• Title/Summary/Keyword: OMP-2

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Complexation of Omeprazole with Meglumine and its Stability (오메프라졸과 메글루민의 복합체 형성과 안정성)

  • Lee, Gye-Ju;Kim, Sung-Wook;Do, Ki-Chan;Park, Chong-Bum;Hwang, Sung-Joo
    • Journal of Pharmaceutical Investigation
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    • v.27 no.4
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    • pp.253-263
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    • 1997
  • To investigate the interaction of omeprazole (OMP) and meglumine (MEG), a complex was prepared by freeze-drying method in ammoniacal aqueous medium at room temperature and subjected to IR, DSC, and 1H NMR analysis. In addition, the stability of the complex was tested by accelerated stability analysis, and the dissolution rate of both powder and enteric coated was determined pellet by paddle method. The results are as follows; i) IR, DSC, and $^{1}H$ NMR studies indicate the formation of inclusion complex between OMP and MEG probably by electrostatic forces as $[OMP]\;[MEGH]^+$ form in a stoichiometric ratio (1:1) of OMP : MEG. ii) The dissolution rate of enteric coated OMP-MEG complex pellet in simulated enteric fluid was 90.6% in 10 minutes, which may satisfy the requirement for the regulation of dissolution. iii) OMP-MEG complex were decomposed according to pseudo 1st order kinetics: while the decomposition of OMP showed a rate constant $(k_{25^{\circ}C})$ of $5.13{\times}10^{-4}{\cdot}\;day^{-1}$, a half-life$(t_{1/2})$ of 1,350 days, a shelf-life$(T_{90%})$ 205 days and an activation energy of 23.53 kcal/mole. OMP-MEG complex inhibited a rate $(k_{25})$ of $2.92{\times}10^{-4}{\cdot}\;day^{-1}$, a half-life$(t_{1/2})$ of 2,373 days, a shelf-life $(T_{90%})$ of 306 days and an activation energy of 20.18 kcal/mole. iv) OMP was stabilized markedly by the formation of OMP-MEG complex between OMP and MEG, and the humidity increased the stability of OMP-MEG complex by decreasing the decomposition rate$(k_{50^{\circ}C})$ from $1.27{\times}10^{-2}{\cdot}\;day^{-1}$ at 31% R.H. to $2.54{\times}10^{-2}{\cdot}\;day^{-1}$ at 90% R.H.

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Genetic Variations of Outer Membrane Protein Genes of Vibrio harveyi Isolated in Korea and Immunogenicity of OmpW in Olive Flounder, Paralichthys olivaceus (한국에서 분리된 Vibrio harveyi 외막단백질의 유전적 차이와 넙치(Paralichthys olivaceus)에 대한 OmpW의 면역원성 분석)

  • KIM, Myoung-Sug;JIN, Ji-Woong;JUNG, Sung-Hee;SEO, Jung-Soo;HONG, Suhee
    • Journal of Fisheries and Marine Sciences Education
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    • v.27 no.5
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    • pp.1508-1521
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    • 2015
  • Vibrio harveyi is a pathogenic marine bacterium causing systemic symptoms resulting in mass mortalities in fishes and shrimps in aquaculture. Outer membrane proteins(OMPs) are related to the pathogenicity and thus good targets for diagnosis and vaccination for Gram negative bacteria. Recently vaccination strategies using the OMPs have been suggested to control vibriosis in several fish species. In this study, we have isolated V. harveyi from diseased marine fishes from different regions of Korea and investigated genetic variations of four OMP genes including OmpK, OmpU, OmpV and OmpW. Consequently, OmpK and U genes could be divided into 3 subgroups of type I, II, III and type A, B, C, respectively, without any correlation with geographical regions and species while OmpV and W were highly homologous. OmpW gene of V. harveyi FP4138 was fully sequenced and predicted the deduced amino acid sequence to form ${\beta}-barrel$ with hydrophobic channel. Indeed, the immunogenicity of recombinant OmpW produced in Escherichia coli was assessed by vaccinating flounder. As a result, the high antibody response with antibody titer of $4.2{\pm}0.7$ and protection with relative percent survival of 60% against artificial infection of V. harveyi were demonstrated. This result indicates that OmpW is a virulence related factor and it can be a vaccine candidate to prevent a high mortality caused by V. harveyi infection in olive flounder, Paralichthys olivaceus.

