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: cell biology of invasion and intracellular growth

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  • Authors: Javier Pizarro-Cerdá1,2,3, Pascale Cossart4,5,6
  • Editors: Vincent A. Fischetti7, Richard P. Novick8, Joseph J. Ferretti9, Daniel A. Portnoy10, Miriam Braunstein11, Julian I. Rood12
    Affiliations: 1: Unité Interactions Bactéries-Cellules, Institut Pasteur, Paris F-75015, FRANCE; 2: INSERM U604, Paris F-75015, FRANCE; 3: INRA USC2020, Paris F-75015, FRANCE; 4: Unité Interactions Bactéries-Cellules, Institut Pasteur, Paris F-75015, FRANCE; 5: INSERM U604, Paris F-75015, FRANCE; 6: INRA USC2020, Paris F-75015, FRANCE; 7: The Rockefeller University, New York, NY; 8: Skirball Institute for Molecular Medicine, NYU Medical Center, New York, NY; 9: Department of Microbiology & Immunology, University of Oklahoma Health Science Center, Oklahoma City, OK; 10: Department of Molecular and Cellular Microbiology, University of California, Berkeley, Berkeley, CA; 11: Department of Microbiology and Immunology, University of North Carolina-Chapel Hill, Chapel Hill, NC; 12: Infection and Immunity Program, Monash Biomedicine Discovery Institute, Monash University, Melbourne, Australia
  • Source: microbiolspec December 2018 vol. 6 no. 6 doi:10.1128/microbiolspec.GPP3-0013-2018
  • Received 19 January 2018 Accepted 19 September 2018 Published 07 December 2018
  • Javier Pizarro-Cerdá, [email protected]
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  • Abstract:

    The Gram-positive pathogen is able to promote its entry into a diverse range of mammalian host cells by triggering plasma membrane remodeling, leading to bacterial engulfment. Upon cell invasion, disrupts its internalization vacuole and translocates to the cytoplasm, where bacterial replication takes place. Subsequently, uses an actin-based motility system that allows bacterial cytoplasmic movement and cell-to-cell spread. therefore subverts host cell receptors, organelles and the cytoskeleton at different infection steps, manipulating diverse cellular functions that include ion transport, membrane trafficking, post-translational modifications, phosphoinositide production, innate immune responses as well as gene expression and DNA stability.

  • Citation: Pizarro-Cerdá J, Cossart P. 2018. : cell biology of invasion and intracellular growth. Microbiol Spectrum 6(6):GPP3-0013-2018. doi:10.1128/microbiolspec.GPP3-0013-2018.


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The Gram-positive pathogen is able to promote its entry into a diverse range of mammalian host cells by triggering plasma membrane remodeling, leading to bacterial engulfment. Upon cell invasion, disrupts its internalization vacuole and translocates to the cytoplasm, where bacterial replication takes place. Subsequently, uses an actin-based motility system that allows bacterial cytoplasmic movement and cell-to-cell spread. therefore subverts host cell receptors, organelles and the cytoskeleton at different infection steps, manipulating diverse cellular functions that include ion transport, membrane trafficking, post-translational modifications, phosphoinositide production, innate immune responses as well as gene expression and DNA stability.

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Image of FIGURE 1

Cellular receptors for in host cells. The receptor for InlA in nonphagocytic polarized cells (including goblet cells) is the transmembrane molecule E-cadherin. Interaction takes place between the InlA leucine-rich repeats (LRRs) and the first extracellular domain of E-cadherin, leading to phosphorylation and ubiquitylation of the cytoplasmic domain of E-cadherin by the kinase Src and the ubiquitin ligase Hakai, respectively. Clustering of E-cadherin requires the presence of lipid rafts (left panel). Via its C-terminal glycine-tryptophan (GW) repeats, InlB interacts with the receptor for the globular part of the C1q complement component (gC1qR) and glycosaminoglycans, which enable interaction of the N-terminal LRRs of InlB with the tyrosine receptor kinase Met in nonphagocytic cells (including trophoblasts). Met dimerization upon interaction with InlB leads to autophosphorylation and recruitment of the ubiquitin ligase Cbl, which ubiquitylates the cytoplasmic tail of Met (center panel). In fibroblasts and monocytes, a function for the FcγRIA receptor has been described for internalization, via interaction with a still unidentified surface molecule (right panel). Modified from reference 12 .

Source: microbiolspec December 2018 vol. 6 no. 6 doi:10.1128/microbiolspec.GPP3-0013-2018
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Image of FIGURE 2

intracellular stages. is able to induce its entry into nonphagocytic cells mainly via the interaction of InlA and InlB with host cells receptors that promote actin recruitment, remodeling of the plasma membrane, and bacterial engulfment. The surface molecule ActA and the secreted pore-forming toxin LLO have also been implicated in the early entry steps (left cell, upper left). In goblet cells, upon internalization, is localized in a vacuole, and through transcytosis the bacterium is translocated to the lamina propria (left cell, left). In other cells, the combined activity of diverse virulence factors, including the pore-forming LLO, the metalloprotease Mpl, the phospholipases PlcA and PlcB, and the pheromone pPplA, favor disruption of the vacuole and release in the cytosol, where the bacteria takes advantage of host metabolites via the phosphate transporter Hpt and the lipoate protein ligase LplA. The surface protein ActA promotes actin-based motility, and the secreted protein InlC favors reduction of plasma membrane cortical tension, allowing to form protrusions and to invade neighboring cells. LLO and the phospholipases PlcA and PlcB contribute to the disruption of the double-membrane vacuole (right cell). has been observed in large spacious compartments that may arise rapidly after internalization of bacteria or upon decrease of ActA expression in already cytoplasmic bacteria (left cell, upper center). Extracellular LLO is able to modulate different cellular functions, including mitochondrial fission, lysosomal permeabilization, protein SUMOylation, ER stress, DNA damage, and chromatin remodeling. The phospholipases PlcA and PlcB, together with actin polymerization by ActA, have been implicated in the resistance to autophagy ( 195 ). The secreted molecule InlC prevents NF-κB translocation to the nucleus. Modified from reference 12 .

Source: microbiolspec December 2018 vol. 6 no. 6 doi:10.1128/microbiolspec.GPP3-0013-2018
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