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Adaptation of Pseudomonas helmanticensis to fat hydrolysates and SDS: fatty acid response and aggregate formation
Ilya N. Zubkov , Anatoly P. Nepomnyshchiy , Vadim D. Kondratyev , Pavel N. Sorokoumov , Konstantin V. Sivak , Edward S. Ramsay , Sergey M. Shishlyannikov
J. Microbiol. 2021;59(12):1104-1111.   Published online October 26, 2021
DOI: https://doi.org/10.1007/s12275-021-1214-5
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AbstractAbstract
An essential part of designing any biotechnological process is examination of the physiological state of producer cells in different phases of cultivation. The main marker of a bacterial cell’s state is its fatty acid (FA) profile, reflecting membrane lipid composition. Consideration of FA composition enables assessment of bacterial responses to cultivation conditions and helps biotechnologists understand the most significant factors impacting cellular metabolism. In this work, soil SDS-degrading Pseudomonas helmanticensis was studied at the fatty acid profile level, including analysis of rearrangement between planktonic and aggregated forms. The set of substrates included fat hydrolysates, SDS, and their mixtures with glucose. Such media are useful in bioplastic production since they can help incrementally lower overall costs. Conventional gas chromatography-mass spectrometry was used for FA analysis. Acridine orange-stained aggregates were observed by epifluorescence microscopy. The bacterium was shown to change fatty acid composition in the presence of hydrolyzed fats or SDS. These changes seem to be driven by the depletion of metabolizable substrates in the culture medium. Cell aggregation has also been found to be a defense strategy, particularly with anionic surfactant (SDS) exposure. It was shown that simple fluidity indices (such as saturated/ unsaturated FA ratios) do not always sufficiently characterize a cell's physiological state, and morphological examination is essential in cases where complex carbon sources are used.

Citations

Citations to this article as recorded by  
  • Effect of different diet composition on the fat profile of two different black soldier fly larvae populations
    M. Tognocchi, L. Abenaim, C. Adamaki-Sotiraki, G.C. Athanassiou, I.C. Rumbos, M. Mele, B. Conti, G. Conte
    animal.2024; 18(7): 101205.     CrossRef
  • Earth to Mars: A Protocol for Characterizing Permafrost in the Context of Climate Change as an Analog for Extraplanetary Exploration
    Kimberley R. Miner, Joseph Razzell Hollis, Charles E. Miller, Kyle Uckert, Thomas A. Douglas, Emily Cardarelli, Rachel Mackelprang
    Astrobiology.2023; 23(9): 1006.     CrossRef
  • Preparation of polyhydroxyalkanoates using Pseudomonas helmanticensis in non-sterile media containing glycerol and sodium dodecyl sulfate
    I. N. Zubkov, Yu. S. Bukin, P. N. Sorokoumov, S. M. Shishlyannikov
    Proceedings of Universities. Applied Chemistry and Biotechnology.2022; 12(3): 479.     CrossRef
Stenotrophomonas maltophilia outer membrane protein A induces epithelial cell apoptosis via mitochondrial pathways
Xin Wang , Yan Li , Xueping Tang , Xueyi Shang , Zunquan Zhao , Yongqiang Jiang , Yan Li
J. Microbiol. 2020;58(10):868-877.   Published online September 2, 2020
DOI: https://doi.org/10.1007/s12275-020-0235-9
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  • 9 Web of Science
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AbstractAbstract
Stenotrophomonas maltophilia (S. maltophilia) is a common opportunistic pathogen in intensive care units and causes infections most often after surgeries in immune-compromised patients such as those undergoing chemotherapy. Outer membrane protein A (OmpA) is the most abundant of the outer membrane proteins in S. maltophilia. Previous studies on OmpA usually focus on its interaction with the host cells and its role in vaccine development. However, the impact of OmpA on the virulence of S. maltophilia to host cells and the effects on apoptosis remain unclear. In this study, we exposed purified recombinant S. maltophilia OmpA (rOmpA) to HEp-2 cells and investigated the effects of OmpA on epithelial cell apoptosis. Morphologic and flow cytometric analyses revealed that HEp-2 cells stimulated with rOmpA multiple apoptosis features, including nuclear roundness and pyknosis, chromatin aggregation, and phosphatidylserine eversion. We found that rOmpA regulated the protein levels of Bax and Bcl-xL in HEp-2 cells, leading to changes in mitochondria permeability and the release of cytochrome c and apoptosis-inducing factors into the cytoplasm. These subsequently activate the caspase-9/caspase-3 pathway that promote apoptosis. We also observed that rOmpA enhanced the generation of reactive oxygen species and increased intracellular Ca2+ levels in HEp-2 cells. Collectively, our data suggested that rOmpA induced epithelial cells apoptosis via mitochondrial pathways.

