References
- Baumler A, Fang FC. Host specificity of bacterial pathogens. Cold Spring Harb Perspect Med. 2013;3(12):a010041.
- Crump JA, Luby SP, Mintz ED. The global burden of typhoid fever. Bull World Health Organ. 2004;82(5):346–353.
- Gunn JS, Marshall JM, Baker S, et al. Salmonella chronic carriage: epidemiology, diagnosis, and gallbladder persistence. Trends Microbiol. 2014;22(11):648–655.
- Majowicz SE, Musto J, Scallan E, et al. The global burden of nontyphoidal Salmonella gastroenteritis. Clin Infect Dis. 2010;50(6):882–889.
- Haraga A, Ohlson MB, Miller SI. Salmonellae interplay with host cells. Nat Rev Micro. 2008;6(1):53–66.
- Chen KW, Gross CJ, Sotomayor FV, et al. The neutrophil NLRC4 inflammasome selectively promotes IL-1beta maturation without pyroptosis during acute Salmonella challenge. Cell Rep. 2014;8(2):570–582.
- Yrlid U, Svensson M, Hakansson A, et al. In vivo activation of dendritic cells and T cells during Salmonella enterica serovar Typhimurium infection. Infect Immun. 2001;69(9):5726–5735.
- Castro-Eguiluz D, Pelayo R, Rosales-Garcia V, et al. B cell precursors are targets for Salmonella infection. Microb Pathog. 2009;47(1):52–56.
- Geddes K, Cruz F, Heffron F. Analysis of cells targeted by Salmonella type III secretion in vivo. PLoS Pathog. 2007;3(12):e196.
- Rosales-Reyes R, Pérez-López A, Sánchez-Gómez C, et al. Salmonella infects B cells by macropinocytosis and formation of spacious phagosomes but does not induce pyroptosis in favor of its survival. Microbial Pathogenesis. 2012;52(6):367–374.
- Souwer Y, Griekspoor A, De Wit J, et al. Selective infection of antigen-specific B lymphocytes by Salmonella mediates bacterial survival and systemic spreading of infection. PLoS One. 2012;7(11):e50667.
- Verjans GM, Ringrose JH, Van Alphen L, et al. Entrance and survival of Salmonella typhimurium and Yersinia enterocolitica within human B- and T-cell lines. Infect Immun. 1994;62(6):2229–2235.
- De Jong HK, Parry CM, Van Der Poll T, et al. Host–pathogen interaction in invasive Salmonellosis. Plos Pathogens. 2012;8(10):1–9.
- Hurley D, McCusker MP, Fanning S, et al. Salmonella-host interactions - modulation of the host innate immune system. Front Immunol. 2014;5:481.
- Marcus SL, Brumell JH, Pfeifer CG, et al. Salmonella pathogenicity islands: big virulence in small packages. Microbes Infect. 2000;2(2):145–156.
- Raffatellu M, Wilson RP, Chessa D, et al. SipA, SopA, SopB, SopD, and SopE2 contribute to Salmonella enterica serotype typhimurium invasion of epithelial cells. Infect Immun. 2005;73(1):146–154.
- Zhou D, Chen LM, Hernandez L, et al. A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization. Molecular Microbiology. 2001;248–259.
- Knodler LA, Finlay BB, Steele-Mortimer O. The Salmonella effector protein SopB protects epithelial cells from apoptosis by sustained activation of Akt. J Biol Chem. 2005;280(11):9058–9064.
- Steele-Mortimer O, Knodler LA, Marcus SL, et al. Activation of Akt/protein kinase B in epithelial cells by the Salmonella typhimurium effector SigD. J Biol Chem. 2000;275(1):37718–37724.
- Hersh D, Monack DM, Smith MR, et al. The Salmonella invasin SipB induces macrophage apoptosis by binding to caspase-1. Proc Natl Acad Sci U S A. 1999;96(5):2396–2401.
