to survive in plasma has not been previously reported. Here we have shown, first, that Shigella was able to divide and grow in the presence of human plasma, and second, we found that SPATEs played a central role in this process by impairing with the activation of the complement system.

microbiology↗

The E3 ubiquitin ligase FBXL6 controls the quality of newly synthesized mitochondrial ribosomal proteins

The large majority of mitochondrial proteins is synthesized in the cytosol and then imported to the organelle. To ensure proper mitochondrial functions, the quality of these proteins needs to be guaranteed. Here, we show that the E3 ubiquitin ligase F-box/LRR-repeat protein 6 (FBXL6) participates to the quality of these mitochondrial proteins at the level of the cytosolic translation. We found that lack of FBXL6 has severe effects including mitochondrial ribosomal protein aggregations, altered mitochondrial metabolism and inhibited cell cycle progression in oxidative conditions. FBXL6 was found to interact specifically with ribosomal-associated quality control proteins and chaperones involved in the regulation of newly synthesized proteins and also it preferentially binds newly synthesized mitochondrial ribosomal proteins. Consistently, deletion of the RQC protein, NEMF or HSP70-family chaperone HSPA1A impedes FBXL6 interaction with its substrate. In addition, cells lacking FBXL6 display altered degradation of defective mitochondrial ribosomal protein containing C-terminal alanyl-threonyl extension.

cell biology↗

FRIENDLY (FMT) is an RNA binding protein associated with cytosolic ribosomes at the mitochondrial surface

The spatial organization of protein synthesis in the eukaryotic cell is essential for maintaining the integrity of the proteome and the functioning of the cell. Translation on free polysomes or on ribosomes associated with the endoplasmic reticulum has been studied for a long time. More recent data have revealed selective translation of mRNAs in other compartments, in particular at the surface of mitochondria. Although these processes have been described in many organisms, in particular in plants, the mRNA targeting and localized translation mechanisms remain poorly understood. Here, the Arabidopsis thaliana Friendly (FMT) protein is shown to be a cytosolic RNA binding protein that associates with cytosolic ribosomes at the surface of mitochondria. Its knockdown delays seedling development and causes mitochondrial clustering. The mutation also disrupts the mitochondrial proteome and the localization of nuclear transcripts on the surface of mitochondria. These data indicate that FMT participates in the localization of mRNAs and their translation at the surface of mitochondria.

plant biology↗