The Intracellular Fate of Salmonella Depends on the Recruitment of Kinesin

  title={The Intracellular Fate of Salmonella Depends on the Recruitment of Kinesin},
  author={Emmanuel Boucrot and Thomas Henry and Jean-Paul Borg and Jean Pierre Gorvel and St{\'e}phane M{\'e}resse},
  pages={1174 - 1178}
Salmonella enterica causes a variety of diseases, including gastroenteritis and typhoid fever. The success of this pathogen depends on its capacity to proliferate within host cells in a membrane-bound compartment. We found that the Salmonella-containing vacuole recruited the plus-end–directed motor kinesin. Bacterial effector proteins translocated into the host cell by a type III secretion system antagonistically regulated this event. Among these effectors, SifA targeted SKIP, a host protein… 

Analysis of kinesin accumulation on Salmonella-containing vacuoles.

This chapter describes techniques that are used to screen by immunofluorescence microscopy the accumulation of kinesin-1 on strains of Salmonella carrying multiple mutations.

The Translocated Salmonella Effector Proteins SseF and SseG Interact and Are Required To Establish an Intracellular Replication Niche

It is shown that SseF interacts functionally and physically with SseG but not SifA and is also required for the perinuclear localization of Salmonella vacuoles and is a complex phenomenon resulting from the combined action of several effector proteins.

Regulation of kinesin-1 activity by the Salmonella enterica effectors PipB2 and SifA

In vitro and in cellulo assays reveal a specific interaction between the two effectors and indicate that, contrary to what studies on infected cells suggested, interaction with PipB2 is sufficient to relieve the autoinhibition of kinesin-1.

The Salmonella Effector SteA Contributes to the Control of Membrane Dynamics of Salmonella-Containing Vacuoles

The analysis of the cellular function of the Salmonella effector SteA indicates that SteA is functionally linked to SseF and SseG and suggests that it might contribute directly or indirectly to the regulation of microtubule motors on the bacterial vacuoles.

The Salmonella effector protein PipB2 is a linker for kinesin-1

The data indicate that the TTSS-2-mediated fine-tuning of kinesin-1 activity associated with the bacterial vacuole is crucial for the virulence of Salmonella.

Endomembrane remodeling and dynamics in Salmonella infection

The role and significance of membrane compartment remodeling observed in infected cells and the bacterial and host cell pathways involved are focused on.

The Virulence Protein SopD2 Regulates Membrane Dynamics of Salmonella-Containing Vacuoles

SopD2 inhibits the vesicular transport and the formation of tubules that extend outward from the SCV and thereby contributes to the sifA− associated phenotypes and highlights the antagonistic roles played by SopD2 and SifA in the membrane dynamics of the vacuole.



Microtubule motors control membrane dynamics of Salmonella-containing vacuoles

The experiments indicate that microtubule motors play important roles in regulating vacuolar membrane dynamics during intracellular replication of S. typhimurium and indicate that recruitment of dynein to SCVs is dependent on Rab7 activity.

SseG, a virulence protein that targets Salmonella to the Golgi network

It is shown that after invasion of epithelial cells and migration to a perinuclear location, the majority of SCVs become surrounded by membranes of the Golgi network, and this process is dependent on the Salmonella pathogenicity island 2 type III secretion system effector SseG.

Dynein-mediated vesicle transport controls intracellular Salmonella replication.

Activation of dynein-mediated vesicle transport can thus control intracellular survival of Salmonella.

Salmonella maintains the integrity of its intracellular vacuole through the action of SifA

It is proposed that the wild‐type strain, through the action of SPI‐2 effectors (including SpiC), diverts the Salmonella‐containing vacuole from the endocytic pathway, and subsequent recruitment and maintenance of vacuolar ATPase/lgp‐containing membranes that enclose replicating bacteria is mediated by translocation of SifA.

Identification of a Salmonella virulence gene required for formation of filamentous structures containing lysosomal membrane glycoproteins within epithelial cells

Salmonella species are facultative intracellular pathogens that invade epithelial cells and reside within lysosomal membrane glycoprotein (Igp)‐containing vacuoles, and they induce the formation of stable Igp‐containing filamentous structures that connect with the Salmonella‐containing Vacuoles.

SifA, a Type III Secreted Effector of Salmonella typhimurium, Directs Salmonella‐Induced Filament (Sif) Formation Along Microtubules

The essential role of microtubule dynamics in the formation of Sifs is demonstrated and the utility of this epitope tagging strategy for the study of bacterial type III secreted proteins is demonstrated.

Salmonella typhimurium SifA Effector Protein Requires Its Membrane-anchoring C-terminal Hexapeptide for Its Biological Function*

Results indicate that membrane anchoring of SifA requires its C-terminal hexapeptide domain, which is important for the biological function of this bacterial effector.

A conserved amino acid sequence directing intracellular type III secretion by Salmonella typhimurium.

  • E. MiaoS. Miller
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 2000
Seven proteins are described that contain conserved amino acid sequences that direct translocation by TTSS in Salmonella typhimurium that are located within temperate bacteriophages, suggesting a common mechanism for the dissemination of more recently evolved STE.

Growth and killing of a Salmonella enterica serovar Typhimurium sifA mutant strain in the cytosol of different host cell lines.

It was found that Salmonella replicates within the cytosol of epithelial cells at a higher rate than that achieved when replicating within the vacuole, but is defective for replication in the cytOSol of fibroblasts or macrophages.

Salmonella induces the formation of filamentous structures containing lysosomal membrane glycoproteins in epithelial cells.

Observations suggest that Salmonella-induced filaments containing lgps are linked to intracellular bacterial replication, which is different from previously described tubular lysosomes.