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Phenotypic characterization of a conserved inner membrane protein YhcB in Escherichia coli
Chul Gi Sung , Umji Choi , Chang-Ro Lee
J. Microbiol. 2020;58(7):598-605.   Published online April 22, 2020
DOI: https://doi.org/10.1007/s12275-020-0078-4
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  • 6 Web of Science
  • 5 Crossref
AbstractAbstract
Although bacteria have diverse membrane proteins, the function of many of them remains unknown or uncertain even in Escherichia coli. In this study, to investigate the function of hypothetical membrane proteins, genome-wide analysis of phenotypes of hypothetical membrane proteins was performed under various envelope stresses. Several genes responsible for adaptation to envelope stresses were identified. Among them, deletion of YhcB, a conserved inner membrane protein of unknown function, caused high sensitivities to various envelope stresses and increased membrane permeability, and caused growth defect under normal growth conditions. Furthermore, yhcB deletion resulted in morphological aberration, such as branched shape, and cell division defects, such as filamentous growth and the generation of chromosome- less cells. The analysis of antibiotic susceptibility showed that the yhcB mutant was highly susceptible to various anti-folate antibiotics. Notably, all phenotypes of the yhcB mutant were completely or significantly restored by YhcB without the transmembrane domain, indicating that the localization of YhcB on the inner membrane is dispensable for its function. Taken together, our results demonstrate that YhcB is involved in cell morphology and cell division in a membrane localization-independent manner.

Citations

Citations to this article as recorded by  
  • Co-ordinated assembly of the multilayered cell envelope of Gram-negative bacteria
    Elayne M Fivenson, Laurent Dubois, Thomas G Bernhardt
    Current Opinion in Microbiology.2024; 79: 102479.     CrossRef
  • Loss of YhcB results in overactive fatty acid biosynthesis
    Hannah M. Stanley, M. Stephen Trent, K. Heran Darwin
    mBio.2024;[Epub]     CrossRef
  • A New Factor LapD Is Required for the Regulation of LpxC Amounts and Lipopolysaccharide Trafficking
    Alicja Wieczorek, Anna Sendobra, Akshey Maniyeri, Magdalena Sugalska, Gracjana Klein, Satish Raina
    International Journal of Molecular Sciences.2022; 23(17): 9706.     CrossRef
  • Loss of YhcB results in dysregulation of coordinated peptidoglycan, LPS and phospholipid synthesis during Escherichia coli cell growth
    Emily C. A. Goodall, Georgia L. Isom, Jessica L. Rooke, Karthik Pullela, Christopher Icke, Zihao Yang, Gabriela Boelter, Alun Jones, Isabel Warner, Rochelle Da Costa, Bing Zhang, James Rae, Wee Boon Tan, Matthias Winkle, Antoine Delhaye, Eva Heinz, Jean-F
    PLOS Genetics.2021; 17(12): e1009586.     CrossRef
  • The inner membrane protein LapB is required for adaptation to cold stress in an LpxC-independent manner
    Han Byeol Lee, Si Hyoung Park, Chang-Ro Lee
    Journal of Microbiology.2021; 59(7): 666.     CrossRef
Review
MINIREVIEW] Shiga Toxins Expressed by Human Pathogenic Bacteria Induce Immune Responses in Host Cells
Moo-Seung Lee , Myung Hee Kim , Vernon L. Tesh
J. Microbiol. 2013;51(6):724-730.   Published online December 19, 2013
DOI: https://doi.org/10.1007/s12275-013-3429-6
  • 55 View
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  • 21 Crossref
AbstractAbstract
Shiga toxins are a family of genetically and structurally related toxins that are the primary virulence factors produced by the bacterial pathogens Shigella dysenteriae serotype 1 and certain Escherichia coli strains. The toxins are multifunctional proteins inducing protein biosynthesis inhibition, ribotoxic and ER stress responses, apoptosis, autophagy, and inflammatory cytokine and chemokine production. The regulated induction of inflammatory responses is key to minimizing damage upon injury or pathogen-mediated infections, requiring the concerted activation of multiple signaling pathways to control cytokine/chemokine expression. Activation of host cell signaling cascades is essential for Shiga toxinmediated proinflammatory responses and the contribution of the toxins to virulence. Many studies have been reported defining the inflammatory response to Shiga toxins in vivo and in vitro, including production and secretion of tumor necrosis factor alpha (TNF-α), interleukin-1β (IL-1β), macrophage inflammatory protein-1α/β (MIP-1α/β), macrophage chemoattractant monocyte chemoattractant protein 1 (MCP-1), interleukin 8 (IL-8), interleukin 6 (IL-6), and Groβ. These cytokines and chemokines may contribute to damage in the colon and development of life threatening conditions such as acute renal failure (hemolytic uremic syndrome) and neurological abnormalities. In this review, we summarize recent findings in Shiga toxin-mediated inflammatory responses by different types of cells in vitro and in animal models. Signaling pathways involved in the inflammatory responses are briefly reviewed.

