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이우곤,백승철,신민경,정명환,Jin-Sik Park,Jong-Hoon Ha,Dong-Hae Lee,Min Jeong Kim,Jeong-ih Shin,강형련 대한미생물학회 2019 Journal of Bacteriology and Virology Vol.49 No.4
In order to investigate the antioxidant effect of alkylhydroxide peroxidase (ahpC) of Helicobacter pylori (H. pylori) 26695, an ahpC-deficient mutant (H. pylori 26695 ahpC::cat) was generated. ahpC-deficient mutant was grown slowly at lower pressure of oxygen (5% oxygen) compared to the H. pylori 26695. Whole cell proteins isolated form H. pylori 26695 and H. pylori 26695 ahpC::cat were analyzed by MALDI-TOF and tandem-MS. The expression of 15 proteins, including Ppa, HypB, GrpE, Elp, RecA, GroES, Mda66, RibE, NapA, GlnA, BioB, TrxB, Tsf, FumC and Icd, was more than doubled in H. pylori 26695 ahpC::cat. Production of 10 proteins such as UreG, FabE, Adk, Pnp, OorC, AtpA, AtpD, Nqq3, Pfr, and TagD decreased below 50% in H. pylori 26695 ahpC::cat compared to the H. pylori 26695. In microarray analysis, 9 genes including sul1, amiE, frxA, fecA, hyuA, and katA increased in transcription level in H. pylori 26695 ahpC::cat compared to H. pylori 26695. A total of 24 genes, including flaB, protein kinase C inhibitor, cag16, pabC, and sabA, reduced in transcription. 27 genes, including HP0889, showed common expression changes in ahpC, katA, and sodB-deficient mutations. As a result of this study, there were not many genes whose expression was commonly changed by the deletion of each of the three major antioxidant enzymes of H. pylori. These results showed the functions and regulation of the three antioxidant enzymes were different in H. pylori.
Production of the Monoclonal Antibody and the Genomic Library of Helicobacter pylori
RHEE, KWANG HO,LEE, WOO KON 경상대학교 유전공학연구소 1990 遺傳工學硏究所報 Vol.9 No.-
Sixty three monoclonal antibodies(Moabs) to H. pylori were produced and classified into 13 groups according to their reaction pattern in Weatern blot analysis using whole cell lysate antigen of H. pylori. Genomic libary of H. pylori DNA was constructed to express recombinant antigen of H. pylori and 6 positive clons were obtained. Affinity-purified rabbit antibody to clone HRI and 2 reacted to 60 and 71kD antigen, respectively, and HR4 and 6 reacted to 66kD antigen in WEstern blot analysis. Antibody to HR3 reacted to several antigens, 71,66,60,55, and 34kD, and antibody to HR5 reacted to 71, 65, 60, 55, 49, and 34kD antigens. The one of MoAb, HPH216, reacted to HR4 recombinant antigen and 7 MoAbs, HPB3, 30, 33, 34, 36, 37 and 67, reacted to HR5 recombinant antigen. From the E. coli iysogens which have been lysogenized with 5 recombinant clones, 165kD fusion protein from HR4 and 180kD fusion protein with 71 and 29kD fragments from HR5 lysogen were detected.
Helicobacter pylori 편모 유전자의 클로닝 및 염기서열 분석
이광호,이우곤,조명제,도영미,백승철,강경희,박필성,이상룡 경상대학교 유전공학연구소 1993 遺傳工學硏究所報 Vol.12 No.-
A λgt11 expression libary of H. pylori DNA in E. coli Y1090 was screened with flagellin-specific rabbit antiserum for molecular cloning of the flagellin gene of H. pylori. A positive clone, λHPF4, was obtained and the recombinant antigen expressed from λHPF4 was a fusion protein with the molecular weight of 168kd. Sequence analysis of antigen-encoding DNA showed that an open reading frame composed of 1,536 nucleotides encodes a polypepride with a oredicted molecular size of 54kd. This open reading frame did not show the homology with flaA gene encoding 56kd protein of H. pylori and was confirmed as a unique sequence through homoligy searching. Therefore, the cloned antigen is supposed to be the carboxy-terminal region of the other flagellin protein of H. pylori, flaB, with the molecular weight of 58kd.