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  • Functional analysis of OmpA and its contribution to pathogenesis of Edwardsiella tarda
    Quan Zhou, Yushuai Hu, Yicheng You, Yingli Gao, Xingqiang Wang, Lei Qin
    Microbial Pathogenesis.2024; 193: 106760.     CrossRef
  • Application of mPEG-CS-cRGD/ Bmi-1RNAi -PTX nanoparticles in suppression of laryngeal cancer by targeting cancer stem cells
    Xiaoyan Xu, Tianhao Zhou, Xudong Wei, Xuelian Jiang, Jiyan Cao
    Drug Delivery.2023;[Epub]     CrossRef
  • Control of host mitochondria by bacterial pathogens
    Saverio Marchi, Gianluca Morroni, Paolo Pinton, Lorenzo Galluzzi
    Trends in Microbiology.2022; 30(5): 452.     CrossRef
  • Lysophosphatidic acid protects cervical cancer HeLa cells from apoptosis induced by doxorubicin hydrochloride
    Xibo Wang, Haihua Wang, Xiaoxiao Mou, Yilin Xu, Wenbo Han, Aimin Huang, Yanwei Li, Hui Jiang, Xiaoyun Yang, Zhenbo Hu
    Oncology Letters.2022;[Epub]     CrossRef
Research Support, Non-U.S. Gov't
Enhanced Production of Carboxymethylcellulase by a Marine Bacterium, Bacillus velezensis A-68, by Using Rice Hulls in Pilot-scale Bioreactor under Optimized Conditions for Dissolved Oxygen
Wa Gao , Hye-Jin Kim , Chung-Han Chung , Jin-Woo Lee
J. Microbiol. 2014;52(9):755-761.   Published online July 30, 2014
DOI: https://doi.org/10.1007/s12275-014-4156-3
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AbstractAbstract
The optimal conditions for the production of carboxymethylcellulase (CMCase) by Bacillus velezensis A-68 at a flask scale have been previously reported. In this study, the parameters involved in dissolved oxygen in 7 and 100 L bioreactors were optimized for the pilot-scale production of CMCase. The optimal agitation speed and aeration rate for cell growth of B. velezensis A-68 were 323 rpm and 1.46 vvm in a 7 L bioreactor, whereas those for the production of CMCase were 380 rpm and 0.54 vvm, respectively. The analysis of variance (ANOVA) implied that the highly significant factor for cell growth was the aeration rate, whereas that for the production of CMCase was the agitation speed. The optimal inner pressures for cell growth and the production of CMCase by B. velezensis A-68 in a 100 L bioreactor were 0.00 and 0.04 MPa, respectively. The maximal production of CMCase in a 100 L bioreactor under optimized conditions using rice hulls was 108.1 U/ml, which was 1.8 times higher than that at a flask scale under previously optimized conditions.

Citations

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  • Utilization of shrimp heads for scaling up of production of Bacillus velezensis EB.KN15, its bioactive compounds and novel anti-fungal effect against durian pathogen fungi
    Van Anh Ngo, San-Lang Wang, Van Bon Nguyen, Tu Quy Phan, Thi Ha Trang Tran, Manh Dung Doan, Dinh Sy Nguyen, Anh Dzung Nguyen
    Research on Chemical Intermediates.2024; 50(10): 5061.     CrossRef
  • Production and stability of a multi-strain Bacillus based probiotic product for commercial use in poultry
    Uraisha Ramlucken, Santosh O. Ramchuran, Ghaneshree Moonsamy, Christine Jansen van Rensburg, Mapitsi S. Thantsha, Rajesh Lalloo
    Biotechnology Reports.2021; 29: e00575.     CrossRef
  • Killing effect of deinoxanthins on cyanobloom-forming Microcystis aeruginosa: Eco-friendly production and specific activity of deinoxanthins
    Wonjae Kim, Minkyung Kim, Minyoung Hong, Woojun Park
    Environmental Research.2021; 200: 111455.     CrossRef
  • Biochemical and Molecular Characterization of Five Bacillus Isolates Displaying Remarkable Carboxymethyl Cellulase Activities
    Esraa Abd Elhameed, Alaa R. M. Sayed, Tharwat E. E. Radwan, Gamal Hassan
    Current Microbiology.2020; 77(10): 3076.     CrossRef
  • Enhanced Production of Carboxymethylcellulase by Recombinant Escherichia coli Strain from Rice Bran with Shifts in Optimal Conditions of Aeration Rate and Agitation Speed on a Pilot-Scale
    Chung-Il Park, Jae-Hong Lee, Jianhong Li, Jin-Woo Lee
    Applied Sciences.2019; 9(19): 4083.     CrossRef
  • Characteristics and Application of a Novel Species of Bacillus: Bacillus velezensis
    Miao Ye, Xiangfang Tang, Ru Yang, Hongfu Zhang, Fangshu Li, Fangzheng Tao, Fei Li, Zaigui Wang
    ACS Chemical Biology.2018; 13(3): 500.     CrossRef
  • Comparison of optimal conditions for mass production of carboxymethylcellulase by Escherichia coli JM109/A-68 with other recombinants in pilot-scale bioreactor
    Myung-Hwan Kim, Wa Gao, Chung-Han Chung, Jin-Woo Lee
    Biotechnology and Bioprocess Engineering.2017; 22(2): 142.     CrossRef
  • Construction of a recombinant Escherichia coli JM109/A-68 for production of carboxymethylcellulase and comparison of its production with its wild type, Bacillus velezensis A-68 in a pilot-scale bioreactor
    Myung-Hwan Kim, Duk-Un Kang, Jin-Woo Lee
    Biotechnology and Bioprocess Engineering.2016; 21(5): 601.     CrossRef

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