Journal of Microbiology

Journal Articles

Regulatory role of cysteines in (2R, 3R)-butanediol dehydrogenase BdhA of Bacillus velezensis strain GH1-13: Yunhee Choi , Yong-Hak Kim; J. Microbiol. 2022;60(4):411-418. Published online March 14, 2022; DOI: https://doi.org/10.1007/s12275-022-2018-y

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Bacillus velezensis strain GH1-13 contains a (2R,3R)-butanediol dehydrogenase (R-BDH) BdhA which converts acetoin to R-BD reversibly, however, little is known about its regulatory cysteine and biological significance. We performed sitedirected mutation of three cysteines in BdhA. The C37S mutant had no enzyme activity and the C34S and C177S mutants differed from each other and wild type (WT). After zinc affinity chromatography, 1 mM ZnCl2 treatment resulted in a 3-fold enhancement of the WT activity, but reduced activity of the C34S mutant by more than 2 folds compared to the untreated ones. However, ZnCl2 treatment did not affect the activity of the C177S mutant. Most of the double and triple mutant proteins (C34S/C37S, C34S/C177S, C37S/C177S, and C34S/C37S/C177S) were aggregated in zinc resins, likely due to the decreased protein stability. All of the purified WT and single mutant proteins increased multiple intermolecular disulfide bonds in the presence of H2O2 as the buffer pH decreased from 7.5 to 5.5, whereas an intramolecular disulfide bond of cysteine 177 and another cysteine in the CGIC motif region was likely formed at pH higher than pKa of 7.5. When pH varied, WT and its C34S or C177S mutants reduced acetoin to R-BD at the optimum pH 5.5 and oxidized R-BD to acetoin at the optimum pH 10. This study demonstrated that cysteine residues in BdhA play a regulatory role for the production of acetoin and R-BD depending on pH as well as metal binding and oxidative stress.

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Significantly enhanced specific activity of Bacillus subtilis (2,3)-butanediol dehydrogenase through computer-aided refinement of its substrate-binding pocket
Bochun Hu, Xiaoqi Xi, Fugang Xiao, Xiaomeng Bai, Yuanyuan Gong, Yifan Li, Xueqin Qiao, Cunduo Tang, Jihong Huang
International Journal of Biological Macromolecules.2024; 281: 136443. CrossRef
Structural and enzymatic characterization of Bacillus subtilis R,R-2,3-butanediol dehydrogenase
Xiaofei Wang, Lingyun Jia, Fangling Ji
Biochimica et Biophysica Acta (BBA) - General Subjects.2023; 1867(4): 130326. CrossRef
Engineering a BsBDHA substrate-binding pocket entrance for the improvement in catalytic performance toward (R)-phenyl-1,2-ethanediol based on the computer-aided design
Bo-Chun Hu, Meng-Ran Li, Ying-Ying Li, Xin-Shuang Yuan, Yu-Ye Hu, Fu-Gang Xiao
Biochemical Engineering Journal.2023; 194: 108907. CrossRef

Oxygen-mediated growth enhancement of an obligate anaerobic archaeon Thermococcus onnurineus NA1: Seong Hyuk Lee , Hwan Youn , Sung Gyun Kang , Hyun Sook Lee; J. Microbiol. 2019;57(2):138-142. Published online January 31, 2019; DOI: https://doi.org/10.1007/s12275-019-8592-y

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Abstract

Thermococcus onnurineus NA1, an obligate anaerobic hyperthermophilic archaeon, showed variable oxygen (O2) sensitivity depending on the types of substrate employed as an energy source. Unexpectedly, the culture with yeast extract as a sole energy source showed enhanced growth by 2-fold in the presence of O2. Genome-wide transcriptome analysis revealed the upregulation of several antioxidant-related genes encoding thioredoxin peroxidase (TON_0862), rubrerythrin (TON_0864), rubrerythrin-related protein (TON_0873), NAD(P)H rubredoxin oxidoreductase (TON_0865), or thioredoxin reductase (TON_1603), which can couple the detoxification of reactive oxygen species with the regeneration of NAD(P)+ from NAD(P)H. We present a plausible mechanism by which O2 serves to maintain the intracellular redox balance. This study demonstrates an unusual strategy of an obligate anaerobe underlying O2-mediated growth enhancement despite not having heme-based or cytochrome-type proteins.

