Pathogenesis of Enterohemorrhagic <i>Escherichia coli</i> O157:H7 is mediated by the cytochrome P450 family in <i>Caenorhabditis elegans</i> animal model

Ryu, S.,Oh, S.,Park, M.R.,Lee, W.J.,Yun, B.,Choi, H.J.,Oh, M.H.,Oh, N.S.,Song, M.H.,Kim, Y. BUTTERWORTH-HEINEMANN 2019 FOOD CONTROL Vol.103 No.-

<P><B>Abstract</B></P> <P>Foodborne pathogens, including enterohemorrhagic <I>Escherichia coli</I> (EHEC) O157:H7, may enter from the farm environment and foods via several different vectors and influence human health. Here, we employed <I>Caenorhabditis elegans</I> as a host model system and compared specific host responses during EHEC O157:H7 infection using whole-transcriptome analysis. To elucidate the immune pathways stimulated by EHEC O157:H7, we employed quantitative real-time polymerase chain reaction (qRT-PCR), transgenic worms, and RNAi. Whole-transcriptome analysis revealed that genes encoding the cytochrome P450 (CYP450) family were induced more than 10-fold during EHEC O157:H7 infection in <I>C. elegans</I> host models. Importantly, <I>C. elegans</I> mutants lacking CYP450 genes were highly susceptible to EHEC O157:H7 infection compared with wild-type N2 worms. Consistent with susceptibility tests, qRT-PCR results indicated that CYP450 loss-of-function mutations significantly affected the transcriptional induction of antimicrobial peptide genes, such as <I>clec-60</I>. Together, our results provide critical insights into host strategies for avoiding EHEC O157:H7 pathogenesis in the gastrointestinal tract via the cytochrome P450 family and highlights potential molecular targets for preventing the virulence of EHEC O157:H7 in foods.</P>

Oxidative degradation of endotoxin by advanced oxidation process (O₃/H₂O₂ & UV/H₂O₂)

Oh, B.T.,Seo, Y.S.,Sudhakar, D.,Choe, J.H.,Lee, S.M.,Park, Y.J.,Cho, M. Elsevier Scientific Pub. Co 2014 Journal of hazardous materials Vol.279 No.-

The presence of endotoxin in water environments may pose a serious public health hazard. We investigated the effectiveness of advanced oxidative processes (AOP: O<SUB>3</SUB>/H<SUB>2</SUB>O<SUB>2</SUB> and UV/H<SUB>2</SUB>O<SUB>2</SUB>) in the oxidative degradation of endotoxin. In addition, we measured the release of endotoxin from Escherichia coli following typical disinfection methods, such as chlorine, ozone alone and UV, and compared it with the use of AOPs. Finally, we tested the AOP-treated samples in their ability to induce tumor necrosis factor alpha (TNF-α) in mouse peritoneal macrophages. The production of hydroxyl radical in AOPs showed superior ability to degrade endotoxin in buffered solution, as well as water samples from Korean water treatment facilities, with the ozone/H<SUB>2</SUB>O<SUB>2</SUB> being more efficient compared to UV/H<SUB>2</SUB>O<SUB>2</SUB>. In addition, the AOPs proved effective not only in eliminating E. coli in the samples, but also in endotoxin degradation, while the standard disinfection methods lead to the release of endotoxin following the bacteria destruction. Furthermore, in the experiments with macrophages, the AOPs-deactivated endotoxin lead to the smallest induction of TNF-α, which shows the loss of inflammation activity, compared to ozone treatment alone. In conclusion, these results suggest that AOPs offer an effective and mild method for endotoxin degradation in the water systems.

H3K27 methylation and H3S28 phosphorylation-dependent transcriptional regulation by INHAT subunit SET/TAF-Iβ

Kim, J.Y.,Kim, K.B.,Son, H.J.,Chae, Y.C.,Oh, S.T.,Kim, D.W.,Pak, J.H.,Seo, S.B. North-Holland Pub ; Elsevier Science Ltd 2012 FEBS letters Vol.586 No.19

Significant progress has been made in understanding the relationship between histone modifications and 'reader' molecules and their effects on transcriptional regulation. A previously identified INHAT complex subunit, SET/TAF-Iβ, binds to histones and inhibits histone acetylation. To investigate the binding specificities of SET/TAF-Iβ to various histone modifications, we employed modified histone tail peptide array analyses. SET/TAF-Iβ strongly recognized PRC2-mediated H3K27me½/3; however, the bindings were completely disrupted by H3S28 phosphorylation. We have demonstrated that SET/TAF-Iβ is sequentially recruited to the target gene promoter ATF3 after the PRC2 complex via H3K27me recognition and may offer additive effects in the repression of the target gene.

