Innate immune response of host cells infected with Salmonella

Open Access

Issue		BIO Web Conf. Volume 111, 2024 2024 6^th International Conference on Biotechnology and Biomedicine (ICBB 2024)


Article Number		01022
Number of page(s)		7
Section		Genetic Engineering and Biotechnology Innovation
DOI		https://doi.org/10.1051/bioconf/202411101022
Published online		31 May 2024

X. Xu, Y. Chen, H. Pan, et al. Genomic characterization of Salmonella Uzaramo for human invasive infection. [J]. Microbial Genomics, 6, mgen000401(2020) [Google Scholar]
R.R. Wittler. Foodborne and Waterborne Illness. [J]. Pediatrics in Review, 44, 81–91 (2023) [CrossRef] [PubMed] [Google Scholar]
R. Silva, F.M. Gomes. Evolution of the Major Components of Innate Immunity in Animals. [J]. J Mol Evol, 92, 3–20 (2024) [CrossRef] [PubMed] [Google Scholar]
K. Seo, J. Seo, J. Yeun, et al. The role of mucosal barriers in human gut health. [J]. Arch Pharm Res, 44, 325-41(2021) [CrossRef] [PubMed] [Google Scholar]
M. Sadeghi, S. Dehnavi, M. Sharifat, et al. Innate immune cells: Key players of orchestra in modulating tumor microenvironment (TME). [J]. Heliyon, 10, e27480(2024) [CrossRef] [Google Scholar]
S. Shaji, R.K. Selvaraj, R. Shanmugasundaram. Salmonella Infection in Poultry: A Review on the Pathogen and Control Strategies. [J]. Microorganisms, 11, 2814 (2023) [CrossRef] [Google Scholar]
M.J. Worley. Salmonella Bloodstream Infections. [J]. Trop Med Infect Dis, 8, 487 (2023) [CrossRef] [Google Scholar]
J.R. Kurtz, J.A. Goggins, J.B. McLachlan. Salmonella infection: Interplay between the bacteria and host immune system. [J]. Immunology Letters, 190, 42–50 (2017) [CrossRef] [Google Scholar]
M. Wang, I.H. Qazi, L. Wang, et al. Salmonella Virulence and Immune Escape. [J]. Microorganisms, 8, 407(2020) [CrossRef] [Google Scholar]
H. Bao, S. Wang, J.-H. Zhao, et al. Salmonella secretion systems: Differential roles in pathogen-host interactions. [J]. Microbiological Research, 241, 126591(2020) [CrossRef] [Google Scholar]
T. Rehman, L. Yin, M.B. Latif, et al. Adhesive mechanism of different Salmonella fimbrial adhesins. [J]. Microbial Pathogenesis, 137, 103748(2019) [CrossRef] [Google Scholar]
B. Yuan, J. Scholz, J. Wald, et al. Structural basis for subversion of host cell actin cytoskeleton during Salmonella infection. [J]. Science Advances, 9, eadj5777(2023) [CrossRef] [Google Scholar]
V. Kumar, J.H. Stewart. cGLRs Join Their Cousins of Pattern Recognition Receptor Family to Regulate Immune Homeostasis. [J]. Int J Mol Sci, 25, 1828 (2024) [CrossRef] [Google Scholar]
Q. Deng, S. Yang, K. Huang, et al. NLRP6 induces RIP1 kinase-dependent necroptosis via TAK1-mediated p38(MAPK)/MK2 phosphorylation in S. typhimurium infection. [J]. iScience, 27, 109339(2024) [CrossRef] [Google Scholar]
H. Huang, Z. Even, Z. Wang, et al. Proteomics Profiling Reveals Regulation of Immune Response to Salmonella enterica Serovar Typhimurium Infection in Mice. [J]. Infect Immun, 91, e00499-22(2023) [Google Scholar]
F. Yang, X. Sheng, X. Huang, et al. Interactions between Salmonella and host macrophages -Dissecting NF-kappaB signaling pathway responses. [J]. Microb Pathog, 154, 104846(2021) [CrossRef] [Google Scholar]
D. Bierschenk, D. Boucher, K. Schroder. Salmonella-induced inflammasome activation in humans. [J]. Mol Immunol, 86, 38–43 (2017) [CrossRef] [Google Scholar]
P.J. Hume, V. Singh, A.C. Davidson, et al. Swiss Army Pathogen: The Salmonella Entry Toolkit. [J]. Frontiers in Cellular and Infection Microbiology, 7, 348(2017) [CrossRef] [Google Scholar]
S. Liu, Z. Dong, W. Tang, et al. Dietary iron regulates intestinal goblet cell function and alleviates Salmonella typhimurium invasion in mice. [J]. Sci China Life Sci, 66, 2006-19(2023) [CrossRef] [PubMed] [Google Scholar]
G.M.H. Birchenough, M.E.V. Johansson. Forming a mucus barrier along the colon. [J]. Science, 370, 402–03 (2020) [CrossRef] [PubMed] [Google Scholar]
