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Volumn 24, Issue 3, 2002, Pages 489-496

Purification and characterization of the major lipoprotein (P28) of Spiroplasma apis

Author keywords

Lipoproteins; Membrane proteins; Mollicutes; Spiralin; Spiroplasma

Indexed keywords

APIS; BACTERIA (MICROORGANISMS); MOLLICUTES; SPIROPLASMA; SPIROPLASMA APIS;

EID: 0036452117     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2001.1600     Document Type: Article
Times cited : (3)

References (41)
  • 1
    • 0030748743 scopus 로고    scopus 로고
    • Spiroplasmas: Infectious agents of plants, arthropods and vertebrates
    • Bové, J. M. (1997) Spiroplasmas: Infectious agents of plants, arthropods and vertebrates. Wien. Klin. Wochenschr. 109, 604-612.
    • (1997) Wien. Klin. Wochenschr. , vol.109 , pp. 604-612
    • Bové, J.M.1
  • 4
    • 0017582667 scopus 로고
    • Purification and characterization of spiralin, the main protein of the Spiroplasma citri membrane
    • Wróblewski, H., Johansson, K.-E., and Hjerten, S. (1977) Purification and characterization of spiralin, the main protein of the Spiroplasma citri membrane. Biochim. Biophys. Acta 465, 275-289.
    • (1977) Biochim. Biophys. Acta , vol.465 , pp. 275-289
    • Wróblewski, H.1    Johansson, K.-E.2    Hjerten, S.3
  • 5
    • 0021321759 scopus 로고
    • Comparison of the amino acid compositions and antigenic properties of spiralins purified from the plasma membrane of different spiroplasmas
    • Wróblewski, H., Robic, D., Thomas, D., and Blanchard, A. (1984) Comparison of the amino acid compositions and antigenic properties of spiralins purified from the plasma membrane of different spiroplasmas. Ann. Microbiol. 135A, 73-82.
    • (1984) Ann. Microbiol. , vol.135 A , pp. 73-82
    • Wróblewski, H.1    Robic, D.2    Thomas, D.3    Blanchard, A.4
  • 7
    • 0030006192 scopus 로고    scopus 로고
    • Spiralin polymorphism in strains of Spiroplasma citri is not due to differences in posttranslational palmitoylation
    • Foissac, X., Saillard, C., Gandar, J., Zreik, L., and Bové, J. M. (1996) Spiralin polymorphism in strains of Spiroplasma citri is not due to differences in posttranslational palmitoylation. J. Bacteriol. 178, 2934-2940.
    • (1996) J. Bacteriol. , vol.178 , pp. 2934-2940
    • Foissac, X.1    Saillard, C.2    Gandar, J.3    Zreik, L.4    Bové, J.M.5
  • 8
    • 0025158477 scopus 로고
    • Spiralins of Spiroplasma citri and Spiroplasma melliferum: Amino acid sequences and putative organization in the cell membrane
    • Chevalier, C., Saillard, C., and Bové, J. M. (1990) Spiralins of Spiroplasma citri and Spiroplasma melliferum: Amino acid sequences and putative organization in the cell membrane. J. Bacteriol. 172, 6090-6097.
    • (1990) J. Bacteriol. , vol.172 , pp. 6090-6097
    • Chevalier, C.1    Saillard, C.2    Bové, J.M.3
  • 10
    • 0029859561 scopus 로고    scopus 로고
    • Inhibition of spiralin processing by the lipopeptide antibiotic globomycin
    • Béven, L., Le Hénaff, M., Fontenelle, C., and Wróblewski, H. (1996) Inhibition of spiralin processing by the lipopeptide antibiotic globomycin. Curr. Microbiol. 33, 317-322.
    • (1996) Curr. Microbiol. , vol.33 , pp. 317-322
    • Béven, L.1    Le Hénaff, M.2    Fontenelle, C.3    Wróblewski, H.4
  • 11
    • 0029017836 scopus 로고
    • Conformation, pore-forming activity, and antigenicity of synthetic peptide analogues of a spiralin putative amphipathic α helix
