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Characterization of the Salmonella typhi Outer Membrane Protein C
Toobak, Hoda,Rasooli, Iraj,Gargari, Seyed Latif Mousavi,Jahangiri, Abolfazl,Nadoushan, Mohammadreza Jalali,Owlia, Parviz,Astaneh, Shakiba Darvish Alipour The Korean Society for Microbiology and Biotechnol 2013 한국미생물·생명공학회지 Vol.41 No.1
Salmonella enterica serovar typhi, a Gram-negative food-borne pathogen, causes typhoid fever in humans. OmpC is an outer membrane porin of S. typhi expressed throughout the infection period. OmpC is potentially an attractive antigen for multivalent vaccines and diagnostic kit designs. In this study we combined in silico, in vitro and in vivo approaches to analyze various aspects of OmpC's antigenic properties. The conserved region, in addition to secondary and tertiary structures, and linear B cell epitopes, were predicted. A number of results obtained from in silico analyses were validated by experimental studies. OmpC was amplified, cloned and then expressed, with the recombinant protein then being purified. BALB/c mice were immunized by purified denatured OmpC. The titer of antibody was raised. Results of challenges with the pathogen revealed that the immunity is non-protective. Most of the theoretical and experimental results were in consensus. Introduced linear B cell epitopes can be employed for the design of diagnostic kits based on antigen-antibody interactions.
Characterization of the Salmonella typhi Outer Membrane Protein C
( Toobak Hoda1 ),( Iraj Rasooli ),( Seyed Latif Mousavi Gargari ),( Abolfazl Jahangiri ),( Mohammadreza Jalali Nadoushan ),( Parviz Owlia ),( Shakiba Darvish Alipour Astaneh ) 한국미생물생명공학회(구 한국산업미생물학회) 2013 한국미생물·생명공학회지 Vol.41 No.1
Salmonella enterica serovar typhi, a Gram-negative food-borne pathogen, causes typhoid fever in humans. OmpC is an outer membrane porin of S. typhi expressed throughout the infection period. OmpC is potentially an attractive antigen for multivalent vaccines and diagnostic kit designs. In this study we combined in silico, in vitro and in vivo approaches to analyze various aspects of OmpC`s antigenic properties. The conserved region, in addition to secondary and tertiary structures, and linear B cell epitopes, were predicted. A number of results obtained from in silico analyses were validated by experimental studies. OmpC was amplified, cloned and then expressed, with the recombinant protein then being purified. BALB/c mice were immunized by purified denatured OmpC. The titer of antibody was raised. Results of challenges with the pathogen revealed that the immunity is non-protective. Most of the theoretical and experimental results were in consensus. Introduced linear B cell epitopes can be employed for the design of diagnostic kits based on antigen-antibody interactions.
( Kyongcheol Ko ),( Binna Lee ),( Daeeun Cheong ),( Yunjon Han ),( Jonghyun Choi ),( Jaejun Song ) 한국미생물 · 생명공학회 2015 Journal of microbiology and biotechnology Vol.25 No.11
A cell surface display system for heterologous expression of the multifunctional cellulase, CelEx-BR12, in Escherichia coli was developed using truncated E. coli outer membrane protein C (OmpC) as an anchor motif. Cell surface expression of CelEx-BR12 cellulase in E. coli harboring OmpC-fused CelEx-BR12, designated MC4100 (pTOCBR12), was confirmed by fluorescence-activated cell sorting and analysis of outer membrane fractions by western blotting, which verified the expected molecular mass of OmpC-fused CelEx-BR12 (~72 kDa). Functional evidence for exocellulase activity was provided by enzymatic assays of whole cells and outer membrane protein fractions from E. coli MC4100 (pTOCBR12). The stability of E. coli MC4100 (pTOCBR12) cellulase activity was tested by carrying out repeated reaction cycles, which demonstrated the reusability of recombinant cells. Finally, we showed that recombinant E. coli cells displaying the CelEx-BR12 enzyme on the cell surface were capable of growth using carboxymethyl cellulose as the sole carbon source.