M.A. McGuckin, J.M. Davies, P. Felgner, et al. MUC13 Cell Surface Mucin Limits Salmonella Typhimurium Infection by Protecting the Mucosal Epithelial Barrier. [J]. Cellular and Molecular Gastroenterology and Hepatology, 16, 985-1009 (2023) [CrossRef] [Google Scholar]
A. Fusco, V. Savio, M. Donniacuo, et al. Antimicrobial Peptides Human Beta-Defensin-2 and -3 Protect the Gut During Candida albicans Infections Enhancing the Intestinal Barrier Integrity: In Vitro Study. [J]. Frontiers in Cellular and Infection Microbiology, 11, 666900(2021) [CrossRef] [Google Scholar]
U. Meyer-Hoffert, M.W. Hornef, B. Henriques-Normark, et al. Secreted enteric antimicrobial activity localises to the mucus surface layer. [J]. Gut, 57, 764–71 (2008) [CrossRef] [PubMed] [Google Scholar]
Q. Wang, Y. Xu, J. Hu. Intracellular mechanism of antimicrobial peptide HJH-3 against Salmonella pullorum. [J]. RSC Advances, 12, 14485–91 (2022) [CrossRef] [Google Scholar]
Y. Xu, Q. Wang, M. Dong, et al. Evaluation of the efficacy of the antimicrobial peptide HJH-3 in chickens infected with Salmonella Pullorum. [J]. Frontiers in Microbiology, 14, 1102789 (2023) [CrossRef] [Google Scholar]
G. Zhou, J. Wang, X. Zhu, et al. Induction of maggot antimicrobial peptides and treatment effect inSalmonella pullorum-infected chickens. [J]. Journal of Applied Poultry Research, 23, 376–83 (2014) [CrossRef] [Google Scholar]
S. Shen, F. Ren, J. He, et al. Recombinant Antimicrobial Peptide OaBac5mini Alleviates Inflammation in Pullorum Disease Chicks by Modulating TLR4/MyD88/NF-kappaB Pathway. [J]. Animals (Basel), 13, 1515 (2023) [Google Scholar]
S. Herp, S. Brugiroux, D. Garzetti, et al. Mucispirillum schaedleri Antagonizes Salmonella Virulence to Protect Mice against Colitis. [J]. Cell Host & Microbe, 25, 681-94.e8(2019) [CrossRef] [Google Scholar]
X. Peng, A. Ed-Dra, Y. Song, et al. Lacticaseibacillus rhamnosus alleviates intestinal inflammation and promotes microbiota-mediated protection against Salmonella fatal infections. [J]. Front Immunol, 13, 973224 (2022) [CrossRef] [Google Scholar]
Q.R. Ducarmon, R.D. Zwittink, B.V.H. Hornung, et al. Gut Microbiota and Colonization Resistance against Bacterial Enteric Infection. [J]. Microbiology and Molecular Biology Reviews, 83, (2019) [Google Scholar]
S. Xie, H. Zhang, R.S. Matjeke, et al. Bacillus coagulans protect against Salmonella enteritidis-induced intestinal mucosal damage in young chickens by inducing the differentiation of goblet cells. [J]. Poultry Science, 101, 101639 (2022) [CrossRef] [Google Scholar]
G. Chemin, A. De Giacomoni, P.E. Joubert. Plasticity of programmed cell death pathways while fighting Salmonella, plenty of possibilities to defend against pathogens. [J]. Med Sci (Paris), 37, 814–16 (2021) [Google Scholar]
G.S. Kopeina, B. Zhivotovsky. Programmed cell death: Past, present and future. [J]. Biochem Biophys Res Commun, 633, 55–58 (2022) [CrossRef] [Google Scholar]
J.M. Stringer, L.R. Alesi, A.L. Winship, et al. Beyond apoptosis: evidence of other regulated cell death pathways in the ovary throughout development and life. [J]. Human Reproduction Update, 29, 434–56 (2023) [CrossRef] [PubMed] [Google Scholar]
H. Miyashita, D. Oikawa, S. Terawaki, et al. Crosstalk Between NDP52 and LUBAC in Innate Immune Responses, Cell Death, and Xenophagy. [J]. Front Immunol, 12, 635475 (2021) [CrossRef] [Google Scholar]
N. Ketelut-Carneiro, K.A. Fitzgerald. Apoptosis, Pyroptosis, and Necroptosis—Oh My! The Many Ways a Cell Can Die. [J]. Journal of Molecular Biology, 434, 167378 (2022) [CrossRef] [Google Scholar]
T.J. Abele, Z.P. Billman, L. Li, et al. Apoptotic signaling clears engineered Salmonella in an organspecific manner. [J]. eLife, 12, RP89210(2023) [CrossRef] [Google Scholar]
C. Yu, F. Du, C. Zhang, et al. Salmonella enterica serovar Typhimurium sseK3 induces apoptosis and enhances glycolysis in macrophages. [J]. BMC Microbiology, 20, 151 (2020) [CrossRef] [Google Scholar]