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How low can they go? Aerobic respiration by microorganisms under apparent anoxia
Jasmine S Berg, Soeren Ahmerkamp, Petra Pjevac, Bela Hausmann, Jana Milucka, Marcel M M Kuypers
FEMS Microbiology Reviews.2022;[Epub] CrossRef
Reductive evolution and unique predatory mode in the CPR bacterium Vampirococcus lugosii
David Moreira, Yvan Zivanovic, Ana I. López-Archilla, Miguel Iniesto, Purificación López-García
Nature Communications.2021;[Epub] CrossRef

Increased susceptibility against Cryptococcus neoformans of lupus mouse models (pristane-induction and FcGRIIb deficiency) is associated with activated macrophage, regardless of genetic background: Saowapha Surawut , Jiradej Makjaroen , Arthid Thim-uam , Jutamas Wongphoom , Tanapat Palaga , Prapaporn Pisitkun , Ariya Chindamporn , Asada Leelahavanichkul; J. Microbiol. 2019;57(1):45-53. Published online November 19, 2018; DOI: https://doi.org/10.1007/s12275-019-8311-8

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Abstract

The severity of cryptococcosis in lupus from varying geneticbackgrounds might be different due to the heterogeneity of lupus-pathogenesis. This study explored cryptococcosis in lupus mouse models of pristane-induction (normal geneticbackground) and FcGRIIb deficiency (genetic defect). Because the severity of lupus nephritis, as determined by proteinuria and serum creatinine, between pristane and FcGRIIb-/- mice were similar at 6-month-old, Cryptococcus neoformans was intravenously administered in 6-month-old mice and were age-matched with wild-type. Indeed, the cryptococcosis disease severity, as evaluated by mortality rate, internal-organ fungal burdens and serum cytokines, between pristane and FcGRIIb-/- mice was not different. However, the severity of cryptococcosis in wild-type was less severe than the lupus mice. On the other hand, phagocytosis activity of peritoneal macrophages from lupus mice (pristane and FcGRIIb-/-) was more predominant than the wild-type without the difference in macrophage killing-activity among these groups. In addition, the number of active T helper cells (Th-cell) in the spleen, including Th-cells with intracellular IFN-γ, from lupus mice (pristane and FcGRIIb-/-) was higher than wildtype. Moreover, these active Th-cells were even higher after 2 weeks of cryptococcal infection. These data support enhanced macrophage activation through prominent Th-cells in both lupus models. In conclusion, an increased susceptibility of cryptococcosis in both lupus models was independent to genetic background. This might due to Th-cell enhanced macrophage phagocytosis with the interference of macrophage killing activity from Cryptococcal immune-evasion properties.