- McCormick BA, Colgan SP, Delp-Archer C, et al. Salmonella typhimurium attachment to human intestinal epithelial monolayers: transcellular signalling to subepithelial neutrophils. J Cell Biol. 1993;123(4):895–907.
- Miao EA, Alpuche-Aranda CM, Dors M, et al. Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1beta via Ipaf. Nat Immunol. 2006;7(6):569–575.
- Miao EA, Rajan JV. Salmonella and caspase-1: a complex interplay of detection and evasion. Front Microbiol. 2011;2:85.
- Franchi L, Amer A, Body-Malapel M, et al. Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1beta in salmonella-infected macrophages. Nat Immunol. 2006;7(6):576–582.
- Perez-Lopez A, Rosales-Reyes R, Alpuche-Aranda CM, et al. Salmonella downregulates Nod-like receptor family CARD domain containing protein 4 expression to promote its survival in B cells by preventing inflammasome activation and cell death. J Immunol. 2013;190(3):1201–1209.
- Fu V, Plouffe SW, Guan KL. The hippo pathway in organ development, homeostasis, and regeneration. Curr Opin Cell Biol. 2018;49:99–107.
- Lapi E, Di Agostino S, Donzelli S, et al. PML, YAP, and p73 are components of a proapoptotic autoregulatory feedback loop. Mol Cell. 2008;32(6):803–814.
- Strano S, Munarriz E, Rossi M, et al. Physical interaction with yes-associated protein enhances p73 transcriptional activity. J Biol Chem. 2001;276(18):15164–15173.
- Subhashini S, Sanjeev G, Vegesna R, et al. Caspase-1 activator Ipaf is a p53-inducible gene involved in apoptosis. Oncogene. 2005;24:627–636.
- Maejima Y, Kyoi S, Zhai P, et al. Mst1 inhibits autophagy by promoting the interaction between Beclin1 and Bcl-2. Nat Med. 2013;19(11):1478–1488.
- Song Q, Mao B, Cheng J, et al. YAP enhances autophagic flux to promote breast cancer cell survival in response to nutrient deprivation. PLoS One. 2015;10(3):e0120790.
- Xiao L, Shi XY, Zhang Y, et al. YAP induces cisplatin resistance through activation of autophagy in human ovarian carcinoma cells. Onco Targets Ther. 2016;9:1105–1114.
- Strano S, Monti O, Pediconi N, et al. The transcriptional coactivator yes-associated protein drives p73 gene-target specificity in response to DNA damage. Molecular Cell. 2005;18:447–459.
- Basu S, Totty NF, Irwin MS, et al. Akt phosphorylates the yes-associated protein, YAP, to induce interaction with 14-3-3 and attenuation of p73-mediated apoptosis. Mol Cell. 2003;11(1):11–23.
- Darwin KH, Robinson LS, Miller VL. SigE is a chaperone for the Salmonella enterica serovar Typhimurium invasion protein SigD. J Bacteriol. 2001;183(4):1452–1454.
- Logie L, Ruiz-Alcaraz AJ, Keane M, et al. Sutherland C. characterization of a protein kinase B inhibitor in vitro and in insulin-treated liver cells. Diabetes. 2007;56(9):2218–2227.
- Najafov A, Sommer EM, Axten JM, et al. Characterization of GSK2334470, a novel and highly specific inhibitor of PDK1. Biochem J. 2011;433(2):357–369.
- Sarbassov DD, Guertin DA, Ali SM, et al. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science. 2005;307(5712):1098–1101.
- Franke TF. PI3K/Akt: getting it right matters. Oncogene. 2008;27:6473–6488.
- Cooper KG, Winfree S, Malik-Kale P, et al. Activation of Akt by the bacterial inositol phosphatase, SopB, is wortmannin insensitive. Plos One. 2011;6(7):e22260.
- Roppenser B, Kwon H, Canadien V, et al. Multiple host kinases contribute to Akt activation during Salmonella infection. PLoS One. 2013;8(8):e71015.