K. Ding, C. Zhang, J. Li, et al. CAMP Receptor Protein of Salmonella enterica Serovar Typhimurium Modulate Glycolysis in Macrophages to Induce Cell Apoptosis. [J]. Current Microbiology, 76, 1–6 (2019) [CrossRef] [PubMed] [Google Scholar]
H.-H. Lin, H.-L. Chen, C.-C. Weng, et al. Activation of apoptosis by Salmonella pathogenicity island-1 effectors through both intrinsic and extrinsic pathways in Salmonella-infected macrophages. [J]. Journal of Microbiology, Immunology and Infection, 54, 616–626 (2021) [CrossRef] [Google Scholar]
K. Venkataranganayaka Abhilasha, G. Kedihithlu Marathe. Bacterial lipoproteins in sepsis. [J]. Immunobiology, 226, 152128 (2021) [CrossRef] [Google Scholar]
J.E. Casanova. Bacterial Autophagy: Offense and Defense at the Host-Pathogen Interface. [J]. Cellular and Molecular Gastroenterology and Hepatology, 4, 237–43 (2017) [CrossRef] [Google Scholar]
L. Zheng, F. Wei, G. Li. The crosstalk between bacteria and host autophagy: host defense or bacteria offense. [J]. J Microbiol, 60, 451–60 (2022) [CrossRef] [Google Scholar]
L.A. Knodler. Salmonella enterica: living a double life in epithelial cells. [J]. Current Opinion in Microbiology, 23, 23–31 (2015) [CrossRef] [Google Scholar]
L.H. Wu, C.R. Pangilinan, C.H. Lee. Downregulation of AKT/mTOR signaling pathway for Salmonella-mediated autophagy in human anaplastic thyroid cancer. [J]. Journal of Cancer, 13, 3268–79 (2022) [CrossRef] [Google Scholar]
X. Cen, Z. Li, X. Chen. Ubiquitination in the regulation of autophagy. [J]. Acta Biochim Biophys Sin (Shanghai), 55, 1348–57 (2023) [CrossRef] [PubMed] [Google Scholar]
M. Polajnar, M.S. Dietz, M. Heilemann, et al. Expanding the host cell ubiquitylation machinery targeting cytosolic Salmonella. [J]. EMBO reports, 18, 1572–85 (2017) [CrossRef] [PubMed] [Google Scholar]
D.H. Kwon, H.K. Song. A Structural View of Xenophagy, a Battle between Host and Microbes. [J]. Molecules and Cells, 41, 27–34 (2018) [Google Scholar]
K. Liu, L. Kong, D.B. Graham, et al. SAC1 regulates autophagosomal phosphatidylinositol-4-phosphate for xenophagy-directed bacterial clearance. [J]. Cell Reports, 36, 109434 (2021) [CrossRef] [Google Scholar]
Jamaal L. Benjamin, R. Sumpter, B. Levine, et al. Intestinal Epithelial Autophagy Is Essential for Host Defense against Invasive Bacteria. [J]. Cell Host & Microbe, 13, 723–34 (2013) [CrossRef] [Google Scholar]
A. Suwandi, M.B. Menon, A. Kotlyarov, et al. P38MAPK/MK2 signaling stimulates host cells autophagy pathways to restrict Salmonella infection. [J]. Frontiers in Immunology, 14, 1245443 (2023) [CrossRef] [Google Scholar]
Q. Chai, Z. Lei, C.H. Liu. Pyroptosis modulation by bacterial effector proteins. [J]. Seminars in Immunology, 69, 101804 (2023) [CrossRef] [Google Scholar]
H.C. Huston, M.J. Anderson, S.L. Fink. Pyroptosis and the cellular consequences ofgasdermin pores. [J]. Seminars in Immunology, 69, 101803 (2023) [CrossRef] [Google Scholar]
F. Shao. Gasdermins: making poresfor pyroptosis. [J]. Nature Reviews Immunology, 21, 620–21 (2021) [CrossRef] [Google Scholar]
J.C. Santos, D. Boucher, L.K. Schneider, et al. Human GBP1 binds LPS to initiate assembly of a caspase-4 activating platform on cytosolic bacteria. [J]. Nature Communications, 11, 3276 (2020) [CrossRef] [Google Scholar]
C. Rogers, T. Fernandes-Alnemri, L. Mayes, et al. Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death. [J]. Nature Communications, 8, 14128 (2017) [CrossRef] [Google Scholar]
S.M. Crowley, X. Han, J.M. Allaire, et al. Intestinal restriction of Salmonella Typhimurium requires caspase-1 and caspase-11 epithelial intrinsic inflammasomes. [J]. PLOS Pathogens, 16, e1008498 (2020) [CrossRef] [Google Scholar]
L. Xiong, S. Wang, J.W. Dean, et al. Group 3 innate lymphoid cell pyroptosis represents a host defence mechanism against Salmonella infection. [J]. Nature Microbiology, 7, 1087–99 (2022) [CrossRef] [Google Scholar]

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