• Journal of Life Science
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• v.18 no.11
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• pp.1606-1611
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• 2008

Outer membrane proteins (OMPs) expressed in the Gram negative bacteria such as Salmonella play multiple functions including material transports, adhesive factors and reception of external signals. This study has been focused on an OmpW protein known as a protein required to form a hydrophobic porin in outer membrane. We have constructed a S. typhimurium CK10 mutant deleting an ompW gene on chromosome. The CK10 strain was more tolerant to SDS than the wild-type strain did. As increase of salt concentration in the culture media, significantly decreased amount of OmpW protein in cells were detected. The maximum OmpW protein was expressed in the absence of salt supplement. However, the growth of CK10 strain was indistinguishable compared to that of the wild-type strain at the variable osmotic conditions. The biological role of differential OmpW expression in response to osmotic conditions remains to be investigated.

• Journal of Pharmaceutical Investigation
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• v.25 no.1
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• pp.19-29
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• 1995

The study was carried out to develop useful formulation for omeprazole(OMP) through OMP-ethylendiamine complex(OMPED), and the pharmaceutical properties of formula were tested to find out the difference in vivo behaviors of formulations between the free and complexed OMP. Oral and suppository dosage forms were also formulated and the dissolution profiles and pharmacokinetic parameters were measured to observe the difference in bioavailability between the free and complex form, and the correlation between dissolution rate and bioavailability was evaluated. The results are summarized as follows; In the case of formulation for oral administration, the release of OMP from enteric OMPED pellets was found satisfactory to the requirement standard and no decomposition of OMP in the pellets was found in acidic solution. Therefore the enteric OMPED pellets are anticipated to be a stable formulation. The release of OMP from OMPED tablet with chitosan as excipient and coated with cellulose acetate phthalate was found to be significantly retarded. The results of bioavailability test for OMP and OMPED tablets with lactose-excipient showed that the AUC value of OMP tablet was $116.89\;{\mu}g\;{\cdot}\;min/ml$, that of OMPED tablet was $161.10\;{\mu}g\;{\cdot}\;min/ml$, respectively. The reason why was thought that OMP decomposes more readily in body than OMPED, and the AUC of the tablet with chitosan-excipient and coated with cellulose acetate phthalate was most enhanced. In the case of bioavailability for suppositories with OMP, $OMP-{\beta}\;-cyclodextrin$ complex and OMPED, the AUC of OMPED suppository was most increased. From the above results, it is thought that the more stable and bioavailable oral or rectal dosage forms could be developed by using the OMPED as a potential OMP complex.

• 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).

• 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.

• Journal of Microbiology and Biotechnology
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• v.16 no.10
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• pp.1529-1536
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• 2006

We cloned a gene of ompH(D:4) from pigs infected with P. multocida D:4 in Korea [16]. The gene is composed of 1,026 nucleotides coding 342 amino acids (aa) with a signal peptide of 20 aa (GenBank accession number AY603962). In this study, we analyzed the ability of the ompH(D:4) to induce protective immunity against a wild-type challenge in mice. To determine appropriate epitope(s) of the gene, one full and three different types of truncated genes of the ompH(D:4) were constructed by PCR using pET32a or pRSET B as vectors. They were named ompH(D:4)-F (1,026 bp [1-1026] encoding 342 aa), ompH(D:4)-t1 (693 bp [55-747] encoding 231 aa), ompH(D:4)-t2 (561 bp [187-747] encoding 187 aa), and ompH(D:4)-t3 (540 bp [487-1026] encoding 180 aa), respectively. The genes were successfully expressed in Escherichia coli BL21(DE3). Their gene products, polypeptides, OmpH(D:4)-F, -t1, -t2, and -t3, were purified individually using nickel-nitrilotriacetic acid (Ni-NTA) affinity column chromatography. Their $M_rs$ were determined to be 54.6, 29, 24, and 23.2 kDa, respectively, using SDS-PAGE. Antisera against the four kinds of polypeptides were generated in mice for protective immunity analyses. Some $50{\mu}g$ of the four kinds of polypeptides were individually provided intraperitoneally with mice (n=20) as immunogens. The titer of post-immunized antiserum revealed that it grew remarkably compared with pre-antiserum. The lethal dose of the wild-type pathogen was determined at $10{\mu}l$ of live P. multocida D:4 through direct intraperitoneal (IP) injection, into post-immune mice (n=5, three times). Some thirty days later, the lethal dose ($10{\mu}l$) of live pathogen was challenged into the immunized mouse groups [OmpH(D:4)-F, -t1, -t2, and -t3; n=20 each, two times] as well as positive and negative control groups. As compared within samples, the OmpH(D:4)-F-immunized groups showed lower immune ability than the OmpH(D:4)-t1, -t2, and -t3. The results show that the truncated-OmpH(D:4)-t1, -t2, and -t3 can be used for an effective vaccine candidate against swine atrophic rhinitis caused by pathogenic P. multocida (D:4) isolated in Korea.

• 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).

• 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.

• 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).

• 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.

• Journal of the Institute of Electronics and Information Engineers
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• v.49 no.9
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• pp.138-144
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• 2012

In this paper, we introduce the time-domain equalizer in orthogonal frequency division multiplexing (OFDM) systems using orthogonal matching pursuit (OMP) algorithm. Since OFDM system inserts guard intervals, it shows robust performance against multi-path fading. However, in Doppler channel, inter-carrier interference (ICI) occurs because an orthogonality of sub-carriers does not maintain. A least squares (LS) algorithm is common method of time-domain equalizer, but if a channel length is longer, the performance deteriorates by noise. The multi-path fading is a summation of the different delay signal. And that has sparse properties in time-domain. Because the OMP algorithm of the compressive sensing (CS) algorithm restores the channel by choosing the important elements of sparse channel, it can reduce the influence of noise. We simulate the performance of time-domain equalizer in OFDM system with various channel environments using OMP algorithm compared with other equalization method.