• Mycobiology
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• v.50 no.1
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• pp.96-98
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• 2022

The Aspergilli of the section Nidulantes series Versicolores are among the most recurrent molds in indoor environments. These species cause damage to the quality of air. Indeed, they are responsible for allergies, aggravation of asthma and can even cause infections in immunocompromised patients. Molds belonging to the Versicolores series also produce sterigmatocystin, a mycotoxin classified as potential human carcinogen by the International Agency for Research on Cancer (group 2B). Here, we provide for the first time the genome of three species of the series Versicolores: Aspergillus creber, Aspergillus jensenii and Aspergillus protuberus which are the most abundant species of this series in bioaerosols. The genomes of these three species could be assembled with a percentage of completeness of 97.02%, 96.21% and 95.35% for Aspergillus creber, A. jensenii and A. protuberus respectively. These data will allow to study the genes and gene clusters responsible for the expression of virulence factors, the biosynthesis of mycotoxins and the proliferation of these ubiquitous and recurrent molds.

• International Journal of Stem Cells
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• v.15 no.1
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• pp.70-84
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• 2022

The advent of human intestinal organoid systems has revolutionized the way we understand the interactions between the human gut and microorganisms given the host tropism of human microorganisms. The gut microorganisms have regionality (i.e., small versus large intestine) and the expression of various virulence factors in pathogens is influenced by the gut milieu. However, the culture conditions, optimized for human intestinal organoids, often do not fully support the proliferation and functionality of gut microorganisms. In addition, the regional identity of human intestinal organoids has not been considered to study specific microorganisms with regional preference. In this review we provide an overview of current efforts to understand the role of microorganisms in human intestinal organoids. Specifically, we will emphasize the importance of matching the regional preference of microorganisms in the gut and tailoring the appropriate luminal environmental conditions (i.e., oxygen, pH, and biochemical levels) for modeling real interactions between the gut and the microorganisms with human intestinal organoids.

• The Plant Pathology Journal
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• v.36 no.4
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• pp.323-334
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• 2020

Lysin motif (LysM) proteins are reported to be necessary for the virulence and immune response suppression in many herbaceous plant pathogens, while far less is documented in woody plant pathogens. In this study, we preliminarily characterized the molecular function of a LysM protein LtLysM1 in woody plant pathogen Lasiodiplodia theobromae. Transcriptional profiles revealed that LtLysM1 is highly expressed at infectious stages, especially at 36 and 48 hours post inoculation. Amino acid sequence analyses revealed that LtLysM1 was a putative glycoprotein with 10 predicted N-glycosylation sites and one LysM domain. Pathogenicity tests showed that overexpressed transformants of LtLysM1 displayed increased virulence on grapevine shoots in comparison with that of wild type CSS-01s, and RNAi transformants of LtLysM1 exhibited significantly decreased lesion length when compared with that of wild type CSS-01s. Moreover, LtLysM1 was confirmed to be a secreted protein by a yeast signal peptide trap assay. Transient expression in Nicotiana benthamiana together with protein immunoblotting confirmed that LtLysM1 was an N-glycosylated protein. In contrast to previously reported LysM protein Slp1 and OsCEBiP, LtLysM1 molecule did not interact with itself based on yeast two hybrid and co-immunoprecipitation assays. These results indicate that LtLysM1 is a secreted protein and functions as a critical virulence factor during the disease symptom development in woody plants.

• Journal of Microbiology and Biotechnology
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• v.12 no.4
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• pp.674-678
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• 2002

Yersinia enterocolitica causes various diseases in humans, including enteritis. The onset of such diseases is closely related with the expression of important virulence factors, particularly outer membrane proteins (OMPs). The expression of OMPs depends on several factors, including temperature, and origin, biotype and serotype of the bacteria. Recently, concerns over food safety have increased along with the demand for the development of sensitive, rapid, and pathogen-specific detection methods. To develop a suitable detection method for Y. enterocolitica isolated from Korean moutainspring water and pig feces, the OMP expression patterns were analyzed phenotypically and immunologically using 12 representative strains from 51 Y. enterocolitica Korean isolates. A 38-kDa OMP was commonly observed in all strains. However, additional OMPs were also observed in different biotypes and serotypes as well as bacterial origins, by incubating Y. enterocolitica at a low temperature. The specificity of the 38-kDa OMP was confirmed by a Western blot analysis with antisera against Y. enterocolitica and Brucella abortus. The results, therefore, indicate that the 38-kDa OMP could be used as a marker for detecting Y. enterocolitica in the environment or for seromonitoring.

