Host endoplasmic reticulum COPII proteins control cell-to-cell spread of the bacterial pathogen<i>L</i><i>isteria monocytogenes</i>

Gianfelice, Antonella; Le, Phuong Huynh Bao; Rigano, Luciano A.; Saila, Susan; Dowd, Georgina C.; McDivitt, Tina; Bhattacharya, Nilakshee; Hong, Wanjin; Stagg, Scott M.; Ireton, Keith

doi:10.1111/cmi.12409

Cited by 22 publications

(25 citation statements)

References 80 publications

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“…InlC disrupts Tuba-mediated tension, which has been proposed to promote protrusion initiation [45] and enhance virulence in mice [47]. Recent work showed that InlC also disrupts the interaction between Tuba and the host membrane-trafficking protein Sec31A [48]. It was proposed that this might regulate spread by regulating the trafficking of tension-regulating proteins to the plasma membrane, although this awaits further investigation.…”

Section: Initiating Protrusionsmentioning

confidence: 99%

Actin-based motility and cell-to-cell spread of bacterial pathogens

Lamason

Welch

2017

Current Opinion in Microbiology

103

110

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Subversion of the host actin cytoskeleton is a critical virulence mechanism used by a variety of intracellular bacterial pathogens during their infectious life cycles. These pathogens manipulate host actin to promote actin-based motility and coordinate motility with cell-to-cell spread. Growing evidence suggests that the tactics employed by pathogens are surprisingly diverse. Here, we review recent advances suggesting that bacterial surface proteins exhibit divergent biochemical mechanisms of actin polymerization and recruit distinct host protein networks to drive motility, and that bacteria deploy secreted effector proteins that alter host cell mechanotransduction pathways to enable spread. Further investigation into the divergent strategies used by bacterial pathogens to mobilize actin will reveal new insights into pathogenesis and cytoskeleton regulation.

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Section: Initiating Protrusionsmentioning

confidence: 99%

Actin-based motility and cell-to-cell spread of bacterial pathogens

Lamason

Welch

2017

Current Opinion in Microbiology

103

110

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“…It also facilitates the life cycles of some key pathogens including Salmonella (Santos et al 2015), Listeria (Gianfelice et al 2015), enteropathogenic E. coli , and Citrobacter (Thanabalasuriar et al 2013). Mutations in some COPII genes are implicated in osteogenesis imperfecta and related disorders (Garbes et al 2015), as well as other diseases including cancer (Lee et al 2016; Yehia et al 2015).…”

Section: Future Perspectivesmentioning

confidence: 99%

COPII-dependent ER export in animal cells: adaptation and control for diverse cargo

McCaughey

Stephens

2018

Histochem Cell Biol

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The export of newly synthesized proteins from the endoplasmic reticulum is fundamental to the ongoing maintenance of cell and tissue structure and function. After co-translational translocation into the ER, proteins destined for downstream intracellular compartments or secretion from the cell are sorted and packaged into transport vesicles by the COPII coat protein complex. The fundamental discovery and characterization of the pathway has now been augmented by a greater understanding of the role of COPII in diverse aspects of cell function. We now have a deep understanding of how COPII contributes to the trafficking of diverse cargoes including extracellular matrix molecules, developmental signalling proteins, and key metabolic factors such as lipoproteins. Structural and functional studies have shown that the COPII coat is both highly flexible and subject to multiple modes of regulation. This has led to new discoveries defining roles of COPII in development, autophagy, and tissue organization. Many of these newly emerging features of the canonical COPII pathway are placed in a context of procollagen secretion because of the fundamental interest in how a coat complex that typically generates 80-nm transport vesicles can package a cargo reported to be over 300 nm. Here we review the current understanding of COPII and assess the current consensus on its role in packaging diverse cargo proteins.

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“…Chemiluminescence was imaged using an Odyssey imaging system (Li-Cor Biosciences). Bands in Western blot images were quantified using ImageJ software as described (Gianfelice et al, 2015).…”

Section: Western Blotting and Immunoprecipitationmentioning

confidence: 99%

A role for host cell exocytosis in InlB-mediated internalisation ofListeria monocytogenes

Ngo

Bhalla

Chen

et al. 2017

Cellular Microbiology

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The bacterial surface protein InlB mediates internalisation of Listeria monocytogenes into human cells through interaction with the host receptor tyrosine kinase, Met. InlB-mediated entry requires localised polymerisation of the host actin cytoskeleton. Apart from actin polymerisation, roles for other host processes in Listeria entry are unknown. Here, we demonstrate that exocytosis in the human cell promotes InlB-dependent internalisation. Using a probe consisting of VAMP3 with an exofacial green fluorescent protein tag, focal exocytosis was detected during InlB-mediated entry. Exocytosis was dependent on Met tyrosine kinase activity and the GTPase RalA. Depletion of SNARE proteins by small interfering RNA demonstrated an important role for exocytosis in Listeria internalisation. Depletion of SNARE proteins failed to affect actin filaments during internalisation, suggesting that actin polymerisation and exocytosis are separable host responses. SNARE proteins were required for delivery of the human GTPase Dynamin 2, which promotes InlB-mediated entry. Our results identify exocytosis as a novel host process exploited by Listeria for infection.

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Host endoplasmic reticulum COPII proteins control cell-to-cell spread of the bacterial pathogenListeria monocytogenes

Cited by 22 publications

References 80 publications

Actin-based motility and cell-to-cell spread of bacterial pathogens

Actin-based motility and cell-to-cell spread of bacterial pathogens

COPII-dependent ER export in animal cells: adaptation and control for diverse cargo

A role for host cell exocytosis in InlB-mediated internalisation ofListeria monocytogenes

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