    • Brenner, C., Ducloyier, H., Krchňák, V., and Wróblewski, H. (1995) Conformation, pore-forming activity, and antigenicity of synthetic peptide analogues of a spiralin putative amphipathic α helix. Biochim. Biophys. Acta 1235, 161-168.
    • (1995) Biochim. Biophys. Acta , vol.1235 , pp. 161-168
    • Brenner, C.1    Ducloyier, H.2    Krchňák, V.3    Wróblewski, H.4
  • 12
    • 0030843508 scopus 로고    scopus 로고
    • Spiralin, a mycoplasmal membrane lipoprotein, induces T-cell-independent B-cell blastogenesis and secretion of proinflammatory cytokines
    • Brenner, C., Wróblewski, H., Le Hénaff, M., Montagnier, L., and Blanchard, A. (1997) Spiralin, a mycoplasmal membrane lipoprotein, induces T-cell-independent B-cell blastogenesis and secretion of proinflammatory cytokines. Infect. Immun. 65, 4322-4329.
    • (1997) Infect. Immun. , vol.65 , pp. 4322-4329
    • Brenner, C.1    Wróblewski, H.2    Le Hénaff, M.3    Montagnier, L.4    Blanchard, A.5
  • 13
    • 0034051279 scopus 로고    scopus 로고
    • Chemical analysis of processing of spiralin, the major lipoprotein of Spiroplasma melliferum
    • Le Hénaff, M., and Fontenelle, C. (2000) Chemical analysis of processing of spiralin, the major lipoprotein of Spiroplasma melliferum. Arch. Microbiol. 173, 339-345.
    • (2000) Arch. Microbiol. , vol.173 , pp. 339-345
    • Le Hénaff, M.1    Fontenelle, C.2
  • 14
    • 0030865158 scopus 로고    scopus 로고
    • Sequence analysis of Spiroplasma phoeniceum and Spiroplasma kunkelii spiralin genes and comparison with other spiralin genes
    • Foissac, X., Bové, J. M., and Saillard, C. (1997) Sequence analysis of Spiroplasma phoeniceum and Spiroplasma kunkelii spiralin genes and comparison with other spiralin genes. Curr. Microbiol. 35, 240-243.
    • (1997) Curr. Microbiol. , vol.35 , pp. 240-243
    • Foissac, X.1    Bové, J.M.2    Saillard, C.3
  • 16
    • 0020947528 scopus 로고
    • Analysis of Spiroplasma proteins: Contribution of group IV spiroplasmas and characterization of spiroplasma protein antigens
    • Mouchés, C., Candresse, T., McGarrity, G. J., and Bové, J. M. (1983) Analysis of Spiroplasma proteins: Contribution of group IV spiroplasmas and characterization of spiroplasma protein antigens. Yale J. Biol. Med. 56, 431-437.
    • (1983) Yale J. Biol. Med. , vol.56 , pp. 431-437
    • Mouchés, C.1    Candresse, T.2    McGarrity, G.J.3    Bové, J.M.4
  • 17
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114
    • Bordier, C. (1981) Phase separation of integral membrane proteins in Triton X-114. J. Biol. Chem. 256, 1604-1607.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0025143157 scopus 로고
    • Antigenic relatedness between the spiralins of Spiroplasma citri and Spiroplasma melliferum
    • Zaaria, A., Fontenelle, C., Le Hénaff, M., and Wróblewski, H. (1990) Antigenic relatedness between the spiralins of Spiro-plasma citri and Spiroplasma melliferum. J. Bacteriol. 172, 5494-5496.
    • (1990) J. Bacteriol. , vol.172 , pp. 5494-5496
    • Zaaria, A.1    Fontenelle, C.2    Le Hénaff, M.3    Wróblewski, H.4
  • 20
    • 0001617588 scopus 로고
    • A quantitative immunoelectrophoresis method
    • Clarke, H. G. M., and Freeman, T. A. (1967) A quantitative immunoelectrophoresis method. Protides Biol. Fluids 14, 503-509.
    • (1967) Protides Biol. Fluids , vol.14 , pp. 503-509
    • Clarke, H.G.M.1    Freeman, T.A.2
  • 21
    • 0000524433 scopus 로고