Citations

Citations to this article as recorded by  
  • Involvement of aquaporins in Shiga toxin-induced swelling and water transport dysfunction in human renal microvascular endothelial cells
    Fernando D. Gomez, Julieta Reppetti, Romina S. Alvarez, Daniel C. Girón Reyes, Flavia Sacerdoti, Alejandro Balestracci, Alicia E. Damiano, Nora A. Martínez, Gisela Di Giusto, María M. Amaral
    Biochimica et Biophysica Acta (BBA) - Molecular Cell Research.2025; 1872(1): 119866.     CrossRef
  • Distribution characteristics of antibiotic resistance in direct-eating food and analysis of Citrobacter freundii genome and pathogenicity
    Qing Wang, Xuening Wang, Shaojing Sun, Litao Wang, Yan Sun, Xinyan Guo, Na Wang, Bin Chen
    World Journal of Engineering.2024; 21(6): 1095.     CrossRef
  • Significance of Pulmonary Endothelial Injury and the Role of Cyclooxygenase-2 and Prostanoid Signaling
    Rosa Nickl, Sandra Hauser, Jens Pietzsch, Torsten Richter
    Bioengineering.2023; 10(1): 117.     CrossRef
  • The predominance of Shiga toxin-producing E. coli in the Southeast Coast of India
    Kannan Kamala, Shanmugam Rajeshkumar, Pitchiah Sivaperumal
    Marine Pollution Bulletin.2022; 174: 113188.     CrossRef
  • Gene expression profile and injury sites in mice treated with Shiga toxin 2 and lipopolysaccharide as a Shiga toxin-associated hemolytic uremic syndrome model
    Yohei Kume, Hayato Go, Ryo Maeda, Kazuhide Suyama, Tsutomu Mori, Yukihiko Kawasaki, Koichi Hashimoto, Mitsuaki Hosoya
    Physiological Genomics.2022; 54(5): 153.     CrossRef
  • SARS-CoV-2 and Emerging Foodborne Pathogens: Intriguing Commonalities and Obvious Differences
    Ahmed G. Abdelhamid, Julia N. Faraone, John P. Evans, Shan-Lu Liu, Ahmed E. Yousef
    Pathogens.2022; 11(8): 837.     CrossRef
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    Romina S. Álvarez, Fernando D. Gómez, Elsa Zotta, Adrienne W. Paton, James C. Paton, Cristina Ibarra, Flavia Sacerdoti, María M. Amaral
    Toxins.2021; 13(8): 536.     CrossRef
  • Shiga toxin remodels the intestinal epithelial transcriptional response to Enterohemorrhagic Escherichia coli
    Alyson R. Warr, Carole J. Kuehl, Matthew K. Waldor, Igor Eric Brodsky
    PLOS Pathogens.2021; 17(2): e1009290.     CrossRef
  • Comparative Transcriptomics of Shiga Toxin-Producing and Commensal Escherichia coli and Cytokine Responses in Colonic Epithelial Cell Culture Infections
    Lisa M. Harrison, David W. Lacher, Mark K. Mammel, Susan R. Leonard
    Frontiers in Cellular and Infection Microbiology.2020;[Epub]     CrossRef
  • Lactobacillus acidophilus attenuates toxin production by Vibrio cholerae and shigella dysenteriae following intestinal epithelial cells infection
    Shabnam Zeighamy Alamdary, Bita Bakhshi
    Microbial Pathogenesis.2020; 149: 104543.     CrossRef