Preventive effect of fermented Maillard reaction products from milk proteins in cardiovascular health

Oh, N.S.,Kwon, H.S.,Lee, H.A.,Joung, J.Y.,Lee, J.Y.,Lee, K.B.,Shin, Y.K.,Baick, S.C.,Park, M.R.,Kim, Y.,Lee, K.W.,Kim, S.H. American Dairy Science Association 2014 Journal of dairy science Vol.97 No.6

The aim of this study was to determine the dual effect of Maillard reaction and fermentation on the preventive cardiovascular effects of milk proteins. Maillard reaction products (MRP) were prepared from the reaction between milk proteins, such as whey protein concentrates (WPC) and sodium caseinate (SC), and lactose. The hydrolysates of MRP were obtained from fermentation by lactic acid bacteria (LAB; i.e., Lactobacillus gasseri H10, L. gasseri H11, Lactobacillus fermentum H4, and L. fermentum H9, where human-isolated strains were designated H1 to H15), which had excellent proteolytic and 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activities (>20%). The antioxidant activity of MRP was greater than that of intact proteins in assays of the reaction with 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt and trivalent ferric ions; moreover, the effect of MRP was synergistically improved by fermentation. The Maillard reaction dramatically increased the level of antithrombotic activity and 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) inhibitory effect of milk proteins, but did not change the level of activity for micellar cholesterol solubility. Furthermore, specific biological properties were enhanced by fermentation. Lactobacillus gasseri H11 demonstrated the greatest activity for thrombin and HMGR inhibition in Maillard-reacted WPC, by 42 and 33%, respectively, whereas hydrolysates of Maillard-reacted SC fermented by L. fermentum H9 demonstrated the highest reduction rate for micellar cholesterol solubility, at 52%. In addition, the small compounds that were likely released by fermentation of MRP were identified by size-exclusion chromatography. Therefore, MRP and hydrolysates of fermented MRP could be used to reduce cardiovascular risks.

Bacteroides fragilis의 독소 유전자 분석 및 발병기전에 관한 연구

오희복,이근영,정경태,성원근 국립보건연구원 2000 국립보건원보 Vol.37 No.-

Clostridium difficile에 대한 분자역학적 Database 구축

오희복,정경태,정예선,성원근 국립보건연구원 1999 국립보건원보 Vol.36 No.-

Expression of mosquitocidal crystal protein genes in non-insecticidal Bacillus thuringiensis subsp. israelensis

Gill, S.S.,Oh, H.W.,Lee, D.W.,Roh, J.Y.,Park, H.W.,Jin, B.R.,Je, Y.H.,Kang, S.K. 東亞大學校附設遺傳工學硏究所 1998 遺傳工學硏究 Vol.- No.5

J.Y.ROH,H.W.PARK,Y.H.JE,D.W.LEE,B.R.JIN, H.W.OH,S.S.GILL AND S.K.KANG.1997. Bacillus thuringiensis NTB-1 isolated from soil samples in Korea produces ovoidal parasporal inclusions with proteins of approximately 24-40kDa in size. Although serological study indicated that the isolate has a flagella (H) antigen identical with subsp. israelensis, it seemed to be non-insecticidal against Lepidoptera and Coleoptera as well as Diptera. To investigate the activity of non-insecticidal B.thuringiensis transformed with insecticidal crystal protein genes, cryIVD and cytA genes of B. thuringiensis subsp. morrisoni PG-14, highly toxic to mosquito larvae, were introduced into the isolate NTB-1. The expression of mosquitocidal crystal protein genes in NTB-1 was characterized by SDS-PAGE analysis and electron microscopy. The results showed that crystalline inclusions of host, CryIVD and CytA were stably expressed in the transformant. However, the mosquitocidal activity of transformant was similar to that of B. thuringiensis subsp. kurstaki Cry-B harbouring cryIVD and cytA genes, demonstrating that a synergistic effect by an interaction of both introduced insecticidal and resident non-insecticidal crystal proteins was not observed.

Paenibacillus pueri sp. nov., isolated from Pu'er tea

Kim, B.-C.,Jeong, W.-J.,Kim, D. Y.,Oh, H.-W.,Kim, H.,Park, D.-S.,Park, H.-M.,Bae, K. S. Microbiology Society 2009 International journal of systematic and evolutiona Vol.59 No.5

