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

Abstract

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.

PGE2 Augments Inflammasome Activation and M1 Polarization in Macrophages Infected With Salmonella Typhimurium and Yersinia enterocolitica

“…Metabolomic studies identified changes in host metabolites upon S. Typhimurium infection, suggesting that metabolites of one of the groups, eicosanoids are elevated during infection in a murine model ( Antunes et al, 2011 ; Deatherage Kaiser et al, 2013 ). The eicosanoid pathway (Figure 1 ), which depends on the activity of cyclooxygenase (COX) enzymes ( Tanioka et al, 2000 ), is known to be affected by infections with bacterial pathogens ( Antunes et al, 2011 ; Deatherage Kaiser et al, 2013 ; Alugubelly et al, 2016 ). For instance, COX-2 is upregulated in murine macrophages infected with S. Typhimurium, which depends on the presence of the Salmonella Pathogenicity Island-2 (SPI-2) SpiC protein ( Uchiya and Nikai, 2004 ).…”

PGE2 Augments Inflammasome Activation and M1 Polarization in Macrophages Infected with Salmonella Typhimurium and Yersinia enterocolitica

“…At the indicated time points, cells were washed, lysed with 0.1% Triton-X, diluted in sterile PBS, and plated on LB plates for CFU counts. A similar protocol was performed for Y. enterocolitica infection, based on our past work (Edelmann et al, 2010;Alugubelly et al, 2016).…”

“…Metabolomic studies identified changes in host metabolites upon S. Typhimurium infection, suggesting that metabolites of one of the groups, eicosanoids are elevated during infection in a murine model (Antunes et al, 2011;Deatherage Kaiser et al, 2013). The eicosanoid pathway (Figure 1), which depends on the activity of cyclooxygenase (COX) enzymes (Tanioka et al, 2000), is known to be affected by infections with bacterial pathogens (Antunes et al, 2011;Deatherage Kaiser et al, 2013;Alugubelly et al, 2016). For instance, COX-2 is upregulated in murine macrophages infected with S. Typhimurium, which depends on the presence of the Salmonella Pathogenicity Island-2 (SPI-2) SpiC protein (Uchiya and Nikai, 2004).…”

USP8 inhibition regulates autophagy flux and controls Salmonella infection

“…DUBs are categorized into seven deubiquitinase sub-groups, including the ubiquitin-specific proteases (USPs), the ovarian tumor proteases (OTUs), JAB1/MPN/MOV34 metalloproteases (JAMMs), the ubiquitin C-terminal hydrolases (UCHs), the Josephins, the motif interacting with ubiquitin (MIU)-containing novel deubiquitinase family (MINDYs), and ZUP1 ( Komander et al., 2009 ). The ubiquitin-proteasome system plays a vital role in the host response to Gram-negative infections ( Lopez-Castejon and Edelmann, 2016 ), and previous studies have shown that bacterial pathogens can interfere with the deubiquitinase-mediated removal of ubiquitin modifications ( Kummari et al., 2015 ; Alugubelly et al., 2016 ; Hui et al., 2018 ). Concurrently, the host also regulates the activity and level of deubiquitinases to its advantage.…”