Proteomes of Host Cell Membranes Modified by Intracellular Activities of Salmonella enterica

Vorwerk, Stephanie; Krieger, Viktoria; Deiwick, Jörg; Hensel, Michael; Hansmeier, Nicole

doi:10.1074/mcp.m114.041145

Cited by 44 publications

(81 citation statements)

References 71 publications

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“…HGS was chosen due to being the highest-ranking hit (Table S2) and the interaction of SPI1-T3SS effector SopB with endosomal sorting complex required for transport (ESCRT) complexes previously reported [49] with HGS being part of the ESCRT-0 complex. Furthermore, RAB1A and RAB11A were included as the highest-ranking Rab GTPases with RAB11A previously being shown to colocalize with SCV as well as SIF [32, 50]. Consistently, RAB7A served as another well-established SCV- and SIF-localizing control [12, 50–52].…”

Section: Resultsmentioning

confidence: 80%

A trafficome-wide RNAi screen reveals deployment of early and late secretory host proteins and the entire late endo-/lysosomal vesicle fusion machinery by intracellularSalmonella

Kehl

Göser

Reuter

et al. 2019

Preprint

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38 The intracellular lifestyle of Salmonella enterica is characterized by the formation of a 39 replication-permissive membrane-bound niche, the Salmonella-containing vacuole (SCV). A 40 further consequence of the massive remodeling of the host cell endosomal system, intracellular 41 Salmonella establish a unique network of various Salmonella-induced tubules (SIT). The 42 bacterial repertoire of effector proteins required for the establishment for one type of these SIT, 43 the Salmonella-induced filaments (SIF), is rather well-defined. However, the corresponding 44 host cell proteins are still poorly understood. To identify host factors required for the formation 45 of SCV and SIF, we performed a sub-genomic RNAi screen. The analyses comprised high-46 resolution live cell imaging to score effects on SIF induction, dynamics and morphology. The 47 hits of our functional RNAi screen comprise: i) The late endo-/lysosomal SNARE (soluble N-48 ethylmaleimide-sensitive factor attachment protein receptor) complex, consisting of STX7, 49 STX8, VTI1B, and VAMP7 or VAMP8, this is, in conjunction with RAB7 and the homotypic 50 fusion and protein sorting (HOPS) tethering complex, a complete vesicle fusion machinery. ii) 51 Novel interactions with the early secretory GTPases RAB1A and RAB1B, possibly providing 52 a link to coat protein complex I (COPI) vesicles and reinforcing recently identified ties to the 53 endoplasmic reticulum. iii) New connections to the late secretory pathway and/or the recycling 54 endosome via the GTPases RAB3A, RAB8A, and RAB8B and the SNAREs VAMP2, VAMP3, 55 and VAMP4. iv) An unprecedented involvement of clathrin-coated structures. The resulting set 56 of hits allowed to characterize completely new host factor interactions, and strengthen 57 observations from several previous studies. 58 Author Summary59 The facultative intracellular pathogen Salmonella enterica serovar Typhimurium induces the 60 reorganization of the endosomal system of mammalian host cells. This activity is dependent on 61 translocated effector proteins of the pathogen. The host cells factors required for endosomal 18.11.2019 Host factors for SIF formation 4 62 remodeling are only partially known. To identify such factors for formation and dynamics of 63 endosomal compartments in Salmonella-infected cell, we performed a live cell imaging-based 64 RNAi screen a to investigate the role of 496 mammalian proteins involved in cellular logistics. 65 We identified that endosomal remodeling by intracellular Salmonella dependent on host factors 66 in following functional classes: i) the late endo-/lysosomal SNARE (soluble N-ethylmaleimide-67 sensitive factor attachment protein receptor) complex, ii) the early secretory pathway, 68 represented by regulators GTPases RAB1A and RAB1B, iii) the late secretory pathway and/or 69 recycling endosomes represented by GTPases RAB3A, RAB8A, RAB8B, and the SNAREs 70 VAMP2, VAMP3, and VAMP4, and iv) clathrin-coated structures. The identification of these 71 new host factors provides further evidence ...