Protective immunity induced by recombinant outer membrane protein H of pasteurella multocida (A:3) of fowl cholera in mice (파스튜렐라(A : 3) 균주의 재조합 외막단백질 H에 의한 가금 콜레라 감염 생쥐의 면역성 검정)

  • Kim, Younghwan;Yang, Joo-Sung;Kwon, Moosik
    • Korean Journal of Veterinary Research
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    • v.46 no.2
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    • pp.127-133
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    • 2006
  • Pasteurella multocida is a terrible veterinary pathogen that causes widespread infections in husbandry. To induce homologous and/or heterologous immunity against the infections, outer membrane protein Hs (OmpH) in the envelope of different strains of P. multocida are thought to be attractive vaccine candidates. Previously we cloned and characterized a gene for OmpH from pathogenic P. multocida (A : 3) (In Press, Korean J. Microbiol. Biotechnol. 2005, 33, December). The gene is composed of 1,047 nucleotides (nt) coding 348 amino acids (aa) with signal peptide of 20 aa. The truncated ompH, a gene without nt coding for the signal peptide, was generated using pRSET A to name "pRSET A/OmpH-F2". This truncated ompH was well expressed in Escherichia coli BL21 (DE3). Truncated OmpH was purified for induction of immunity against live pathogen of fowl cholera (P. multocida A : 3) in mice. Some $50{\mu}g$ of the purified polypeptide was intraperitoneally injected into mice two times with 10 day interval. Lethal dose ($25{\mu}l$) of live P. multocida A : 3 was determined by directly injecting the pathogen into wild mice (n = 25). To demonstrate the vaccine candidate of the truncated OmpH, the live pathogen ($25{\mu}l$) was challenged with the OmpH-immunized mouse group as well as positive & negative controls (n = 80). The results show that the truncated OmpH can be used for an effective vaccine production to prevent fowl cholera caused by pathogenic P. multocida (A : 3).

Effect of Cimetidine and Phenobarbital on Metabolite Kinetics of Omeprazole in Rats

  • Park Eun-Ja;Cho Hea-Young;Lee Yong-Bok
    • Archives of Pharmacal Research
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    • v.28 no.10
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    • pp.1196-1202
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    • 2005
  • Omeprazole (OMP) is a proton pump inhibitor used as an oral treatment for acid-related gastrointestinal disorders. In the liver, it is primarily metabolized by cytochrome P-450 (CYP450) isoenzymes such as CYP2C19 and CYP3A4. 5-Hyroxyomeprazole (5-OHOMP) and omeprazole sulfone (OMP-SFN) are the two major metabolites of OMP in human. Cimetidine (CMT) inhibits the breakdown of drugs metabolized by CYP450 and reduces, the clearance of coad-ministered drug resulted from both the CMT binding to CYP450 and the decreased hepatic blood flow due to CMT. Phenobarbital (PB) induces drug metabolism in laboratory animals and human. PB induction mainly involves mammalian CYP forms in gene families 2B and 3A. PB has been widely used as a prototype inducer for biochemical investigations of drug metabolism and the enzymes catalyzing this metabolism, as well as for genetic, pharmacological, and toxicological investigations. In order to investigate the influence of CMT and PB on the metabolite kinetics of OMP, we intravenously administered OMP (30 mg/kg) to rats intraperitoneally pretreated with normal saline (5 mL/kg), CMT (100 mg/kg) or PB (75 mg/kg) once a day for four days, and compared the pharmacokinetic parameters of OMP. The systemic clearance ($CL_{t}$) of OMP was significantly (p<0.05) decreased in CMT-pretreated rats and significantly (p<0.05) increased in PB-pretreated rats. These results indicate that CMT inhibits the OMP metabolism due to both decreased hepatic blood flow and inhibited enzyme activity of CYP2C19 and 3A4 and that PB increases the OMP metabolism due to stimulation of the liver blood flow and/or bile flow, due not to induction of the enzyme activity of CYP3A4.

Sparse Signal Recovery with Parallel Orthogonal Matching Pursuit for Multiple Measurement Vectors (병렬OMP 기법을 통한 복수 측정 벡터기반 성긴 신호의 복원)

  • Park, Jeonghong;Ban, Tae Won;Jung, Bang Chul
    • Journal of the Korea Institute of Information and Communication Engineering
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    • v.17 no.10
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    • pp.2252-2258
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    • 2013
  • In this paper, parallel orthogonal matching pursuit (POMP) is proposed to supplement the simultaneous orthogonal matching pursuit (S-OMP) which has been widely used as a greedy algorithm for sparse signal recovery for multiple measurement vector (MMV) problem. The process of POMP is simple but effective: (1) multiple indexes maximally correlated with the observation vector are chosen at the first iteration, (2) the conventional S-OMP process is carried out in parallel for each selected index, (3) the index set which yields the minimum residual is selected for reconstructing the original sparse signal. Empirical simulations show that POMP for MMV outperforms than the conventional S-OMP both in terms of exact recovery ratio (ERR) and mean-squared error (MSE).

