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- 저자 : Langridge, Sean (검색결과 2 건)
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Synthesis and Assembly of Porphyromonas gingivalis Fimbrial Protein in Potato Tissues
Shin, Eun-Ah,Park, Yong Keun,Lee, Kang Oh,Langridge, William H. R.,Lee, Jin-Yong Springer-Verlag 2009 Molecular biotechnology Vol.43 No.2
<P>Periodontal disease caused by the gram-negative oral anaerobic bacterium Porphyromonas gingivalis is thought to be initiated by the binding of P. gingivalis fimbrial protein to saliva-coated oral surfaces. To assess whether biologically active fimbrial antigen can be synthesized in edible plants, a cDNA fragment encoding the C-terminal binding portion of P. gingivalis fimbrial protein, fimA (amino acids 266-337), was cloned behind the mannopine synthase promoter in plant expression vector pPCV701. The plasmid was transferred into potato (Solanum tuberosum) leaf cells by Agrobacterium tumefaciens in vivo transformation methods. The fimA cDNA fragment was detected in transformed potato leaf genomic DNA by PCR amplification methods. Further, a novel immunoreactive protein band of ~6.5 kDa was detected in boiled transformed potato tuber extracts by acrylamide gel electrophoresis and immunoblot analysis methods using primary antibodies to fimbrillin, a monomeric P. gingivalis fimbrial subunit. Antibodies generated against native P. gingivalis fimbriae detected a dimeric form of bacterial-synthesized recombinant FimA(266-337) protein. Further, a protein band of ~160 kDa was recognized by anti-FimA antibodies in undenatured transformed tuber extracts, suggesting that oligomeric assembly of plant-synthesized FimA may occur in transformed plant cells. Based on immunoblot analysis, the maximum amount of FimA protein synthesized in transformed potato tuber tissues was approximately 0.03% of total soluble tuber protein. Biosynthesis of immunologically detectable FimA protein and assembly of fimbrial antigen subunits into oligomers in transformed potato tuber tissues demonstrate the feasibility of producing native FimA protein in edible plant cells for construction of plant-based oral subunit vaccines against periodontal disease caused by P. gingivalis.</P>
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Choi, Eun-Mi,Fix, Thomas,Kursumovic, Ahmed,Kinane, Christy J,Arena, Darí,o,Sahonta, Suman-Lata,Bi, Zhenxing,Xiong, Jie,Yan, Li,Lee, Jun-Sik,Wang, Haiyan,Langridge, Sean,Kim, Young-Min,Borisevich John WileySons, Ltd 2014 Advanced Functional Materials Vol.24 No.47
<P>Highly strained films of BiFe<SUB>0.5</SUB>Mn<SUB>0.5</SUB>O<SUB>3</SUB> (BFMO) grown at very low rates by pulsed laser deposition were demonstrated to exhibit both ferrimagnetism and ferroelectricity at room temperature and above. Magnetisation measurements demonstrated ferrimagnetism (<I>T<SUB>C</SUB></I> ∼ 600K), with a room temperature saturation moment (<I>M<SUB>S</SUB></I>) of up to 90 emu/cc (∼ 0.58 <I>μ<SUB>B</SUB></I>/f.u) on high quality (001) SrTiO<SUB>3</SUB>. X-ray magnetic circular dichroism showed that the ferrimagnetism arose from antiferromagnetically coupled Fe<SUP>3+</SUP> and Mn<SUP>3+</SUP>. While scanning transmission electron microscope studies showed there was no long range ordering of Fe and Mn, the magnetic properties were found to be strongly dependent on the strain state in the films. The magnetism is explained to arise from one of three possible mechanisms with Bi polarization playing a key role. A signature of room temperature ferroelectricity in the films was measured by piezoresponse force microscopy and was confirmed using angular dark field scanning transmission electron microscopy. The demonstration of strain induced, high temperature multiferroism is a promising development for future spintronic and memory applications at room temperature and above.</P>
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