    • Charge-shift electrophoresis: Simple method for distinguishing between amphiphilic and hydrophilic proteins in detergent solution
    • Helenius, A., and Simons, K. (1977) Charge-shift electrophoresis: Simple method for distinguishing between amphiphilic and hydrophilic proteins in detergent solution. Proc. Natl. Acad Sci. USA 74, 529-532.
    • (1977) Proc. Natl. Acad Sci. USA , vol.74 , pp. 529-532
    • Helenius, A.1    Simons, K.2
  • 22
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • Kyhse-Anderson, J. (1984) Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J. Biochem. Biophys. Methods 10, 203-209.
    • (1984) J. Biochem. Biophys. Methods , vol.10 , pp. 203-209
    • Kyhse-Anderson, J.1
  • 23
    • 0020074305 scopus 로고
    • A dot-immunobinding assay for monoclonal and other antibodies
    • Hawkes, R., Niday, E., and Gordon, J. (1982) A dot-immunobinding assay for monoclonal and other antibodies. Anal. Biochem. 119, 142-147.
    • (1982) Anal. Biochem. , vol.119 , pp. 142-147
    • Hawkes, R.1    Niday, E.2    Gordon, J.3
  • 24
    • 0001934225 scopus 로고
    • Identification and characterization of lipid modified membrane proteins
    • Hooper, N. M., and Turner, A. J., Eds., IRL Press, Oxford
    • Hayashi, S., and Wu, H. C. (1992) Identification and characterization of lipid modified membrane proteins, in "Lipid Modification of Proteins: A Practical Approach" (Hooper, N. M., and Turner, A. J., Eds.), pp. 261-285, IRL Press, Oxford.
    • (1992) Lipid Modification of Proteins: A Practical Approach , pp. 261-285
    • Hayashi, S.1    Wu, H.C.2
  • 25
    • 0025947274 scopus 로고
    • Determination of fatty acids in the main lipoprotein classes by capillary gas chromatography: BF3/methanol transesterification of lyophilized sample instead of Folch extraction gives higher yields
    • Sattler, W., Puhl, H., Hayn, M., Kostner, G. M., and Esterbauer, H. (1991) Determination of fatty acids in the main lipoprotein classes by capillary gas chromatography: BF3/methanol transesterification of lyophilized sample instead of Folch extraction gives higher yields. Anal. Biochem. 198, 184-190.
    • (1991) Anal. Biochem. , vol.198 , pp. 184-190
    • Sattler, W.1    Puhl, H.2    Hayn, M.3    Kostner, G.M.4    Esterbauer, H.5
  • 27
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and in lipoprotein samples
    • Markwell, M. A. K., Hass, S. M., Bieder, L. L., and Tolbert, N. E. (1978) A modification of the Lowry procedure to simplify protein determination in membrane and in lipoprotein samples. Anal. Biochem. 87, 206-210.
    • (1978) Anal. Biochem. , vol.87 , pp. 206-210
    • Markwell, M.A.K.1    Hass, S.M.2    Bieder, L.L.3    Tolbert, N.E.4
  • 28
    • 0027316094 scopus 로고
    • Adaptative surface variation in mycoplasmas
    • Wise, K. S. (1993) Adaptative surface variation in mycoplasmas. Trends Microbiol. 1, 59-63.
    • (1993) Trends Microbiol. , vol.1 , pp. 59-63
    • Wise, K.S.1
  • 29
    • 0033385551 scopus 로고    scopus 로고
    • Interactions between mycoplasma lipoproteins and the host immune system
    • Chambaud, I., Wróblewski, H., and Blanchard, A. (1999) Interactions between mycoplasma lipoproteins and the host immune system. Trends Microbiol. 7, 493-499.
    • (1999) Trends Microbiol. , vol.7 , pp. 493-499
    • Chambaud, I.1    Wróblewski, H.2    Blanchard, A.3
  • 30
    • 0028067877 scopus 로고
    • Lipid modification of bacterial prolipoprotein
