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Caspase-3 inhibitor inhibits enterovirus D68 production
Wenbo Huo , Jinghua Yu , Chunyu Liu , Ting Wu , Yue Wang , Xiangling Meng , Fengmei Song , Shuxia Zhang , Ying Su , Yumeng Liu , Jinming Liu , Xiaoyan Yu , Shucheng Hua
J. Microbiol. 2020;58(9):812-820.   Published online September 1, 2020
DOI: https://doi.org/10.1007/s12275-020-0241-y
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  • 8 Web of Science
  • 8 Crossref
AbstractAbstract
Enterovirus D68 (EVD68) is an emerging pathogen that recently caused a large worldwide outbreak of severe respiratory disease in children. However, the relationship between EVD68 and host cells remains unclear. Caspases are involved in cell death, immune response, and even viral production. We found that caspase-3 was activated during EVD68 replication to induce apoptosis. Caspase-3 inhibitor (Z-DEVDFMK) inhibited viral production, protected host cells from the cytopathic effects of EVD68 infection, and prevented EVD68 from regulating the host cell cycle at G0/G1. Meanwhile, caspase-3 activator (PAC-1) increased EVD68 production. EVD68 infection therefore activates caspase-3 for virus production. This knowledge provides a potential direction for the prevention and treatment of disease related to EVD68.

Citations

Citations to this article as recorded by  
  • Non-Polio Enterovirus Inhibitors: Scaffolds, Targets, and Potency─What’s New?
    Hugo Fernando Georges Roux, Franck Touret, Pascal Rathelot, Pietro Sciò, Antonio Coluccia, Patrice Vanelle, Manon Roche
    ACS Infectious Diseases.2024;[Epub]     CrossRef
  • Mode of cell death in the penile cavernous tissue of type 1 diabetes mellitus rats
    Jing Li, Qilan Jiang, Jun Jiang, Rui Jiang
    The Journal of Sexual Medicine.2024; 21(8): 652.     CrossRef
  • MDA5 Enhances Invasive Candida albicans Infection by Regulating Macrophage Apoptosis and Phagocytosis/Killing Functions
    Yayun Chen, Qian Jiang, Furong Qing, Junxia Xue, Qiuxiang Xiao, Wenji He, Lina Sui, Zhiping Liu
    Inflammation.2024; 47(1): 191.     CrossRef
  • Caspase-8 activation regulates enterovirus D68 infection-induced inflammatory response and cell death
    Yuanyuan Zhou, Chongtao Zhang, Yuhan Zhang, Fei Li, Jun Shen
    Biosafety and Health.2024; 6(3): 171.     CrossRef
  • Enterovirus D68 Infection Induces TDP-43 Cleavage, Aggregation, and Neurotoxicity
    Lili Zhang, Jiaxin Yang, Huili Li, Zhe Zhang, Zhilin Ji, Lirong Zhao, Wei Wei, Rebecca Ellis Dutch
    Journal of Virology.2023;[Epub]     CrossRef
  • Inhibitory effect of tanshinone IIA, resveratrol and silibinin on enterovirus 68 production through inhibiting ATM and DNA-PK pathway
    Ying Su, Ting Wu, Xiao-Yan Yu, Wen-Bo Huo, Shao-Hua Wang, Chen Huan, Yu-Meng Liu, Jin-Ming Liu, Min-Na Cui, Xin-Hua Li, Jing-Hua Yu
    Phytomedicine.2022; 99: 153977.     CrossRef
  • Urolithin A inhibits enterovirus 71 replication and promotes autophagy and apoptosis of infected cells in vitro
    Shengyu Wang, Junhua Qiao, Yaping Chen, Langfei Tian, Xin Sun
    Archives of Virology.2022; 167(10): 1989.     CrossRef
  • Mst1/2-ALK promotes NLRP3 inflammasome activation and cell apoptosis during Listeria monocytogenes infection
    Aijiao Gao, Huixin Tang, Qian Zhang, Ruiqing Liu, Lin Wang, Yashan Liu, Zhi Qi, Yanna Shen
    Journal of Microbiology.2021; 59(7): 681.     CrossRef
Research Support, Non-U.S. Gov'ts
Cell-Surface Expression of Aspergillus saitoi-Derived Functional α-1,2-Mannosidase on Yarrowia lipolytica for Glycan Remodeling
Hye Yun Moon , Trinh Luu Van , Seon Ah Cheon , Jinho Choo , Jeong-Yoon Kim , Hyun Ah Kang
J. Microbiol. 2013;51(4):506-514.   Published online August 30, 2013
DOI: https://doi.org/10.1007/s12275-013-3344-x
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  • 13 Crossref
AbstractAbstract
Expression of proteins on the surface of yeast has a wide range of applications, such as development of live vaccines, screening of antibody libraries, and use as whole-cell biocatalysts. The hemiascomycetes yeast Yarrowia lipolytica has been raised as a potential host for heterologous expression of recombinant proteins. In this study, we report the expression of Aspergillus saitoi α-1,2-mannosidase, encoded by the msdS gene, on the cell surface of Y. lipolytica. As the first step to achieve the secretory expression of msdS protein, four different signal sequences-derived from the endogenous Y. lipolytica Lip2 and Xpr2 prepro regions and the heterologous A. niger α-amylase and rice α-amylase signal sequences-were analyzed for their secretion efficiency. It was shown that the YlLip2 prepro sequence was most efficient in directing the secretory expression of msdS in fully N-glycosylated forms. The surface display of msdS was subsequently directed by fusing GPI anchoring motifs derived from Y. lipolytica cell wall proteins, YlCwp1p and YlYwp1p, respectively, to the C-terminus of the Lip2 prepro-msdS protein. The expression of actively functional msdS protein on the cell surface was confirmed by western blot, flow cytometry analysis, along with the α-1,2-mannosidase activity assay using intact Y. lipolytica cells as the enzyme source. Furthermore, the glycoengineered Y. lipolytica Δoch1Δmpo1 strains displaying α-1,2-mannosidase were able to convert Man8GlcNAc2 to Man5GlcNAc2 efficiently on their cell-wall mannoproteins, demonstrating its potential used for glycoengineering in vitro or in vivo.