<P>Pu'er tea is a fermented drink made from the leaves of the tea plant, Camellia sinensis. Two novel bacteria, designated strains b09i-3(T) and b13i-1, were isolated during the process of fermentation of this tea. These isolates were Gram-positive, endospore-forming, motile rods that grew at 25-42 degrees C and pH 5.5-10.4. The DNA G+C content was 56.6-58.4 mol%, the predominant isoprenoid quinone was MK-7 and the predominant cellular fatty acid was anteiso-C(15 : 0) (49.0-50 % of the total). Phylogenetic analysis based on 16S rRNA gene sequences showed that strains b09i-3(T) and b13i-1 shared 99.9 % similarity and were affiliated with a cluster within the family Paenibacillaceae. Strains b09i-3(T) and b13i-1 were related most closely to Paenibacillus ginsengihumi DCY16(T) (97 % 16S rRNA gene sequence similarity). Levels of DNA-DNA relatedness between the two novel isolates and P. ginsengihumi DCY16(T) were below 56 %. The phylogenetic and phenotypic characteristics of these novel isolates allowed them to be distinguished clearly from recognized species of the genus Paenibacillus. Based on these data, strains b09i-3(T) and b13i-1 are considered to represent a novel species of the genus Paenibacillus, for which the name Paenibacillus pueri sp. nov. is proposed. The type species is b09i-3(T) (=KCTC 13223(T)=CECT 7360(T)).</P>

Comparison of 90‐day case‐fatality after ischemic stroke between two different stroke outcome registries using propensity score matching analysis

Yu, K‐,H.,Hong, K‐,S.,Lee, B‐,C.,Oh, M‐,S.,Cho, Y‐,J.,Koo, J‐,S.,Park, J‐,M.,Bae, H‐,J.,Han, M‐,K.,Ju, Y‐,S.,Kang, D‐,W.,Appelros, P. Blackwell Publishing Ltd 2011 Acta neurologica Scandinavica Vol.123 No.5

<P>Yu K‐H, Hong K‐S, Lee B‐C, Oh M‐S, Cho Y‐J, Koo J‐S, Park J‐M, Bae H‐J, Han M‐K, Ju Y‐S, Kang D‐W, Appelros P, Norrving B, Terent A. Comparison of 90‐day case‐fatality after ischemic stroke between two different stroke outcome registries using propensity score matching analysis. 
Acta Neurol Scand: 2011: 123: 325–331. 
© 2010 John Wiley & Sons A/S.</P><P><B>Background – </B> It has not been clarified whether the disparity in ischemic stroke outcome between populations is caused by ethnic and geographic differences or by variations in case mix. Propensity score matching (PSM) analysis can overcome some analytical problems but is rarely used in stroke outcome research. This study was to compare the ischemic stroke case‐fatality between two PSM cohorts of Sweden and Korea.</P><P><B>Methods – </B> Prognostic variables related to baseline characteristics and stroke care were included in our PSM model. Then, we selected 7675 Swedish and 1220 Korean patients with ischemic stroke from each stroke registers and performed one‐to‐one matching based on propensity scores of each patient.</P><P><B>Results – </B> After PSM, all measured variables were well balanced in 1163 matched subjects, and the 90‐day case‐fatality was identical 6.2% (HR 0.997, 95%CI 0.905–1.099) in Sweden and Korea.</P><P><B>Conclusions – </B> No difference is found in the 90‐day case‐fatality in propensity score‐matched Swedish and Korean patients with ischemic stroke.</P>

In vivo imaging of tumor apoptosis using histone H1-targeting peptide

Wang, K.,Purushotham, S.,Lee, J.Y.,Na, M.H.,Park, H.,Oh, S.J.,Park, R.W.,Park, J.Y.,Lee, E.,Cho, B.C.,Song, M.N.,Baek, M.C.,Kwak, W.,Yoo, J.,Hoffman, A.S.,Oh, Y.K.,Kim, I.S.,Lee, B.H. Elsevier Science Publishers 2010 Journal of controlled release Vol.148 No.3

In vivo imaging of apoptosis could allow monitoring of tumor response to cancer treatments such as chemotherapy. Using phage display, we identified the CQRPPR peptide, named ApoPep-1(Apoptosis-targeting Peptide-1), that was able to home to apoptotic and necrotic cells in tumor tissue. ApoPep-1 also bound to apoptotic and necrotic cells in culture, while only little binding to live cells was observed. Its binding to apoptotic cells was not dependent on calcium ion and not competed by annexin V. The receptor for ApoPep-1 was identified to be histone H1 that was exposed on the surface of apoptotic cells. In necrotic cells, ApoPep-1 entered the cells and bound to histone H1 in the nucleus. The imaging signals produced during monitoring of tumor apoptosis in response to chemotherapy was enhanced by the homing of a fluorescent dye- or radioisotope-labeled ApoPep-1 to tumor treated with anti-cancer drugs, whereas its uptake of the liver and lung was minimal. These results suggest that ApoPep-1 holds great promise as a probe for in vivo imaging of apoptosis, while histone H1 is a unique molecular signature for this purpose.