• Journal of Life Science
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• v.25 no.2
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• pp.136-150
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• 2015

Pseudomonas syringae pathovar tabaci is a plant pathogenic bacterium that causes wildfire disease in tobacco plants. In P. syringae pv. tabaci, PsyI, a LuxI-type protein, acts as an AHL synthase, while primary and secondary sequence analysis of PsyR has revealed that it is a homolog of the LuxR-type transcriptional regulator that responds to AHL molecules. In this study, using phenotypic and genetic analyses in P. syringae pv. tabaci, we show the effect of PsyR protein as a quorum-sensing (QS) transcriptional regulator. Regulatory effects of PsyR on swarming motility and production of siderophores, tabtoxin, and N-acyl homoserine lactones were examined via phenotypic assays, and confirmed by quantitative real-time reverse transcription-polymerase chain reaction (qRT-PCR). Further qRT-PCR showed that PsyR regulates expression of these virulence genes in response to environmental signals. However, an upstream region of the gene was not bound with purified MBP-PsyR protein; rather, PsyR was only able to shift the upstream region of psyI. These results suggested that PsyR may be indirectly controlled via intermediate-regulatory systems and that auto-regulation by PsyR does not occur.

• Journal of Food Hygiene and Safety
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• v.38 no.6
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• pp.544-550
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• 2023

To develop a functional probiotic that inhibits gingipain, a major virulence factor of Porphyromonas gingivlais (P. gingivalis), we screened over 30 probiotic strains for their ability to inhibit gingipian activity. We investigated the inhibition of expression of gingipain genes kgp, rgpA, and rgpB as well as gingipain activity, using freeze dried cell-free supernatants of Weisiella cibaria SPM402 (WC402) and Lactobacillus paracasei SMP412 (LP412), both of which demonstrated antibacterial activity against P. gingivalis. Thus, it was verified that kgp expression was reduced by approximately 0.71±0.02 folds and rgpB expression was reduced by approximately 0.71±0.14 folds at a concentration of WC402 10 mg/mL. Meanwhile, at the same concentration of 10 mg/mL of LP412, kgp expression was reduced by approximately 0.19±0.08 folds, rgpA expression was reduced by approximately 0.09±0.02 folds, and rgpB expression was reduced by approximately 0.24±0.03 folds. At a concentration of 10 mg/mL, Kgp activity was inhibited by approximately 78.65±3.58% (cell associated gingipain, CAG), 82.45±1.22% (cell-free gingipain, CFG) by WC402 and 80.71±2.11% (CAG), and 85.81±0.05% (CFG) by LP412 respectively. Rgp activity was also effectively inhibited by approximately 78.6±1.01% (CAG), 86.78±0.47% (CFG) and 82.93±1.26% (CAG), 88.81±0.36% (CFG) by WC402 and LP412 respectively. Based on these results, W. cibaria SPM402 and L. paracasei SPM412 can be regarded as functional probiotics with the ability to inhibit gingipain activity and exhibit antibacterial effects against P. gingivalis.

