메뉴 건너뛰기




Volumn 274, Issue 21, 2007, Pages 5749-5758

Expression of the recombinant bacterial outer surface protein A in tobacco chloroplasts leads to thylakoid localization and loss of photosynthesis

Author keywords

Lyme disease; Outer surface protein A; Plant vaccine; Protein palmitoylation; Thylakoid targeting

Indexed keywords

CHLOROPHYLL; OUTER MEMBRANE PROTEIN A; RECOMBINANT PROTEIN;

EID: 35448994846     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.06095.x     Document Type: Article
Times cited : (46)

References (38)
  • 1
    • 33845756751 scopus 로고    scopus 로고
    • Approaches to achieve high-level heterologous protein production in plants
    • Streatfield SJ (2007) Approaches to achieve high-level heterologous protein production in plants. Plant Biotechnol J 5, 2 15.
    • (2007) Plant Biotechnol J , vol.5 , pp. 2-15
    • Streatfield, S.J.1
  • 2
    • 23744514106 scopus 로고    scopus 로고
    • Molecular farming for new drugs and vaccines. Current perspectives on the production of pharmaceuticals in transgenic plants
    • Ma JK, Barros E, Bock R, Christou P, Dale PJ, Dix PJ, Fischer R, Irwin J, Mahoney R, Pezzotti M et al. (2005) Molecular farming for new drugs and vaccines. Current perspectives on the production of pharmaceuticals in transgenic plants. EMBO Rep 6, 593 599.
    • (2005) EMBO Rep , vol.6 , pp. 593-599
    • Ma, J.K.1    Barros, E.2    Bock, R.3    Christou, P.4    Dale, P.J.5    Dix, P.J.6    Fischer, R.7    Irwin, J.8    Mahoney, R.9    Pezzotti, M.10
  • 3
    • 0042698429 scopus 로고    scopus 로고
    • Benefits and risks of antibody and vaccine production in transgenic plants
    • Warzecha H Mason HS (2003) Benefits and risks of antibody and vaccine production in transgenic plants. J Plant Physiol 160, 755 764.
    • (2003) J Plant Physiol , vol.160 , pp. 755-764
    • Warzecha, H.1    Mason, H.S.2
  • 4
    • 34147153529 scopus 로고    scopus 로고
    • Production of biopharmaceuticals and vaccines in plants via the chloroplast genome
    • Daniell H (2006) Production of biopharmaceuticals and vaccines in plants via the chloroplast genome. Biotechnol J 1, 1071 1079.
    • (2006) Biotechnol J , vol.1 , pp. 1071-1079
    • Daniell, H.1
  • 5
    • 34147158443 scopus 로고    scopus 로고
    • Plastid biotechnology: Prospects for herbicide and insect resistance, metabolic engineering and molecular farming
    • Bock R (2007) Plastid biotechnology: prospects for herbicide and insect resistance, metabolic engineering and molecular farming. Curr Opin Biotechnol 18, 100 106.
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 100-106
    • Bock, R.1
  • 6
    • 0035979785 scopus 로고    scopus 로고
    • Expression of the native cholera toxin b subunit gene and assembly as functional oligomers in transgenic tobacco chloroplasts
    • Daniell H, Lee SB, Panchal T Wiebe PO (2001) Expression of the native cholera toxin b subunit gene and assembly as functional oligomers in transgenic tobacco chloroplasts. J Mol Biol 311, 1001 1009.
    • (2001) J Mol Biol , vol.311 , pp. 1001-1009
    • Daniell, H.1    Lee, S.B.2    Panchal, T.3    Wiebe, P.O.4
  • 10
    • 0024362494 scopus 로고
    • Lyme-disease
    • Steere AC (1989) Lyme-disease. N Engl J Med 321, 586 596.
    • (1989) N Engl J Med , vol.321 , pp. 586-596
    • Steere, A.C.1
  • 12
    • 0032560790 scopus 로고    scopus 로고