Helicobacter pylori와 대장균의 Shuttle Vector 개발
조명제,이우곤,이상룡,김경희,안영숙,김성희,김현주,류복덕,최여정,윤영혜,백승철,전영석,이광호 경상대학교 유전공학연구소 1997 遺傳工學硏究所報 Vol.16 No.-
In this study, a vehicle vector using cryptic plasmids was constructed for gene transfer in Helicobacter pylori. pHP51(3.9 kb) and pHP489(1.2 kb) were selected for constructing vectors from cryptic plasmid of H. pylori isolates in Korea. The HindⅢ-digestedDNA fragment(1.2kb) of pHP489 and 1.6kb DNA fragment of pHP51 were ligated with a kanamycin resistance gene(aph3'-Ⅲ) from C. jejuni to produce the recombinant plasmids pHP489K and pHP51K, respectively. Transformation frequency of pHP51K by electroporation was low. But pHP489K could be effectively transformed into various H. pylori strains. In order to design an intermdiate vehicle vector for gene transfer into H. pylori, pBlueHP489K was prepared by recloning pHP489K DNA into pBluescript and pTZ19R vector. This vector permitted the DNA fragment containing pHP489 sequence, aph3'-Ⅲ, and cloned DNA to be cut and self-ligated in the SacⅠ site after cloning. ureA and ureB gene were inserted into pBlueHP489K, resulting in pBlueHP489K/AB. The DNA fragment containing pHP489, kanamycin resistance gene(aph3'-Ⅲ), and urease structural gene was cut away from pBlueHP489K/AB and self-ligated to generate pBlueHP489K/AB. pBlueHP489K/AB made urease-negative H. pylori strains restore their urease activity. By this experiment, pBlueHP489K was confirmed to be the vehicle system for transferring H. pylori genes.
Cloning and DNA Sequencing of Flagellin Gene of Helicobacter pylori
RHEE, KWANG-HO,LEE, WON-KON,CHO, MYUNG-JE,DOH, YOUNG-MI,BAIK, SEUNG-CHUL 경상대학교 유전공학연구소 1992 遺傳工學硏究所報 Vol.11 No.-
A λgtll expression library of Helicobacter pylori DNA was screened with flagllin-specific rabbit antiserum for molecular cloning of the flagellin gene of Helicobacter pylori. A positive clone,λHPF4, was obtained and the recombinant antigen expressed from λHPF4 was a fusion protein with the molecular weight of 168kd. Sequence analysis of antigen-encoding DNA ahowed that an open reading frame of 1536 nucletides encodes a polypeptide with a predicted molecular size of 54kd. This open reading frame did not show any homology with flaA gene encoding 56kd protein of Helicobacter pylori amd was confirmed as a uniques sequence through homology searching. The cloned antigen is tentatively supposed to be the carboxy-termonal region of the other flagellin protein of Helicobacter pylori, flaB, with the molecular weight of 58kd.
이태희,황주희,이우곤,신민경,우혜련,정경민,이창섭 대한의학회 2018 Journal of Korean medical science Vol.33 No.42
Pathogenic gram-negatives that produce 16S ribosomal RNA methyltransferases (16S RMTases) have already been distributed all over the world. To investigate the predominance of aminoglycoside resistance associated with 16S RMTases in Korea, we collected a total of 222 amikacin resistant Gram-negative clinical isolates from patient specimens between 1999 and 2015 from three hospital banks across Korea. ArmA and rmtB were the predominant 16S RMTase genes responsible for aminoglycoside-resistant isolates circulating in Korean community settings although only one rmtA-producing isolate was detected in 2006.