Citations

Citations to this article as recorded by  
  • Engineering novel Yarrowia lipolytica whole-cell biocatalysts by cell surface display of the native Lip2 lipase for biodiesel production
    Maria Orfanidou, Eleftheria Panagiotidou, Antonios M. Makris, Eleni Theodosiou
    Biotechnology for the Environment.2025;[Epub]     CrossRef
  • Yeast Surface Display System: Strategies for Improvement and Biotechnological Applications
    Karla V. Teymennet-Ramírez, Fernando Martínez-Morales, María R. Trejo-Hernández
    Frontiers in Bioengineering and Biotechnology.2022;[Epub]     CrossRef
  • Dietary intake of GDF11 delays the onset of several biomarkers of aging in male mice through anti-oxidant system via Smad2/3 pathway
    Lili Song, Fei Wu, Congjun Li, Shicui Zhang
    Biogerontology.2022; 23(3): 341.     CrossRef
  • Hydrolytic secretome engineering in Yarrowia lipolytica for consolidated bioprocessing on polysaccharide resources: review on starch, cellulose, xylan, and inulin
    Ewelina Celińska, Jean-Marc Nicaud, Wojciech Białas
    Applied Microbiology and Biotechnology.2021; 105(3): 975.     CrossRef
  • Yarrowia lipolytica Strains and Their Biotechnological Applications: How Natural Biodiversity and Metabolic Engineering Could Contribute to Cell Factories Improvement
    Catherine Madzak
    Journal of Fungi.2021; 7(7): 548.     CrossRef
  • Engineering Yarrowia lipolytica for Use in Biotechnological Applications: A Review of Major Achievements and Recent Innovations
    Catherine Madzak
    Molecular Biotechnology.2018; 60(8): 621.     CrossRef
  • Synthetic biology tools for engineering Yarrowia lipolytica
    M. Larroude, T. Rossignol, J.-M. Nicaud, R. Ledesma-Amaro
    Biotechnology Advances.2018; 36(8): 2150.     CrossRef
  • Development of recombinant Yarrowia lipolytica producing virus-like particles of a fish nervous necrosis virus
    Van-Trinh Luu, Hye Yun Moon, Jee Youn Hwang, Bo-Kyu Kang, Hyun Ah Kang
    Journal of Microbiology.2017; 55(8): 655.     CrossRef
  • Using a vector pool containing variable-strength promoters to optimize protein production in Yarrowia lipolytica
    Rémi Dulermo, François Brunel, Thierry Dulermo, Rodrigo Ledesma-Amaro, Jérémy Vion, Marion Trassaert, Stéphane Thomas, Jean-Marc Nicaud, Christophe Leplat
    Microbial Cell Factories.2017;[Epub]     CrossRef
  • Yarrowia lipolytica: recent achievements in heterologous protein expression and pathway engineering
    Catherine Madzak
    Applied Microbiology and Biotechnology.2015; 99(11): 4559.     CrossRef
  • Biotechnological applications of Yarrowia lipolytica: Past, present and future
    Hu-Hu Liu, Xiao-Jun Ji, He Huang
    Biotechnology Advances.2015; 33(8): 1522.     CrossRef
  • Functional characterization of extracellular chitinase encoded by the YlCTS1 gene in a dimorphic yeast Yarrowia lipolytica
    Jeong-Nam Park, Chang Pyo Han, Dong-Jik Lee, Seon Ah Cheon, Hyun Ah Kang
    Journal of Microbiology.2014; 52(4): 284.     CrossRef
  • Characterization of putative glycosylphosphatidylinositol-anchoring motifs for surface display in the methylotrophic yeast Hansenula polymorpha
    Seon Ah Cheon, Jinhee Jung, Jin Ho Choo, Doo-Byoung Oh, Hyun Ah Kang
    Biotechnology Letters.2014; 36(10): 2085.     CrossRef
Molecular Analysis of a Prolonged Spread of Klebsiella pneumoniae Co-producing DHA-1 and SHV-12 β-Lactamases