    • Sankaran, K., and Wu, H. C. (1994) Lipid modification of bacterial prolipoprotein. J. Biol. Chem. 269, 19701-19706.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19701-19706
    • Sankaran, K.1    Wu, H.C.2
  • 31
    • 0021100166 scopus 로고
    • Proteolipid formation in Mycoplasma capricolum
    • Dahl, C. E., Dahl, J. S., and Bloch, K. (1983) Proteolipid formation in Mycoplasma capricolum. J. Biol. Chem. 258, 11814-11818.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11814-11818
    • Dahl, C.E.1    Dahl, J.S.2    Bloch, K.3
  • 32
    • 0026533923 scopus 로고
    • Membrane protein acylation: Preference for exogenous myristic acid or endogenous saturated chains in Acholeplasma laidlawii
    • Nyström, S., Wallbrandt, P., and Wieslander, Å. (1992) Membrane protein acylation: Preference for exogenous myristic acid or endogenous saturated chains in Acholeplasma laidlawii. Eur. J. Biochem. 204, 231-240.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 231-240
    • Nyström, S.1    Wallbrandt, P.2    Wieslander, Å.3
  • 33
    • 0344146587 scopus 로고    scopus 로고
    • Selective acylation of plasma membrane proteins of Mycoplasma agalactiae, the causal agent of agalactia
    • Le Hénaff, M., Guéguen, M. M., and Fontenelle, C. (2000) Selective acylation of plasma membrane proteins of Mycoplasma aga-lactiae, the causal agent of agalactia. Curr. Microbiol. 40, 23-28.
    • (2000) Curr. Microbiol. , vol.40 , pp. 23-28
    • Le Hénaff, M.1    Guéguen, M.M.2    Fontenelle, C.3
  • 34
    • 0035197927 scopus 로고    scopus 로고
    • Chemical analysis of lipid-modified membrane proteins in Acholeplasma laidlawii
    • Le Hénaff, M., Chollet, A., and Fontenelle, C. (2001) Chemical analysis of lipid-modified membrane proteins in Acholeplasma laidlawii. Curr. Microbiol. 43, 424-428.
    • (2001) Curr. Microbiol. , vol.43 , pp. 424-428
    • Le Hénaff, M.1    Chollet, A.2    Fontenelle, C.3
  • 35
    • 0030110769 scopus 로고    scopus 로고
    • Purification of Mycoplasma gallisepticum membrane proteins p52, p67 (pMGA), and p77 by high-performance liquid chromatography
    • Jan, G., Brenner, C., and Wróblewski, H. (1996) Purification of Mycoplasma gallisepticum membrane proteins p52, p67 (pMGA), and p77 by high-performance liquid chromatography. Protein Expression Purif. 7, 160-166.
    • (1996) Protein Expression Purif. , vol.7 , pp. 160-166
    • Jan, G.1    Brenner, C.2    Wróblewski, H.3
  • 36
    • 0031664437 scopus 로고    scopus 로고
    • Structure and specific activity of macrophage-stimulating lipopeptides from Mycoplasma hyorhinis
    • Mühlradt, P. F., Kiess, M., Meyer, H., Süssmuth, R., and Jung, G. (1998) Structure and specific activity of macrophage-stimulating lipopeptides from Mycoplasma hyorhinis. Infect. Immun. 66, 4804-4810.
    • (1998) Infect. Immun. , vol.66 , pp. 4804-4810
    • Mühlradt, P.F.1    Kiess, M.2    Meyer, H.3    Süssmuth, R.4    Jung, G.5
  • 37
    • 0030811859 scopus 로고    scopus 로고
    • Comparative analysis of the genomes of the bacteria Mycoplasma pneumoniae and Mycoplasma genitalium
    • Himmelreich, R., Plagens, H., Hillbert, H., Reiner, B., and Herrmann, R. (1997) Comparative analysis of the genomes of the bacteria Mycoplasma pneumoniae and Mycoplasma genitalium. Nucleic Acids Res. 25, 701-712.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 701-712
    • Himmelreich, R.1    Plagens, H.2    Hillbert, H.3    Reiner, B.4    Herrmann, R.5
  • 40


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