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Section: Resultsmentioning

confidence: 80%

A trafficome-wide RNAi screen reveals deployment of early and late secretory host proteins and the entire late endo-/lysosomal vesicle fusion machinery by intracellularSalmonella

Kehl

Göser

Reuter

et al. 2019

Preprint

Self Cite

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“…Whereas some pathogens escape phagosomes and replicate in the host cytoplasm most of the described pathogens replicate in membrane bound, vacuole-like compartments. Such intracellular niches of various pathogens are diverse, and biogenesis often depends on the delivery of bacterial effector proteins into the host cell cytoplasm (Vorwerk et al 2015).…”

Section: An Intracellular Lifestylementioning

confidence: 99%

A Glance at Prokaryotes and Eukaryotes Interplay and Campylobacter jejuni–Host Interaction

Santos

Martins

Tavares

et al. 2016

Campylobacter Spp. And Related Organisms in Poultry

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This chapter begins with the historical background to the evolutionary development of the cells. The endosymbiosis theory by which prokaryotes gave rise to the first eukaryotic cells describe the relationship between cell types that may have evolved through predation to mutualism or parasitism. There is also discussion of some interactions between parasitic unicellular organisms and their cell hosts taking into account the dynamic actin cytoskeleton and the immune response resulting from the invasion. Finally, C. jejuni, its types of invasion routes, intracellular traffic, virulence factors, and colonization of poultry cells by C. jejuni are discussed.

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“…Y ersinia pathogens are facultative intracellular pathogens, which translocate their virulence factors, which modify the eukaryotic proteome to interfere with the anti-microbial responses [2], but at the same time the host cell also modifies expression of its proteins to defy the bacterial infection. Proteomics has been utilized to understand the molecular basis of pathogenesis in several bacterial infections, including Listeria monocytogenes [3–5], Salmonella enterica Typhimurium [6, 7], and Mycobacterium tuberculosis [8]. Proteomics has also been a useful tool in characterization of proteins encoded by Yersiniae [9–15].…”

Section: Introductionmentioning

confidence: 99%

Analysis of differentially expressed proteins in Yersinia enterocolitica-infected HeLa cells

Alugubelly

Hercík

Kibler

et al. 2016

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Yersinia enterocolitica is a facultative intracellular pathogen and a causative agent of yersiniosis, which can be contracted by ingestion of contaminated food. Yersinia secretes virulence factors to subvert critical pathways in the host cell. In this study we utilized shotgun label-free proteomics to study differential protein expression in epithelial cells infected with Yersinia enterocolitica. We identified a total of 551 proteins, amongst which 42 were downregulated (e.g. Prostaglandin E Synthase 3, POH-1 and Karyopherin alpha) and 22 were upregulated (e.g. Rab1c and RhoA) in infected cells. We validated some of these results by western blot analysis of proteins extracted from Caco-2 and HeLa cells. The proteomic dataset was used to identify host canonical pathways and molecular functions modulated by this infection in the host cells. This study constitutes a proteome of Yersinia-infected cells and can support new discoveries in the area of host-pathogen interactions.

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Proteomes of Host Cell Membranes Modified by Intracellular Activities of Salmonella enterica

Cited by 44 publications

References 71 publications

A trafficome-wide RNAi screen reveals deployment of early and late secretory host proteins and the entire late endo-/lysosomal vesicle fusion machinery by intracellularSalmonella

A trafficome-wide RNAi screen reveals deployment of early and late secretory host proteins and the entire late endo-/lysosomal vesicle fusion machinery by intracellularSalmonella

A Glance at Prokaryotes and Eukaryotes Interplay and Campylobacter jejuni–Host Interaction

Analysis of differentially expressed proteins in Yersinia enterocolitica-infected HeLa cells

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