Young Kyung Yoon , Hye Won Cheong , Hyunjoo Pai , Kyoung Ho Roh , Jeong Yeon Kim , Dae Won Park , Jang Wook Sohn , Seung Eun Lee , Byung Chul Chun , Hee Sun Sim , Min Ja Kim
J. Microbiol. 2011;49(3):363-368.   Published online June 30, 2011
DOI: https://doi.org/10.1007/s12275-011-0491-9
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  • 4 Scopus
AbstractAbstract
The study investigated molecular mechanisms for prolonged nosocomial spread of multidrug-resistant Klebsiella pneumoniae co-producing plasmid-mediated AmpC β-lactamase DHA-1 and extended-spectrum β-lactamase SHV-12. Forty-eight clinical isolates of K. pneumonia, resistant to the extended-spectrum cephalosporins, were collected in a 750-bed university hospital over a year. The isolates were characterized for PCR-based β-lactamase genotypes, isoelectric focusing and pulsed-field gel electrophoresis (PFGE) profiles. Resistance transfer was performed by plasmid conjugation and confirmed by a duplex-PCR and Southern hybridization. On β-lactamase typing, the strains producing only the DHA-1 enzyme (n=17) or co-producing DHA-1 and SHV-12 enzymes (n=15) were predominant. Judging from a one year-distribution of PFGE profiles, the co-producer was spread primarily with single clonal expansion of the PFGE-type A with subtypes (n=14), whereas the strains producing only DHA-1 enzyme were spread simultaneously with the PFGE-type A (n=11) and other PFGE types (n=6). Transconjugants of the co-producers were confirmed to harbor either both blaDHA-1 and blaSHV-12 or only the blaDHA-1. In conclusion, this study indicated that the persistent nosocomial spread of multidrug-resistant K. pneumoniae strains was primarily associated with expansion of a clone harboring both the blaDHA-1 and blaSHV-12 or the blaDHA-1 only, and to a lesser extent with the horizontal transfer of the resistant plasmids. Our observations have clinical implication for the control and prevention of nosocomial dissemination of multidrug-resistant K. pneumoniae strains.
The Antimicrobial Activity of Essential Oil from Dracocephalum foetidum against Pathogenic Microorganisms
Saet Byoul Lee , Kwang Hyun Cha , Su Nam Kim , Shataryn Altantsetseg , Sanduin Shatar , Oidovsambuu Sarangerel , Chu Won Nho
J. Microbiol. 2007;45(1):53-57.
DOI: https://doi.org/2491 [pii]
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AbstractAbstract
A number of essential oils from Mongolian aromatic plants are claimed to have antimicrobial activities. The essential oil of Dracocephalum foetidum, a popular essential oil used in Mongolian traditional medicine, was examined for its antimicrobial activity. Eight human pathogenic microorganisms including B. subtilis, S. aureus, M. lutens, E. hirae, S. mutans, E. coli, C. albicans, and S. cerevisiae were examined. The essential oil of Dracocephalum foetidum exhibited strong antimicrobial activity against most of the pathogenic bacteria and yeast strains that were tested; by both the agar diffusion method and the minimum inhibitory concentration (MIC) assay (MIC range was 26-2592 μg/ml). Interestingly, Dracocephalum foetidum even showed antimicrobial activity against methicilin-resistant Staphylococcus aureus (MRSA) strains. We also analyzed the chemical composition of the oil by GC-MS and identified several major components, including n-Mentha-1,8-dien-10-al, limonene, geranial, and neral.

Journal of Microbiology : Journal of Microbiology
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