- Leyva-Rangel JP, MdeLosA H-C, Galan-Enriquez CS, et al. Bacterial clearance reverses a skewed T-cell repertoire induced by Salmonella infection. Immun Inflamm Dis. 2015;3(3):209–223.
- Rosales-Reyes R, Alpuche-Aranda C, Ramırez-Aguilar ML, et al. Survival of Salmonella enterica serovar typhimurium within late endosomal-lysosomal compartments of B lymphocytes is associated with the inability to use the vacuolar alternative major histocompatibility complex class I antigen-processing pathway. Infection and Immunity. 2005;73(7):3937–3944.
- Norris FA, Wilson MP, Wallis TS, et al. SopB, a protein required for virulence of Salmonella dublin, is an inositol phosphate phosphatase. Proc Natl Acad Sci U S A. 1998;95(24):14057–14059.
- Hu GQ, Song PX, Chen W, et al. Cirtical role for Salmonella effector SopB in regulating inflammasome activation. Mol Immunol. 2017;90:280–286.
- Kuijl C, Savage NDL, Marsman M, et al. Intracellular bacterial growth is controlled by a kinase network around PKB/AKT1. Nature. 2007;450:725–730.
- Lindsay DR, Nat FB, Yuan F, et al. Phosphoproteomic analysis of Salmonella-infected cells identifies key kinase regulators and SopB-dependent host phosphorylation events. Host-Pathogen Interactions. 2011;4(191):1–13.
- Roppenser B, Grinstein S, Brumell JH. Modulation of host phosphoinositide metabolism during Salmonella invasion by the type III secreted effector SopB. Methods Cell Biol. 2012;108:173–186.
- Chaulk SG, Lattanzi VJ, Hiemer SE, et al. The Hippo pathway effectors TAZ/YAP regulate dicer expression and microRNA biogenesis through Let-7. J Biol Chem. 2014;289(4):1886–1891.
- Diamond CE, Leong KWK, Vacca M, et al. Salmonella typhimurium-induced IL-1 release from primary human monocytes requires NLRP3 and can occur in the absence of pyroptosis. Sci Rep. 2017;7(1):6861.
- Kayagaki N, Ib S, Bl L, et al. Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling. Nature. 2015;526(7575):666–671.
- Liu X, Zhang ZB, Ruan JB, et al. Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores. Nature. 2016;535(7610):153-+.
- Evavold CL, Ruan J, Tan Y, et al. The pore-forming protein gasdermin D regulates interleukin-1 secretion from living macrophages. Immunity. 2018;48(1): 35–44 e6.
- Heilig R, Dick MS, Sborgi L, et al. The Gasdermin-D pore acts as a conduit for IL-1beta secretion in mice. Eur J Immunol. 2018;48(4):584–592.
- Harris J. Autophagy and cytokines. Cytokine. 2011;56(2):140–144.
- Shi J, Wang H, Guan H, et al. IL10 inhibits starvation-induced autophagy in hypertrophic scar fibroblasts via cross talk between the IL10-IL10R-STAT3 and IL10-AKT-mTOR pathways. Cell Death Dis. 2016;7:e2133.
- Neves P, Lampropoulou V, Calderon-Gomez E, et al. Signaling via the MyD88 adaptor protein in B cells suppresses protective immunity during Salmonella typhimurium infection. Immunity. 2010;33(5):777–790.
- Ruan HH, Zhang Z, Wang SY, et al. Tumor necrosis factor receptor-associated factor 6 (TRAF6) mediates ubiquitination-dependent STAT3 activation upon Salmonella Typhimurium infection. Infect Immun. 2017.
- Datsenko KA, Wanner BL. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci U S A. 2000;97(12):6640–6645.
- Buchmeier NA, Heffron F. Intracellular survival of wild-type Salmonella typhimurium and macrophage-sensitive mutants in diverse populations of macrophages. Infect Immun. 1989;57(1):1–7.