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Comparative time-series analyses of gut microbiome profiles in genetically and chemically induced lupus-prone mice and the impacts of fecal transplantation
Piraya Chatthanathon, Asada Leelahavanichkul, Thanya Cheibchalard, Alisa Wilantho, Nattiya Hirankarn, Naraporn Somboonna
Scientific Reports.2024;[Epub] CrossRef
Fungal microbiome in gut of systemic lupus erythematosus (SLE)-prone mice (pristane and FCGRIIb deficiency), a possible impact of fungi in lupus
Thanya Cheibchalard, Asada Leelahavanichkul, Piraya Chatthanathon, Piriya Klankeo, Nattiya Hirankarn, Naraporn Somboonna, Veena Taneja
PLOS ONE.2024; 19(12): e0314662. CrossRef
Obesity Exacerbates Lupus Activity in Fc Gamma Receptor IIb Deficient Lupus Mice Partly through Saturated Fatty Acid-Induced Gut Barrier Defect and Systemic Inflammation
Kanyarat Udompornpitak, Awirut Charoensappakit, Kritsanawan Sae-Khow, Thansita Bhunyakarnjanarat, Cong Phi Dang, Wilasinee Saisorn, Peerapat Visitchanakun, Pornpimol Phuengmaung, Tanapat Palaga, Patcharee Ritprajak, Somkanya Tungsanga, Asada Leelahavanich
Journal of Innate Immunity.2023; 15(1): 240. CrossRef
Myracrodruon urundeuva lectins present anticancer and anticryptococcal activities with low cytotoxic or genotoxic effects
Larissa Cardoso Corrêa de Araújo Videres, Matheus Cavalcanti de Barros, Thamara Figueiredo Procópio, Gustavo Ramos Salles Ferreira, Pollyanna Michelle da Silva, André Mariano Batista, Maria Madalena Pessoa Guerra, Marilene Henning Vainstein, Jaciana dos S
South African Journal of Botany.2023; 157: 614. CrossRef
Enhanced lupus progression in alcohol‐administered Fc gamma receptor‐IIb–deficiency lupus mice, partly through leaky gut‐induced inflammation
Wiwat Chancharoenthana, Supitcha Kamolratanakul, Phatcharapon Yiengwattananon, Pornpimol Phuengmaung, Kanyarat Udompornpitak, Wilasinee Saisorn, Pratsanee Hiengrach, Peerapat Visitchanakun, Marcus J Schultz, Asada Leelahavanichkul
Immunology & Cell Biology.2023; 101(8): 746. CrossRef
A Comparison Between 1 Day versus 7 Days of Sepsis in Mice with the Experiments on LPS-Activated Macrophages Support the Use of Intravenous Immunoglobulin for Sepsis Attenuation
Jiradej Makjaroen, Arthid Thim-Uam, Cong Phi Dang, Trairak Pisitkun, Poorichaya Somparn, Asada Leelahavanichkul
Journal of Inflammation Research.2021; Volume 14: 7243. CrossRef
Quantum dots conjugated to lectins from Schinus terebinthifolia leaves (SteLL) and Punica granatum sarcotesta (PgTeL) as potential fluorescent nanotools for investigating Cryptococcus neoformans
Abdênego Rodrigues da Silva, Weslley Felix de Oliveira, Pollyanna Michelle da Silva, Leydianne Leite de Siqueira Patriota, Robson Raion de Vasconcelos Alves, Ana Patrícia Silva de Oliveira, Maria Tereza dos Santos Correia, Patrícia Maria Guedes Paiva, Mar
International Journal of Biological Macromolecules.2021; 192: 232. CrossRef
Lipopolysaccharide-Enhanced Responses against Aryl Hydrocarbon Receptor in FcgRIIb-Deficient Macrophages, a Profound Impact of an Environmental Toxin on a Lupus-Like Mouse Model
Kanyarat Udompornpitak, Thansita Bhunyakarnjanarat, Awirut Charoensappakit, Cong Phi Dang, Wilasinee Saisorn, Asada Leelahavanichkul
International Journal of Molecular Sciences.2021; 22(8): 4199. CrossRef
Prominent Indomethacin-Induced Enteropathy in Fcgriib Defi-cient lupus Mice: An Impact of Macrophage Responses and Immune Deposition in Gut
Thansita Bhunyakarnjanarat, Kanyarat Udompornpitak, Wilasinee Saisorn, Bhumdhanin Chantraprapawat, Peerapat Visitchanakun, Cong Phi Dang, Jiraphorn Issara-Amphorn, Asada Leelahavanichkul
International Journal of Molecular Sciences.2021; 22(3): 1377. CrossRef
A Synergy Between Endotoxin and (1→3)-Beta-D-Glucan Enhanced Neutrophil Extracellular Traps in Candida Administered Dextran Sulfate Solution Induced Colitis in FcGRIIB-/- Lupus Mice, an Impact of Intestinal Fungi in Lupus
Supichcha Saithong, Wilasinee Saisorn, Peerapat Visitchanakun, Kritsanawan Sae-khow, Direkrit Chiewchengchol, Asada Leelahavanichkul
Journal of Inflammation Research.2021; Volume 14: 2333. CrossRef
A1 and A2A adenosine receptors play a protective role to reduce prevalence of autoimmunity following tissue damage
Reut Riff, Oshri Naamani, Julia Mazar, Yosef S Haviv, Cidio Chaimovitz, Amos Douvdevani
Clinical & Experimental Immunology.2021; 205(3): 278. CrossRef
Acute Kidney Injury Induced Lupus Exacerbation Through the Enhanced Neutrophil Extracellular Traps (and Apoptosis) in Fcgr2b Deficient Lupus Mice With Renal Ischemia Reperfusion Injury
Wilasinee Saisorn, Supichcha Saithong, Pornpimol Phuengmaung, Kanyarat Udompornpitak, Thansita Bhunyakarnjanarat, Peerapat Visitchanakun, Awirut Chareonsappakit, Prapaporn Pisitkun, Direkrit Chiewchengchol, Asada Leelahavanichkul
Frontiers in Immunology.2021;[Epub] CrossRef
Syk inhibitor attenuates inflammation in lupus mice from FcgRIIb deficiency but not in pristane induction: the influence of lupus pathogenesis on the therapeutic effect
Jiraphorn Issara-Amphorn, Naraporn Somboonna, Prapaporn Pisitkun, Nattiya Hirankarn, Asada Leelahavanichkul
Lupus.2020; 29(10): 1248. CrossRef