    • A vaccine consisting of recombinant Borrelia burgdorferi outer-surface protein a to prevent Lyme disease. Recombinant Outer-Surface Protein a Lyme Disease Vaccine Study Consortium
    • Sigal LH, Zahradnik JM, Lavin P, Patella SJ, Bryant G, Haselby R, Hilton E, Kunkel M, Adler-Klein D, Doherty T et al. (1998) A vaccine consisting of recombinant Borrelia burgdorferi outer-surface protein A to prevent Lyme disease. Recombinant Outer-Surface Protein A Lyme Disease Vaccine Study Consortium. N Engl J Med 339, 216 222.
    • (1998) N Engl J Med , vol.339 , pp. 216-222
    • Sigal, L.H.1    Zahradnik, J.M.2    Lavin, P.3    Patella, S.J.4    Bryant, G.5    Haselby, R.6    Hilton, E.7    Kunkel, M.8    Adler-Klein, D.9    Doherty, T.10
  • 13
    • 0025264283 scopus 로고
    • Immunogenic integral membrane proteins of Borrelia burgdorferi are lipoproteins
    • Brandt ME, Riley BS, Radolf JD Norgard MV (1990) Immunogenic integral membrane proteins of Borrelia burgdorferi are lipoproteins. Infect Immun 58, 983 991.
    • (1990) Infect Immun , vol.58 , pp. 983-991
    • Brandt, M.E.1    Riley, B.S.2    Radolf, J.D.3    Norgard, M.V.4
  • 15
    • 0027978073 scopus 로고
    • Biological activities of native and recombinant Borrelia burgdorferi outer surface protein A: Dependence on lipid modification
    • Weis JJ, Ma Y Erdile LF (1994) Biological activities of native and recombinant Borrelia burgdorferi outer surface protein A: dependence on lipid modification. Infect Immun 62, 4632 4636.
    • (1994) Infect Immun , vol.62 , pp. 4632-4636
    • Weis, J.J.1    Ma, Y.2    Erdile, L.F.3
  • 17
    • 0028987131 scopus 로고
    • Lipoproteins of Gram-positive bacteria
    • Sutcliffe IC Russell RR (1995) Lipoproteins of Gram-positive bacteria. J Bacteriol 177, 1123 1128.
    • (1995) J Bacteriol , vol.177 , pp. 1123-1128
    • Sutcliffe, I.C.1    Russell, R.R.2
  • 18
    • 0028067877 scopus 로고
    • Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol
    • Sankaran K Wu HC (1994) Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol. J Biol Chem 269, 19701 19706.
    • (1994) J Biol Chem , vol.269 , pp. 19701-19706
    • Sankaran, K.1    Wu, H.C.2
  • 19
    • 0036066456 scopus 로고    scopus 로고
    • Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes
    • Sutcliffe IC Harrington DJ (2002) Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes. Microbiology 148, 2065 2077.
    • (2002) Microbiology , vol.148 , pp. 2065-2077
    • Sutcliffe, I.C.1    Harrington, D.J.2
  • 20
    • 0024393453 scopus 로고
    • The structure of signal peptides from bacterial lipoproteins
    • Vonheijne G (1989) The structure of signal peptides from bacterial lipoproteins. Protein Eng 2, 531 534.
    • (1989) Protein Eng , vol.2 , pp. 531-534
    • Vonheijne, G.1
  • 21
    • 0000587078 scopus 로고    scopus 로고
    • Biosynthesis of lipoproteins
    • In. Neidhardt, R.C.I., Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., Reznikoff, W.S., Schaechter, M. Umbarger, H.E., eds), pp. American Society for Microbiology, Washington, D.C.
    • Wu HC (1996) Biosynthesis of lipoproteins. In Escherichia coli and Salmonella. Cellular and Molecular Biology (Neidhardt RCI, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Schaechter M Umbarger HE, eds), pp. 1005 1014. American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella. Cellular and Molecular Biology , pp. 1005-1014