• Journal of Life Science
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• v.26 no.12
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• pp.1470-1476
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• 2016

The viral hemorrhagic septicemia virus (VHSV), which belongs to the Novirhabdovirus genus of the Rhabdoviridae family, is a viral pathogen that causes severe losses in the olive flounder farming industry. Among six encoding VHSV proteins, the non-virion (NV) protein has been shown to have an impact on virulence. In our previous studies, transcriptomics microarray analysis by using VHSV-infected olive flounder showed that VHSV infection significantly down-regulated the mRNA expression of glycolytic enzymes. In addition, VHSV NV protein variants decreased the intracellular ATP level. Based on these results, we have tried to examine the effect of VHSV NV protein on glycolytic enzyme glucokinase expression, which phosphorylates glucose to glucose 6-phosphate. Our results indicated that the NV protein significantly decreased the mRNA expression of glucokinase in olive flounder HINAE cells. Furthermore, the NV protein played a negative role in the promoter activation of glucokinase. Furthermore, glucose uptake was effectively inhibited by VHSV infection and NV protein expression in olive flounder HINAE cells. These results suggest that the VHSV NV protein negatively regulates glycolytic enzyme expression by a transcription level and eventually leads to gradual morbidity of olive flounder through cellular energy deprivation. The present results may be useful for the prevention and diagnosis of VHSV infection in olive flounder.

• Korean Journal of Microbiology
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• v.42 no.3
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• pp.195-198
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• 2006

Lethal toxin is a critical virulence factor of anthrax. It is composed two protein: protective antigen (PA) and lethal factor (LF). PA binds to specific cell surface receptors and, forms a membrane channel that mediates entry of LF into the cell. LF is a zinc-dependent metalloprotease, which cleaves MKKs [MAPK (mitogen-activated protein kinase) kinases] at peptide bonds very close to their N-termini. In this study, we suggest application of cell-based assays in the early phase of drug discovery, with a particular focus on the use of yeast cells. We constructed MEK1 expression system in yeast to determine LF activity and approached cell-based assay system to screen inhibitors, in which the results covering the construction of LF-substrate in yeast expression vector, expression, and LF-mediated proteolysis of substrate were described. These results could provided the basic steps in design of cell-based assay system with the high efficiency, rapidly and easy way to screening of inhibitors.

• The Plant Pathology Journal
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• v.28 no.3
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• pp.311-316
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• 2012

Fusarium root disease can be a serious problem in forest and conservation nurseries in the western United States. Fusarium inoculum is commonly found in most container and bareroot nurseries on healthy and diseased seedlings, in nursery soils, and on conifer seeds. Fusarium spp. within the F. oxysporum species complex have been recognized as pathogens for more than a century, but attempts to distinguish virulence by correlating morphological characteristics with results of pathogenicity tests were unsuccessful. Recent molecular characterization and pathogenicity tests, however, revealed that selected isolates of F. oxysporum are benign on Douglas-fir (Pseudotsuga menziesii) seedlings. Other morphologically indistinguishable isolates, which can be virulent, were identified as F. commune, a recently described species. In a replicated greenhouse study, inoculating Douglas-fir seedlings with one isolate of F. oxysporum prevented expression of disease caused by a virulent isolate of F. commune. Moreover, seedling survival and growth was unaffected by the presence of the F. oxysporum isolate, and this isolate yielded better biological control than a commercial formulation of Bacillus subtilis. These results demonstrate that an isolate of nonpathogenic F. oxysporum can effectively reduce Fusarium root disease of Douglas-fir caused by F. commune under nursery settings, and this biological control approach has potential for further development.

• Journal of Microbiology and Biotechnology
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• v.27 no.3
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• pp.610-615
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• 2017

When Shigella infect host cells, various effecter molecules are delivered into the cytoplasm of the host cell through the type III secretion system (TTSS) to facilitate their invasion process and control the host immune responses. Among these effectors, the S. flexneri effector OspF dephosphorylates mitogen-activated protein kinases and translocates itself to the nucleus, thus preventing histone H3 modification to regulate expression of proinflammatory cytokines. Despite the critical role of OspF, the mechanism by which it localizes in the nucleus has remained to be elucidated. In the present study, we identified a potential small ubiquitin-related modifier (SUMO) modification site within OspF and we demonstrated that Shigella TTSS effector OspF is conjugated with SUMO in the host cell and this modification mediates the nuclear translocation of OspF. Our results show a bacterial virulence factor can exploit host post-translational machinery to execute its intracellular trafficking.