The in vitro and in vivo efficacy of fluconazole in combination with farnesol against Candida albicans isolates using a murine vulvovaginitis model: Aliz Bozó , Marianna Domán , László Majoros , Gábor Kardos , István Varga , Renátó Kovács; J. Microbiol. 2016;54(11):753-760. Published online October 29, 2016; DOI: https://doi.org/10.1007/s12275-016-6298-y

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Abstract

Farnesol is a quorum-sensing molecule that inhibits biofilm formation in Candida albicans. Previous in vitro data suggest that, in combination with certain antifungals, farnesol may have an adjuvant anti-biofilm agent. However, the in vivo efficacy of farnesol is very questionable. Therefore, the in vitro and in vivo activity of fluconazole combined with farnesol was evaluated against C. albicans biofilms using fractional inhibitory concentration index (FICI) determination, time-kill experiments and a murine vulvovaginitis model. The median biofilm MICs of fluconazole-sensitive C. albicans isolates ranged between 4 -> 512 mg/L and 150–300 μM for fluconazole and farnesol, respectively. These values were 512 -> 512 mg/L and > 300 μM for fluconazole-resistant clinical isolates. Farnesol decreased the median MICs of fluconazole by 2-64-fold for biofilms. Based on FICI, synergistic interaction was observed only in the case of the sessile SC5314 reference strain (FICIs: 0.16–0.27). In time-kill studies, only the 512 mg/L fluconazole and 512 mg/L fluconazole + 75 μM farnesol reduced biofilm mass significantly at each time point in the case of all isolates. The combination reduced the metabolic activity of biofilms for all isolates in a concentration- and time-dependent manner. Our findings revealed that farnesol alone was not protective in a murine vulvovaginitis model. Farnesol was not beneficial in combination with fluconazole for fluconazole-susceptible isolates, but partially increased fluconazole activity against one fluconazole- resistant isolate, but not the other one.

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Ágnes Jakab, Kinga Csillag, Károly Antal, Imre Boczonádi, Renátó Kovács, István Pócsi, Tamás Emri
Fungal Biology.2024; 128(2): 1664. CrossRef
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María del Rosario Agustín, María Clara Tarifa, María Soledad Vela-Gurovic, Lorena Inés Brugnoni
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Yingzhe Wang, Wei Long, Feiyin Zhang, Meimei Zhang, Kang Zeng, Xiaoliang Zhu, Gustavo H. Goldman
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Research Support, Non-U.S. Gov'ts

Dimethyl sulfoxide reduction by a hyperhermophilic archaeon Thermococcus onnurineus NA1 via a cysteine-cystine redox shuttle: Ae Ran Choi , Min-Sik Kim , Sung Gyun Kang , Hyun Sook Lee; J. Microbiol. 2016;54(1):31-38. Published online January 5, 2016; DOI: https://doi.org/10.1007/s12275-016-5574-1

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Abstract

A variety of microbes grow by respiration with dimethyl sulfoxide (DMSO) as an electron acceptor, and several distinct DMSO respiratory systems, consisting of electron carriers and a terminal DMSO reductase, have been characterized. The heterotrophic growth of a hyperthermophilic archaeon Thermococcus onnurineus NA1 was enhanced by the addition of DMSO, but the archaeon was not capable of reducing DMSO to DMS directly using a DMSO reductase. Instead, the archaeon reduced DMSO via a cysteine-cystine redox shuttle through a mechanism whereby cystine is microbially reduced to cysteine, which is then reoxidized by DMSO reduction. A thioredoxin reductase-protein disulfide oxidoreductase redox couple was identified to have intracellular cystine-reducing activity, permitting recycle of cysteine. This study presents the first example of DMSO reduction via an electron shuttle. Several Thermococcales species also exhibited enhanced growth coupled with DMSO reduction, probably by disposing of excess reducing power rather than conserving energy.