A Brucella Omp16 Conditional Deletion Strain Is Attenuated in BALB/c Mice

  • Zhi, Feijie;Fang, Jiaoyang;Zheng, Weifang;Li, Junmei;Zhang, Guangdong;Zhou, Dong;Jin, Yaping;Wang, Aihua
    • Journal of Microbiology and Biotechnology
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    • v.32 no.1
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    • pp.6-14
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    • 2022
  • Brucella spp. are facultative intracellular pathogens that invade, survive and proliferate in numerous phagocytic and non-phagocytic cell types, thereby leading to human and animal brucellosis. Outer membrane proteins (Omps) are major immunogenic and protective antigens that are implicated in Brucella virulence. A strain deleted of the omp16 gene has not been obtained which suggests that the Omp16 protein is vital for Brucella survival. Nevertheless, we previously constructed an omp16 conditional deletion strain of Brucella, ∆Omp16. Here, the virulence and immune response elicted by this strain were assessed in a mouse model of infection. Splenomegaly was significantly reduced at two weeks post-infection in ∆Omp16-infected mice compared to infection with the parental strain. The bacterial load in the spleen also was significantly decreased at this post-infection time point in ∆Omp16-infected mice. Histopathological changes in the spleen were observed via hematoxylin-eosin staining and microscopic examination which showed that infection with the ∆Omp16 strain alleviated spleen histopathological alterations compared to mice infected with the parental strain. Moreover, the levels of humoral and cellular immunity were similar in both ∆Omp16-infected mice and parental strain-infected mice. The results overall show that the virulence of ∆Omp16 is attenuated markedly, but that the immune responses mediated by the deletion and parental strains in mice are indistinguishable. The data provide important insights that illuminate the pathogenic strategies adopted by Brucella.

Detection of Salmonella in Milk by Sandwich ELISA using Anti-Outer Membrane Protein Immunoglobulins (Anti-Outer Membrane Protein 면역단백질을 이용한 Sandwich ELISA 방법에 의한 우유 내 Salmonella의 검출)

  • 최석호
    • Food Science of Animal Resources
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    • v.24 no.2
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    • pp.176-181
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    • 2004
  • The specificity of sandwich enzyme-linked immunosorbent assay (ELISA) to detect Salmonella in milk was determined in this study. The antibodies used in sandwich ELISA were egg yolk immunoglobulin G (IgY) obtained after immunization of hen with outer membrane protein (OMP) fraction from Salmonella typhimurium and rabbit IgG obtained after immunization of rabbit with the purified OMP with the molecular weight of 40,000. The immunoblot assay showed that the IgY reacted strongly with OMP with the molecular weight of 6,000 and the rabbit IgG reacted strongly with OMP with the molecular weights of 40,000, 35,000, and 6,000 from the bacteria including Salmonella which belongs to Enterobacteriaceae. The IgY and rabbit IgG also reacted with other proteins from Salmonella typhimurium in immunoblot assay. Competitive ELISA showed that IgY showed specifity to react with two strains of Salmonella typhimurium and Salmonella cholerasuis but not with Escherichia coli and Yersinia enterocolitica. Two strains of Salmonella typhimurium added to UHT milk showed the highest absorbance of all the bacteria used in the sandwich ELISA. Some strains of Salmonella cholerasuis showed higher absorbances than non-Salmonella bacteria.

OmpR Is Essential for Growth and Expression of Virulence-related Genes in the Fish Pathogen Edwardsiella piscicida (어류 병원체 Edwardsiella piscicida의 OmpR은 생육과 병원성과 관련된 유전자의 발현에 필수적)

  • Ray, Durga;Kim, Yeon Ha;Choe, unjeong;Kang, Ho Young
    • Journal of Life Science
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    • v.31 no.1
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    • pp.28-36
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    • 2021
  • Edwardsiella piscicida is a significant cause of hemorrhagic septicemia in fish and gastrointestinal infections in humans. Survival bacteria require specialized mechanisms to adapt to environmental fluctuations. Hence, to understand the mechanism through which E. piscicida senses and responds to environmental osmolarity changes, we determined the protein expression profile and physiological properties under various salinity conditions in this study. The OmpR protein is a part of the Env-ZOmpR two-component system that has been implicated in sensing salt stress in bacteria. However, the physiological role played by this protein in E. piscicida remains to be elucidated. Therefore, in this work, the function of the OmpR protein in response to salt stress was investigated. Phenotypic analysis revealed that, in the mutant, three of the biochemical phenotypes were different from the wild type, including, citrate utilization, hydrogen sulfide, and indole production. Introduction of the plasmid containing the entire ompR gene to the mutant strain returned it to its parental phenotype. The retarded growth rate also partially recovered. Furthermore, in our studies, OmpR was not found to be related to cell motility. Taken together, our results from the mutational analysis, the growth assay, MALDI-TOF MS, qRT-PCR, and the phenotype studies suggest that the OmpR of E. piscicida is implicated in osmoregulation, growth, expression of porins (ETAE_1826), virulence-related genes (EseC, EseD and EvpC), and certain genes of unknown function (ETAE_1540 and ETAE_2706).