    • Wu, H.C.1
  • 22
    • 0034868497 scopus 로고    scopus 로고
    • Stable genetic transformation of tomato plastids and expression of a foreign protein in fruit
    • Ruf S, Hermann M, Berger IJ, Carrer H Bock R (2001) Stable genetic transformation of tomato plastids and expression of a foreign protein in fruit. Nat Biotechnol 19, 870 875.
    • (2001) Nat Biotechnol , vol.19 , pp. 870-875
    • Ruf, S.1    Hermann, M.2    Berger, I.J.3    Carrer, H.4    Bock, R.5
  • 23
    • 3543099503 scopus 로고    scopus 로고
    • Palmitoylation of intracellular signaling proteins: Regulation and function
    • Smotrys JE Linder ME (2004) Palmitoylation of intracellular signaling proteins: regulation and function. Annu Rev Biochem 73, 559 587.
    • (2004) Annu Rev Biochem , vol.73 , pp. 559-587
    • Smotrys, J.E.1    Linder, M.E.2
  • 24
    • 0028001503 scopus 로고
    • Efficient targeting of foreign genes into the tobacco plastid genome
    • Zoubenko OV, Allison LA, Svab Z Maliga P (1994) Efficient targeting of foreign genes into the tobacco plastid genome. Nucleic Acids Res 22, 3819 3824.
    • (1994) Nucleic Acids Res , vol.22 , pp. 3819-3824
    • Zoubenko, O.V.1    Allison, L.A.2    Svab, Z.3    Maliga, P.4
  • 25
    • 0035144228 scopus 로고    scopus 로고
    • Sequences downstream of the translation initiation codon are important determinants of translation efficiency in chloroplasts
    • Kuroda H Maliga P (2001) Sequences downstream of the translation initiation codon are important determinants of translation efficiency in chloroplasts. Plant Physiol 125, 430 436.
    • (2001) Plant Physiol , vol.125 , pp. 430-436
    • Kuroda, H.1    Maliga, P.2
  • 26
    • 0033804343 scopus 로고    scopus 로고
    • Disruption of the petB-petD intergenic region in tobacco chloroplasts affects petD RNA accumulation and translation
    • Monde RA, Greene JC Stern DB (2000) Disruption of the petB-petD intergenic region in tobacco chloroplasts affects petD RNA accumulation and translation. Mol Gen Genet 263, 610 618.
    • (2000) Mol Gen Genet , vol.263 , pp. 610-618
    • Monde, R.A.1    Greene, J.C.2    Stern, D.B.3
  • 28
    • 0035852327 scopus 로고    scopus 로고
    • Post-translational protein translocation into thylakoids by the Sec and DeltapH-dependent pathways
    • Mori H Cline K (2001) Post-translational protein translocation into thylakoids by the Sec and DeltapH-dependent pathways. Biochim Biophys Acta 1541, 80 90.
    • (2001) Biochim Biophys Acta , vol.1541 , pp. 80-90
    • Mori, H.1    Cline, K.2
  • 29
    • 0024852098 scopus 로고
    • The reaction specificities of the thylakoidal processing peptidase and Escherichia coli leader peptidase are identical
    • Halpin C, Elderfield PD, James HE, Zimmermann R, Dunbar B Robinson C (1989) The reaction specificities of the thylakoidal processing peptidase and Escherichia coli leader peptidase are identical. EMBO J 8, 3917 3921.
    • (1989) EMBO J , vol.8 , pp. 3917-3921
    • Halpin, C.1    Elderfield, P.D.2    James, H.E.3    Zimmermann, R.4    Dunbar, B.5    Robinson, C.6
  • 30
    • 0025297347 scopus 로고
    • Expression in Escherichia coli of the psbO gene encoding the 33 kd protein of the oxygen-evolving complex from spinach
    • Seidler A Michel H (1990) Expression in Escherichia coli of the psbO gene encoding the 33 kd protein of the oxygen-evolving complex from spinach. EMBO J 9, 1743 1748.