  • Roles of Shiga Toxins in Immunopathology
    Moo-Seung Lee, Vernon L. Tesh
    Toxins.2019; 11(4): 212.     CrossRef
  • Nucleolar fibrillarin is an evolutionarily conserved regulator of bacterial pathogen resistance
    Varnesh Tiku, Chun Kew, Parul Mehrotra, Raja Ganesan, Nirmal Robinson, Adam Antebi
    Nature Communications.2018;[Epub]     CrossRef
  • Simulation Study of cDNA Dataset to Investigate Possible Association of Differentially Expressed Genes of Human THP1-Monocytic Cells in Cancer Progression Affected by Bacterial Shiga Toxins
    Syed A. Muhammad, Jinlei Guo, Thanh M. Nguyen, Xiaogang Wu, Baogang Bai, X. Frank Yang, Jake Y. Chen
    Frontiers in Microbiology.2018;[Epub]     CrossRef
  • Anti-inflammatory agents reduce microglial response, demyelinating process and neuronal toxin uptake in a model of encephalopathy produced by Shiga Toxin 2
    Alipio Pinto, Clara Berdasco, David Arenas-Mosquera, Adriana Cangelosi, Patricia A. Geoghegan, Myriam C. Nuñez, Jorge Goldstein
    International Journal of Medical Microbiology.2018; 308(8): 1036.     CrossRef
  • Shiga Toxins as Multi-Functional Proteins: Induction of Host Cellular Stress Responses, Role in Pathogenesis and Therapeutic Applications
    Moo-Seung Lee, Sunwoo Koo, Dae Jeong, Vernon Tesh
    Toxins.2016; 8(3): 77.     CrossRef
  • Shiga Toxins Activate the NLRP3 Inflammasome Pathway To Promote Both Production of the Proinflammatory Cytokine Interleukin-1β and Apoptotic Cell Death
    Moo-Seung Lee, Haenaem Kwon, Eun-Young Lee, Dong-Jae Kim, Jong-Hwan Park, Vernon L. Tesh, Tae-Kwang Oh, Myung Hee Kim, B. A. McCormick
    Infection and Immunity.2016; 84(1): 172.     CrossRef
  • Angiotensin-(1–7) protects from brain damage induced by shiga toxin 2-producing enterohemorrhagicEscherichia coli
    Jorge Goldstein, Tomás R. Carden, María J. Perez, Carlos A. Taira, Christian Höcht, Mariela M. Gironacci
    American Journal of Physiology-Regulatory, Integrative and Comparative Physiology.2016; 311(6): R1173.     CrossRef
  • Bacteria, the endoplasmic reticulum and the unfolded protein response: friends or foes?
    Jean Celli, Renée M. Tsolis
    Nature Reviews Microbiology.2015; 13(2): 71.     CrossRef
  • The roles of the virulence factor IpaB in Shigella spp. in the escape from immune cells and invasion of epithelial cells
    Shih-Chun Yang, Chi-Feng Hung, Ibrahim A. Aljuffali, Jia-You Fang
    Microbiological Research.2015; 181: 43.     CrossRef
  • Update on molecular epidemiology of Shigella infection
    Ila F.N. Lima, Alexandre Havt, Aldo A.M. Lima
    Current Opinion in Gastroenterology.2015; 31(1): 30.     CrossRef
  • Shiga Toxin (Stx) Classification, Structure, and Function
    Angela R. Melton-Celsa, Vanessa Sperandio, Carolyn J. Hovde
    Microbiology Spectrum.2014;[Epub]     CrossRef

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