Construction and Immunogenicity of Recombinant Swinepox Virus Expressing Outer Membrane Protein L of Salmonella

  • Fang, Yizhen;Lin, Huixing;Ma, Zhe;Fan, Hongjie
    • Journal of Microbiology and Biotechnology
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    • v.26 no.7
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    • pp.1173-1181
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    • 2016
  • Salmonella spp. are gram-negative flagellated bacteria that cause a variety of diseases in humans and animals, ranging from mild gastroenteritis to severe systemic infection. To explore development of a potent vaccine against Salmonella infections, the gene encoding outer membrane protein L (ompL) was inserted into the swinepox virus (SPV) genome by homologous recombination. PCR, western blot, and immunofluorescence assays were used to verify the recombinant swinepox virus rSPV-OmpL. The immune responses and protection efficacy of rSPV-OmpL were assessed in a mouse model. Forty mice were assigned to four groups, which were immunized with rSPV-OmpL, inactive Salmonella (positive control), wild-type SPV (wtSPV; negative control), or PBS (challenge control), respectively. The OmpL-specific antibody in the rSPV-OmpL-immunized group increased dramatically and continuously over time post-vaccination, and was present at a significantly higher level than in the positive control group (p < 0.05). The concentrations of IFN-γ and IL-4, which represent Th1-type and Th2-type cytokine responses, were significantly higher (p < 0.05) in the rSPV-OmpL-vaccinated group than in the other three groups. After intraperitoneal challenge with a lethal dose of Salmonella typhimurium CVCC542, eight out of ten mice in the rSPV-OmpL-vaccinated group were protected, whereas all the mice in the negative control and challenge control groups died within 3 days. Passive immune protection assays showed that hyperimmune sera against OmpL could provide mice with effective protection against challenge from S. typhimurium. The recombinant swinepox virus rSPV-OmpL might serve as a promising vaccine against Salmonella infection.

Ethylenediamine Complex for Stabilization of Omeprazole (오메프라졸의 안정화를 위한 에칠렌디아민 복합체 개발)

  • Oh, Sea-Jong;Kim, Eun-Young;Kim, Kil-Soo;Kim, Yuon-Jeung;Lee, Gye-Ju
    • Journal of Pharmaceutical Investigation
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    • v.25 no.1
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    • pp.9-17
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    • 1995
  • To stabilize omeprazole(OMP), ethylenediamine(ED) complex of omeprazole(OMPED) was prepared by reaction between OMP and ED in methanol, and the complex formation was confirmed by the instrumental analysis, i.e., IR, DSC, EA, NMR, MS and XRD. The rates of decomposition of OMP and OMPED in aqueous solution and the shelf lives at standard temperature were measured by accelerated stability analysis. The results are summarized as follows; The mole ratio of OMP and ED in OMPED complex is 1:1, the energy of formation within OMPED might be combined between polar imidazole group of OMP with induced a dipole amine group in the readily polarizable ED molecule. At standard temperature the degradation rate constant of OMP in aqueous solution is $2.540{\times}10^{-2}\;hr^{-1}$ and the shelf life is 4.15 hrs, and in the case of OMPED the degradation rate constant is $7.986{\times}10^{-4}\;hr^{-1}$ and the shelf life is 131.96 hrs. So, the OMPED has about 31 times longer shelf life than OMP. The activation energy of OMP and OMPED are 5.23 and 18.55 kcal $mole^{-1}$ respectively. The stability of OMP is dependent chiefly on pH in the solutions and it decomposes readily in acidic medium by hydrogen ion catalized reaction but becomes stable beyond pH 9.0. In case of the ED-complex, OMPED is stable in neutral as well as in dilute acidic solutions even in pH 6, OMPED is very stable to light(UV), that is, the rate constant and shelf life of OMP are $k=1.0188{\times}10^{-2}\;day^{-1}$, $T_{90%}=4.5 \;days$, on the other hand, the those of OMPED are $k=7.138{\times}10^{-4}\;day^{-1}$, $T_{90%}=64.1\;days$, respectively. From the above results, it is thought that new dosage forms could be developed by using the OMPED as a potential OMP complex.

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