    • (1990) EMBO J , vol.9 , pp. 1743-1748
    • Seidler, A.1    Michel, H.2
  • 31
    • 0022240072 scopus 로고
    • An alternate pathway for the processing of the prolipoprotein signal peptide in Escherichia coli
    • Ghrayeb J, Lunn CA, Inouye S Inouye M (1985) An alternate pathway for the processing of the prolipoprotein signal peptide in Escherichia coli. J Biol Chem 260, 10961 10965.
    • (1985) J Biol Chem , vol.260 , pp. 10961-10965
    • Ghrayeb, J.1    Lunn, C.A.2    Inouye, S.3    Inouye, M.4
  • 32
    • 0027398358 scopus 로고
    • High-frequency plastid transformation in tobacco by selection for a chimeric aadA gene
    • Svab Z Maliga P (1993) High-frequency plastid transformation in tobacco by selection for a chimeric aadA gene. Proc Natl Acad Sci USA 90, 913 917.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 913-917
    • Svab, Z.1    Maliga, P.2
  • 33
    • 0002788379 scopus 로고
    • Extraction of DNA from milligram amounts of fresh, herbarium and mummified plant tissues
    • Rogers SO Bendich AJ (1985) Extraction of DNA from milligram amounts of fresh, herbarium and mummified plant tissues. Plant Mol Biol 5, 69 76.
    • (1985) Plant Mol Biol , vol.5 , pp. 69-76
    • Rogers, S.O.1    Bendich, A.J.2
  • 35
    • 0027163642 scopus 로고
    • Promoter specificity and deletion analysis of three heat stress transcription factors of tomato
    • Treuter E, Nover L, Ohme K Scharf KD (1993) Promoter specificity and deletion analysis of three heat stress transcription factors of tomato. Mol Gen Genet 240, 113 125.
    • (1993) Mol Gen Genet , vol.240 , pp. 113-125
    • Treuter, E.1    Nover, L.2    Ohme, K.3    Scharf, K.D.4
  • 36
    • 4544267873 scopus 로고    scopus 로고
    • Pulse-amplitude-modulation (PAM) fluorometry and saturation pulse method: An overview
    • In. Papageorgiou, G. Govindjee, eds), pp. Springer, Dordrecht.
    • Schreiber U (2004) Pulse-amplitude-modulation (PAM) fluorometry and saturation pulse method: an overview. In Chlorophyll a Fluorescence. A Signature of Photosynthesis (Papageorgiou G Govindjee, eds), pp. 279 319. Springer, Dordrecht.
    • (2004) Chlorophyll a Fluorescence. a Signature of Photosynthesis , pp. 279-319
    • Schreiber, U.1
  • 37
    • 33750985694 scopus 로고    scopus 로고
    • Infection with virulent and avirulent P-syringae strains differentially affects photosynthesis and sink metabolism in Arabidopsis leaves
    • Bonfig KB, Schreiber U, Gabler A, Roitsch T Berger S (2006) Infection with virulent and avirulent P-syringae strains differentially affects photosynthesis and sink metabolism in Arabidopsis leaves. Planta 225, 1 12.
    • (2006) Planta , vol.225 , pp. 1-12
    • Bonfig, K.B.1    Schreiber, U.2    Gabler, A.3    Roitsch, T.4    Berger, S.5
  • 38
    • 0018782257 scopus 로고
    • Resolution of the light-harvesting chlorophyll a-B-protein of Vicia faba chloroplasts into 2 different chlorophyll-protein complexes
    • Machold O Meister A (1979) Resolution of the light-harvesting chlorophyll a-B-protein of Vicia faba chloroplasts into 2 different chlorophyll-protein complexes. Biochim Biophys Acta 546, 472 480.
    • (1979) Biochim Biophys Acta , vol.546 , pp. 472-480
    • MacHold, O.1    Meister, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.