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Heavy Metal-Resistant Biohybrid System Boosts Dissimilatory Nitrate Reduction to Ammonium for Agronomic Sustainability
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Phenotypic and genomic characterization of Bathyarchaeum tardum gen. nov., sp. nov., a cultivated representative of the archaeal class Bathyarchaeia
Maria A. Khomyakova, Alexander Y. Merkel, Dana D. Mamiy, Alexandra A. Klyukina, Alexander I. Slobodkin
Frontiers in Microbiology.2023;[Epub] CrossRef
Direct Electron Transfer between the frhAGB -Encoded Hydrogenase and Thioredoxin Reductase in the Nonmethanogenic Archaeon Thermococcus onnurineus NA1
Hae-Chang Jung, Jae Kyu Lim, Tae-Jun Yang, Sung Gyun Kang, Hyun Sook Lee, Haruyuki Atomi
Applied and Environmental Microbiology.2020;[Epub] CrossRef
A peroxiredoxin of Thermus thermophilus HB27: Biochemical characterization of a new player in the antioxidant defence
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A Reexamination of Thioredoxin Reductase from Thermoplasma acidophilum, a Thermoacidophilic Euryarchaeon, Identifies It as an NADH-Dependent Enzyme
Dwi Susanti, Usha Loganathan, Austin Compton, Biswarup Mukhopadhyay
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Redox regulation of SurR by protein disulfide oxidoreductase in Thermococcus onnurineus NA1
Jae Kyu Lim, Hae-Chang Jung, Sung Gyun Kang, Hyun Sook Lee
Extremophiles.2017; 21(3): 491. CrossRef
Exploring membrane respiratory chains
Bruno C. Marreiros, Filipa Calisto, Paulo J. Castro, Afonso M. Duarte, Filipa V. Sena, Andreia F. Silva, Filipe M. Sousa, Miguel Teixeira, Patrícia N. Refojo, Manuela M. Pereira
Biochimica et Biophysica Acta (BBA) - Bioenergetics.2016; 1857(8): 1039. CrossRef

Structural basis for the ATP-independent proteolytic activity of LonB proteases and reclassification of their AAA+ modules: Young Jun An , Jung-Hyun Na , Myung-Il Kim , Sun-Shin Cha; J. Microbiol. 2015;53(10):711-717. Published online October 2, 2015; DOI: https://doi.org/10.1007/s12275-015-5417-5

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Abstract

Lon proteases degrade defective or denature proteins as well as some folded proteins for the control of cellular protein quality. There are two types of Lon proteases, LonA and LonB. Each consists of two functional components: a protease component and an ATPase associated with various cellular activities (AAA+ module). Here, we report the 2.03 Å-resolution crystal structure of the isolated AAA+ module (iAAA+ module) of LonB from Thermococcus onnurineus NA1 (TonLonB). The iAAA+ module, having no bound nucleotide, adopts a conformation virtually identical to the ADP-bound conformation of AAA+ modules in the hexameric structure of TonLonB; this provides insights into the ATP-independent proteolytic activity observed in a LonB protease. Structural comparison of AAA+ modules between LonA and LonB revealed that the AAA+ modules of Lon proteases are separated into two distinct clades depending on their structural features. The AAA+ module of LonB belongs to the ‘H2 & Ins1 insert clade (HINS clade)’ defined for the first time in this study, while the AAA+ module of LonA is a member of the HCLR clade.

