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- W2093200380 abstract "Virulent <i>Mycobacterium tuberculosis</i> (<i>Mtb</i>) H37Rv induces necrosis of host macrophages (Mφ), initiated by mitochondrial inner membrane perturbation and plasma membrane disruption, which serves as a microbial virulence mechanism allowing dissemination of the pathogen. Infection of Mφ with <i>Mtb</i> creates a local disruption of the plasma membrane, which can be repaired in a Ca<sup>2+</sup>dependent manner by trafficking of intracellular vesicles to the plasma membrane as membrane donors. We demonstrate that attenuated H37Ra induce significant exocytosis of LAMP1, a lysosome marker, and mannosidase 2, a Golgi apparatus marker, to the plasma membrane surface leading to cell membrane repair. Successful membrane repair prevents fluorescent dextran (FDx) diffusion into the cytosol. In contrast, Mφ infected with virulent H37Rv show much less LAMP1 and mannosidase 2 exocytosis and more FDx diffusion. Confocal analysis indicates that plasma membrane LAMP1 is partially colocalized with synaptotagmin7 (Syt 7), an essential regulator of exocytosis. Silencing of Syt 7 leads to less LAMP1 exocytosis and increases FDx diffusion and necrosis. Suppression of mannosidase 2 exocytosis by Brefeldin A implies the endoplasmic reticulum indirectly as a contributor to membrane repair. These findings reveal a virulence mechanism of H37Rv that blocks plasma membrane repair and leads to necrosis (Supported by NIH grant AI50216)." @default.
- W2093200380 created "2016-06-24" @default.
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- W2093200380 date "1984-11-01" @default.
- W2093200380 modified "2023-09-25" @default.
- W2093200380 title "The Eye in General Medicine" @default.
- W2093200380 doi "https://doi.org/10.1136/bjo.68.11.847-a" @default.
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