TaqMan 실시간 중합 효소 연쇄반응에 의한 살모넬라속의 검출 및 ompC 항원단백 유전자의 비교
이영성,최경성,김명철,한재철,채준석,Lee, Young-Sung,Choi, Kyoung-Seong,Kim, Myeong-Chul,Han, Jae-Cheol,Chae, Joon-Seok 대한수의학회 2002 大韓獸醫學會誌 Vol.42 No.4
Antigenic ompC genes of S. gallinarum, S. pullorum and S. dublin were characterized among Salmonella spp. isolated from chickens and other animals to identify genetic variation. Salmonella ompC gene fragment (1,027 bp) was amplified by PCR and the amplicons were cloned for comparison of nucleotide sequences. The identity of the sequences between S. gallinarum and S. pullorum, S. gallinarum and S. dublin, S. pullorum and S. dublin was 99.8%, 97.6% and 97.8%, respectively. Also, we found that ompC has some diversity between S. gallinarum and S. pullorum, and other Salmonella spp. which may be useful to type the organisms. Similar to diagnosis in other organisms, the TaqMan PCR method can be applied to rapid and accurate diagnosis of salmonellosis in chickens and other animals. We designed PCR primers and TaqMan probe for flagellin gene (fliC) for detection of Salmonella spp. by TaqMan PCR. The TaqMan PCR method was 10,000 times more sensitive than conventional PCR.
In Vitro Selection of RNA Aptamer Specific to Salmonella Typhimurium
( Seung Ryul Han ),( Seong Wook Lee ) 한국미생물 · 생명공학회 2013 Journal of microbiology and biotechnology Vol.23 No.6
Salmonella is a major foodborne pathogen that causes a variety of human diseases. Development of ligands directly and specifically binding to the Salmonella will be crucial for the rapid detection of, and thus for efficient protection from, the virulent bacteria. In this study, we identified a RNA aptamer-based ligand that can specifically recognize Salmonella Typhimurium through SELEX technology. To this end, we isolated and characterized an RNase-resistant RNA aptamer that bound to the OmpC protein of Salmonella Typhimurium with high specificity and affinity (Kd ~ 20 nM). Of note, the selected aptamer was found to specifically bind to Salmonella Typhimurium, but neither to Gram-positive bacteria (Staphylococcus aureus) nor to other Gram-negative bacteria (Escherichia coli O157:H7). This was evinced by aptamer-immobilized ELISA and aptamer-linked precipitation experiments. This Salmonella species-specific aptamer could be useful as a diagnostic ligand against pathogen-caused foodborne sickness.
최경민,김미현,Hua Cai,이용진,홍영진,류필열 전남대학교 의과학연구소 2018 전남의대학술지 Vol.54 No.1
Salmonella enterica serovar Typhimurium is one of the most important bacterial pathogenscausing diarrhea. The resistance of S. typhimurium to antimicrobial agents, whichhas recently been isolated from patients, is causing serious problems. We investigatedthe effects of salicylic acid (Sal) and acetyl salicylate (AcSal) on the susceptibility ofS. typhimurium to cephalosporin antibiotics, which are known to increase resistanceto cephalosporin and quinolone antibiotics. The MIC of cephalosporin antibiotics washigher than that of the media without Sal. The rate of accumulation of ethidium bromide(EtBr) in the bacteria by the outer membrane protein (Omp) was not different fromthat of the bacteria cultured in the medium containing Sal. However, Carbonyl cyanide-m-chlorophenylhydrazone (CCCP), an inhibitor of bacterial efflux pumps, significantlyreduced the rate of accumulation of EtBr in bacteria cultured on Sal containingmedium. In the medium containing CCCP, the MIC of the antimicrobial agent tendedto decrease as compared with the control. In addition, the MIC of the bacteria treatedwith CCCP and Sal was higher than that of the antimicrobial agent against the CCCPtreated experimental bacteria. These results suggest that Sal decreases the expressionof OmpF in the Omp of S. typhimurium and reduces the permeability of cephalosporinantibiotics to bacteria, which may induce tolerance to cephalosporin antibiotics.