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Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases
Alla Gustchina, Mi Li, Anna G. Andrianova, Arsen M. Kudzhaev, George T. Lountos, Bartosz Sekula, Scott Cherry, Joseph E. Tropea, Ivan V. Smirnov, Alexander Wlodawer, Tatyana V. Rotanova
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Analysis of cepA Encoding an Efflux Pump-like Protein in Corynebacterium glutamicum: Soo-Yeon Sim , Eun-Ji Hong , Younhee Kim , Heung-Shick Lee; J. Microbiol. 2014;52(4):278-283. Published online February 17, 2014; DOI: https://doi.org/10.1007/s12275-014-3461-1

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Abstract

A gene encoding a homolog of purine efflux proteins of Escherichia coli and Bacillus subtilis was identified in the genome of Corynebacterium glutamicum and designated as cepA. The gene encoded a putative protein product, containing 12 transmembrane helixes, which is a typical feature of integral membrane transport proteins. To elucidate the function of the gene, we constructed a cepA deletion mutant (ΔcepA) and a cepA-overexpressing strain and analyzed their physiological characteristics. The cepA gene could be deleted with no critical effect on cell growth. However, the cell yield of a ΔcepA strain was decreased by 10% as compared to that of a strain carrying a cepA-overexpression plasmid (P180-cepA). Further analysis identified increased resistance of the P180-cepA strain to the purine analogues 6-mercaptopurine and 6-mercaptoguanine, but not to 2-aminopurine and purine nucleoside analogues. Moreover, this strain showed increased resistance to the antibiotics nalidixic acid and ampicillin. Collectively, these data suggest that cepA is a novel multidrug resistance gene and probably functions in the efflux of toxic substances from the inside of cells to the environment, thus allowing cells to reach a higher cell yield.

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Tobias Michael Rosch, Julia Tenhaef, Tim Stoltmann, Till Redeker, Dominic Kösters, Niels Hollmann, Karin Krumbach, Wolfgang Wiechert, Michael Bott, Susana Matamouros, Jan Marienhagen, Stephan Noack
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Characterization of Thermostable Deblocking Aminopeptidases of Archaeon Thermococcus onnurineus NA1 by Proteomic and Biochemical Approaches: Yeol Gyun Lee , Sun-Hee Leem , Young-Ho Chung , Seung Il Kim; J. Microbiol. 2012;50(5):792-797. Published online November 4, 2012; DOI: https://doi.org/10.1007/s12275-012-2461-2

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Abstract: Thermococcus onnurineus NA1 is a hyperthermophilic archaeon that grows optimally at >80°C. The deblocking aminopeptidase (DAP) (TNA1-DAP1) encoded in Ton_1032 of T. onnurineus NA1 is considered a major DAP. However, four genes encoding putative DAP have been identified from a genomic analysis of T. onnurineus NA1. A proteomic analysis revealed that all four DAPs were differentially induced in YPS culture medium and, particularly, two DAPs (TNA1-DAP1 and TNA1-DAP2) were dominantly expressed in T. onnurineus NA1. The biochemical properties and enzyme activity of DAPs induced in an E. coli expression system suggested that the two major DAPs play complementary roles in T. onnurineus NA1.

Characterization of Hyperthermostable Fructose-1,6-Bisphosphatase from Thermococcus onnurineus NA1: Yeol Gyun Lee , Sung Gyun Kang , Jung-Hyun Lee , Seung Il Kim , Young-Ho Chung; J. Microbiol. 2010;48(6):803-807. Published online January 9, 2011; DOI: https://doi.org/10.1007/s12275-010-0377-2

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Abstract: To understand the physiological functions of thermostable fructose-1,6-bisphosphatase (TNA1-Fbp) from Thermococcus onnurineus NA1, its recombinant enzyme was overexpressed in Escherichia coli, purified, and the enzymatic properties were characterized. The enzyme showed maximal activity for fructose-1,6- bisphosphate at 95°C and pH 8.0 with a half-life (t1/2) of about 8 h. TNA1-Fbp had broad substrate specificities for fructose-1,6-bisphosphate and its analogues including fructose-1-phosphate, glucose-1-phosphate, and phosphoenolpyruvate. In addition, its enzyme activity was increased five-fold by addition of 1 mM Mg2+, while Li+ did not enhance enzymatic activity. TNA1-Fbp activity was inhibited by ATP, ADP, and phosphoenolpyruvate, but AMP up to 100 mM did not have any effect. TNA1-Fbp is currently defined as a class V fructose-1,6-bisphosphatase (FBPase) because it is very similar to FBPase of Thermococcus kodakaraensis KOD1 based on sequence homology. However, this enzyme shows a different range of substrate specificities. These results suggest that TNA1-Fbp can establish new criterion for class V FBPases.

