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Volumn 9, Issue 5, 1998, Pages 506-509

Use of cell wall-less bacteria (L-forms) for efficient expression and secretion of heterologous gene products

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; PROTEINASE; RECOMBINANT PROTEIN;

EID: 0032190666     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(98)80037-2     Document Type: Article
Times cited : (33)

References (19)
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    • Germany: University of Halle-Wittenberg. [Title translation: Characterisation of the membrane lipids from the stable protoplast type L-form and N-form of Escherichia coli, Proteus miribalis and Streptomyces hygroscopicus.]
    • Gura K. Charakterisierung der Membranlipide aus stabilen Protoplastentyp L-Formen und N-Formen von Escherichia coli, Proteus mirabilis und Streptomyces hygroscopicus. PhD Thesis. 1998;University of Halle-Wittenberg, Germany. [Title translation: Characterisation of the membrane lipids from the stable protoplast type L-form and N-form of Escherichia coli, Proteus miribalis and Streptomyces hygroscopicus.].
    • (1998) PhD Thesis
    • Gura, K.1
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    • Lipid and fatty acid composition of cytoplasmic membranes from Streptomyces hygroscopicus and its stable protoplast type L-form
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  • 9
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    • Complete secretion of activable bovine prochymosin by genetically engineered L-forms of Proteus mirabilis
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  • 10
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    • Novel shuttle vectors for improved streptokinase expression in streptococci and bacterial L-forms
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  • 11
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    • Heterologous signal peptide processing in fusion interferon synthesis by engineered L-forms of Proteus mirabilis
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  • 12
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    • Synthesis and secretion of recombinant penicillin G acylase in bacterial L-forms
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  • 13
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    • Expression and secretion of functional miniantibodies McPC603scFvDhlx in cell wall-less L-form strains of Proteus mirabilis and Escherichia coli: A comparison of the synthesis capacities of L-form strains with an E. coli producer strain
    • of outstanding interest. The results show that L-form cells of P. mirabilis have a similar high-synthesis capacity for a miniantibody protein as the producer strain E. coli RV308 and that the portion of the active antibody can be improved by lowering the growth temperature and by special supplements. They demonstrate further that a periplasmic compartment is not a prerequisite for the correct folding and modification of the miniantibody molecules.
    • Kujau M, Hoischen C, Riesenberg D, Gumpert J. Expression and secretion of functional miniantibodies McPC603scFvDhlx in cell wall-less L-form strains of Proteus mirabilis and Escherichia coli: a comparison of the synthesis capacities of L-form strains with an E. coli producer strain. of outstanding interest Appl Microbiol Biotechnol. 49:1998;51-58 The results show that L-form cells of P. mirabilis have a similar high-synthesis capacity for a miniantibody protein as the producer strain E. coli RV308 and that the portion of the active antibody can be improved by lowering the growth temperature and by special supplements. They demonstrate further that a periplasmic compartment is not a prerequisite for the correct folding and modification of the miniantibody molecules.
    • (1998) Appl Microbiol Biotechnol , vol.49 , pp. 51-58
    • Kujau, M.1    Hoischen, C.2    Riesenberg, D.3    Gumpert, J.4
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    • Sieben S. Die stabilen Protoplasten-Typ L-Formen von Proteus mirabilis als neues Expressionssystem für sekretorische proteine und integrale Membranproteine. PhD Thesis. 1998;University of Jena, Germany. [Title translation: Stable protoplast-type L-forms of Proteus mirabilis represent a new expression system for secretory and integral membrane proteins.].
    • (1998) PhD Thesis
    • Sieben, S.1
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