• Title, Summary, Keyword: 38 kDa OMP

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Prevalence of antibody against 38 kDa outer membrane protein of Yersinia enterocolitica in swine (국내 사육돼지에서의 Yersinia enterocolitica 38 kDa outer membrane protein에 대한 항체가 분포)

  • Shin, Seong-jae;Park, Joo-youn;Choi, In-soo;Shin, Na-ri;Yoo, Han-sang
    • Korean Journal of Veterinary Research
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    • v.41 no.1
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    • pp.73-78
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    • 2001
  • Yersinia enterocolitica is an inhabitant in the lower intestinal tract of many domestic and wild animals as well as in the nature. Of the several forms of diseases caused by Y. enterocolitica, an acute enteritis, especially in young children, is the most common form. Infection of the bacteria usually occurs through fecal-oral route by contaminated foods or water, especially mountainspring water. Of the domestic animals, swine has been known as one of the most important carrier in the human infection. Based on the knowledge, prevalence of antibody against Y enterocolitica was investigated with swine sera collected from Korea for the survey of Y enterocolitica infection in swine. As the first step of this survey, we analyzed outer membrane protein (OMP) profiles of the representative strains of Y enterocolitica isolated from the feces of piglets and mountainspring water in Korea. Thirty-eight kDa OMP was identified as the common OMP regardless of origin, serotype, or biotype of Y enterocolitica isolates. Presence of antibody specific for 38 kDa OMP of Y enterocolitica in 1,076 swine sera collected from November 1999 to October 2000 was analysed with ELISA. Antibody titer in sows was significantly higher than that in piglets, growing pigs and finishing pigs (p<0.05). Also, there was seasonal difference in the prevalence of antibody against Y enterocolitica. These results would provide the basic knowledge for controlling the Y enterocolitica infection in human as well as swine.

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Analysis of Outer Membrane Proteins of Yersinia enterocolitica Isolated from Mountainspring Water and Pig

  • Shin, Sung-Jae;Park, Joo-Youn;Park, In-Soo;Shin, Na-Ri;Lee, Deog-Yong;Cho, Young-Wook;Park, Yong-Ha;Yoo, Han-Sang
    • 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.

Proteomic Analysis of Outer Membrane Proteins from Acinetobacter baumannii DU202 in Tetracycline Stress Condition

  • Yun, Sung-Ho;Choi, Chi-Won;Park, Soon-Ho;Lee, Je Chul;Leem, Sun-Hee;Choi, Jong-Soon;Kim, Soohyun;Kim, Seung Il
    • Journal of Microbiology
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    • v.46 no.6
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    • pp.720-727
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    • 2008
  • Acinetobacter baumannii readily developed antimicrobial resistance to clinically available antibiotics. A. baumannii DU202 is a multi-drug resistant strain, and is highly resistant to tetracycline (MIC> $1,024{\mu}g/ml$). The surface proteome of A. baumannii DU202 in response to the sub-minimal inhibitory concentration (subMIC) of tetracycline was analyzed by 2-DE/MS-MS and 1-DE/LC/MS-MS to understand the pathways that form barriers for tetracycline. Membrane expression of major outer membrane proteins (Omps) was significantly decreased in response to the subMIC of tetracycline. These Omps with sizes of 38, 32, 28, and 21 kDa were identified as $OmpA_{38}$, $OmpA_{32}$, CarO, and OmpW, respectively. However, transcription level of these Omps was not significantly changed. 1-DE/LC/MS-MS analysis of secreted proteins showed that $OmpA_{38}$, CarO, OmpW, and other Omps were increasingly secreted at tetracycline condition. This result suggests that A. baumannii actively regulates the membrane expression and the secretion of Omps to overcome antibiotic stress condition.

Molecular Cloning and Characterization of the Gene for Outer Membrane Protein H in a Pasteurella multocida (D:4) Isolate from Pigs with Atrophic Rhinitis Symptoms in Korea

  • LEE, JEONG-MIN;KANG, SEO-YOUNG;PARK, SHIN-IN;WOO, HEE-JONG;KWON, MOO-SIK
    • Journal of Microbiology and Biotechnology
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    • v.14 no.6
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    • pp.1343-1349
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    • 2004
  • A native strain of Pasteurella multocida was isolated from pigs suffering from severe atrophic rhinitis at domestic farms in Gyeonggi Province, Korea, and was identified as capsular serogroup 'D' and somatic serotype '4' by disc diffusion decapsulation and gel diffusion precipitation tests, respectively. The P. multocida (D:4) induced atrophic rhinitis in healthy pigs by the secondary infection. The gene for outer membrane protein H (ompH) of P. multocida (D:4) was cloned in Escherichia coli DH5$\alpha$ by PCR. The open reading frame of the ompH was composed of 1,023 bp, possibly encoding a protein with 341 amino acid residues containing a signal peptide of 20 amino acids at N-terminus, and the gene product with molecular mass of ca. 38 kDa was identified by SDS-PAGE. Hydropathy profiles indicated that there are two variable domains in the OmpH. To express the ompH in E. coli, the gene was manipulated in various ways. Expression of the truncated as well as full-length forms of the recombinant OmpH was fatal to the host E. coli BL21 (DE3). However, the truncated OmpH fused with GST was consecutively expressed in E. coli DH5$\alpha$. A large quantity of the fused polypeptide was purified through GST-affinity chromatography.

Isolation and characterization of the outer membrane vesicle (OMV) protein from Vibrio anguillarum O1 (Vibrio anguillarum O1이 생산하는 Outer Membrane Vesicle (OMV)의 분리 및 OMV 내의 단백질 특성)

  • Hong, Gyeong-Eun;Kim, Dong-Gyun;Min, Mun-Kyeong;Kong, In-Soo
    • Journal of Marine Bioscience and Biotechnology
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    • v.2 no.2
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    • pp.123-125
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    • 2007
  • Vibrio anguillarum is a gram-negative bacterium that causes vibriosis in approximately 80 different fish species. V. anguillarum produces several exotoxins are correlated with the pathogenesis of vibriosis. This study is focused on the composition of the outer membrane vesicle. Most of gram-negative bacteria produce outer membrane vesicle (OMV) during cell growth. OMV was formed from the outer membrane surface of cell and than released to extracellular environment. OMV consists of outer membrane lipids, outer membrane protein (OMP), LPS, and soluble periplasmic components. Also, they contain toxins, adhesions, and immunomodulatory. Many gram-negative bacteria were studied out forming OMV. In Vibrio sp., formation of OMV by electron microscopy has been reported from V. cholerae and V. parahaemolyticus. In present study, we isolated OMV from V. anguillarum and OMV protein was separated by SDS-PAGE. Magor band was sliced and analyzed by MALDI-TOF. The major protein band of 38kDa was identified as OmpU by MALDI-TOF MS analysis.

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