Newly Identified CpG ODNs, M5-30 and M6-395, Stimulate MouseNewly Identified CpG ODNs, M5-30 and M6-395, Stimulate Mouse Immune Cells to Secrete TNF-α and Enhance Th1-Mediated Immunity: Sun-Shim Choi , Eunkyung Chung , Yu-Jin Jung; J. Microbiol. 2010;48(4):512-517. Published online August 20, 2010; DOI: https://doi.org/10.1007/s12275-010-0053-6

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Abstract: Bacterial CpG motifs are known to induce both innate and adaptive immunity in infected hosts via toll-like receptor 9 (TLR9). Because small oligonucleotides (ODNs) mimicking bacterial CpG motifs are easily synthesized, they have found use as immunomodulatory agents in a number of disease models. We have developed a novel bioinformatics approach to identify effective CpG ODN sequences and evaluate their function as TLR9 ligands in a murine system. Among the CpG ODNs we identified, M5-30 and M6-395 showed significant ability to stimulate TNF-α and IFN-γ production in a mouse macrophage cell line and mouse splenocytes, respectively. We also found that these CpG ODNs activated cells through the canonical NF-κB signaling pathway. Moreover, both CpG ODNs were able to induce Th1-mediated immunity in Mycobacterium tuberculosis (Mtb)-infected mice. Our results demonstrate that M5-30 and M6-395 function as TLR9-specific ligands, making them useful in the study of TLR9 functionality and signaling in mice.

In Vivo Studies with a Candida tropicalis Isolate Exhibiting Paradoxical Growth In Vitro in the Presence of High Concentration of Caspofungin: Sedigh Bayegan , Laszlo Majoros , Gabor Kardos , Adam Kemény-Beke , Cecilia Miszti , Renato Kovacs , Rudolf Gesztelyi; J. Microbiol. 2010;48(2):170-173. Published online May 1, 2010; DOI: https://doi.org/10.1007/s12275-010-9221-y

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Abstract: We investigated the activity of caspofungin against a Candida tropicalis clinical isolate showing paradoxical growth in vitro. BALB/c mice immunosuppressed by cyclophosphamide were infected intraperitoneally using 107 CFU/mouse. Caspofungin was administered intraperitoneally once daily for 5 days or as a single dose using the following doses: 0.12, 0.25, 1, 2, 3, 5, and 15 mg/kg. The single dose of caspofungin was effective only at 5 and 15 mg/kg concentrations (100% survival). Five-day caspofungin treatment led to 100% survival at doses of 1 mg/kg or higher. Caspofungin treatment significantly decreased the number of viable yeasts in the peritoneal lavage samples as well as in the infected abscesses at doses 1, 3, 5, and 15 mg/kg caspofungin as compared to the untreated control (P<0.001 in all cases), and even to the group treated with 0.12 mg/kg caspofungin (P<0.05 in all cases). At 2 mg/kg caspofungin dose, sterilization of the internal organs was reproducibly incomplete, suggesting that the role of paradoxical growth in the late clinical failure cannot be excluded.

Comparative Analysis of Immune Responses to Mycobacterium abscessus Infection and Its Antigens in Two Murine Models: Bo-Young Jeon , Jeongyeon Kwak , Seung-Sub Lee , SangNae Cho , Chul Jae Won , Jin Man Kim , Sung Jae Shin; J. Microbiol. 2009;47(5):633-640. Published online October 24, 2009; DOI: https://doi.org/10.1007/s12275-009-0139-1

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Abstract: Mycobacterium abscessus has been identified as an emerging pulmonary pathogen in humans. Because little is known regarding immune responses elicited by M. abscessus or its antigens, immunological responses were studied in two murine models subjected to intravenous (high-dose or systemic infection) or pulmonary (low-dose or local infection) inoculation with M. abscessus ATCC 19977. An overall comparison between the two models showed similar patterns of bacterial survival and host immune responses. The colonization of M. abscessus was the highest at 5 days post-infection (dpi) and its elimination was positively correlated with cell-mediated immunity in both challenges. However, an inverse relationship was observed between progressive inflammation and mycobacterial colonization levels in mice infected with a high dose at 14 dpi. Regarding antigens, culture filtrate (CF) of M. abscessus strongly induced IFN-γ secretion, whereas cellular extract (CE) antigen elicited strong antibody responses. The antibody response to M. abscessus antigens in mice subjected to low-dose infection increased when the cellular immune response decreased over 14 dpi. However, the antibody response for the high-dose infection increased promptly after the infection. In comparison of cytokine expression in lung homogenates after M. abscessus infection, Th1 and Th2 cytokines increased simultaneously in the high-dose infection, whereas only cell-mediated immunity developed in the low-dose pulmonary infection. These findings not only enhance our understanding of the immune response to M. abscessus infection according to systemic or pulmonary infection, but may also aid in immunological diagnosis and vaccine development.

Purification and characterization of purine nucleoside phosphorylase (PNP) in micrococcus luteus: Choi , Hye Seon; J. Microbiol. 1996;34(1):82-89.

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Abstract: Purine nucleoside phosphorylase (PNP) was purified in Micrococcus luteus (M. luteus) using streptomycin sulfate and amomonium sulfate fractionation, three times by a Sephadex G-100 gel filtration and a DEAE-Sephadex A-50 ion exchange chromatography. The enzyme was purified 72 folds with a 11% recovery and showed a single band in a nondenaturing gel electrophoresis. The M. W. of PNP turned out to be 1.35 × 10^5 dalton in G-150 gel filtration chromatography. The stability of the enzyme was increased by treatment with both substrates, MgCI₂or CaCI₂, but not significantly kcal/mol. M. luteus PNP catalyzed the phosphorolysis of inosine, deoxyinosine, guanosine and deoxyguanosine with the Km value of 1.5 × 10^-3 M, 3.0 × 10^-3 M, 5.0 × 10^-4 M, respectively. The enzyme was reacted with adenosine, 1-methylnosine and 1-methylguanosine as substrates, which were shown to be poor substrates for mammalian enzyme.

Inhibition of purine nucleoside phosphorylase (PNP) in micrococcus luteus phenylglyoxal: Choi , Hye Seon; J. Microbiol. 1996;34(3):270-273.

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Abstract: Micrococcus luteus purine nucleoside phosphorylase (PNP) has been purified and characterized. The physical and kinetic properties have been described previously. Chemical modification of the enzyme was attempted to gain insight on the active site. The enzyme was inactivated in a time-dependent manner by the arginine- specific modifying reagent phenylglyoxal. There was a linear relationship between the observed rate of inactivation and the phenylglyoxal concentration. At 30℃ the bimolecular rate constant for the modification was 0.015 min^-1 mM^-1 in 50 mM NaHCO₃buffer, pH 7.5. The plot of logk versus log phenylglyoxal concentration was a strainght line with a slope enzyme. Preincuation with saturated solutions of substrates protected the enzyme from inhibition of phenylglyoxal, indicating that reactions with phenylglyoxal were directed at arginyl residues essential for the catalytic functioning of the enzyme.

Catalytic mechanism and inhibition studies of purine nucleoside phosphorylase (PNP) in micrococcus luteus: Choi , Hye Seon; J. Microbiol. 1997;35(1):15-20.

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Abstract: Kinetic studies were done to elucidate the reaction mechanism of purine nucleoside phosphorylase (PNP) in Micrococcus Luteus. PNP catalyzes the reversible phosphorolysis of ribonucleosides to their respective base. The effect of alternative competing substrates suggested that a single enzyme was involved in binding to the active site for all purine nucleosides, inosine, deoxyiosine, guanosine, deoxyguanosine, adenosine and deoxyadenosine. Affinity studies showed that pentose moiety reduced the binding capacity and methylation of ring N-1 of inosine and guanosine had little effect on binding to bacterial enzyme, whereas these compounds did not bind to the mammalian enzymes. The initial velocity and product inhibition studies demonstrated that the predominant mechanism of reaction was an ordered bi, bi reaction. The nucleoside bound to the enzyme first, followed by phosphate. Ribose 1-phosphate was the first product to leave, followed by base.

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