Abstract
Using the Escherichia coli OmpC protein as an anchoring motif, four different poly-His units (1, 2, 3 and 6 copies of 6-His) were displayed on the seventh loop of the OmpC. Recombinant E. coli strains displaying 1, 3 or 6 copies of poly-His became much more sensitive to SDS (0.1%, w/v) and EDTA (2 mM) compared with control strains. However, recombinant E. coli cells displaying 2 copies of poly-His were resistant to SDS and EDTA; greater than 70% and 90% of cells maintained cell integrity after 60 min treatment with SDS and EDTA, respectively, suggesting its usefulness as a whole cell biosorbent.
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References
Boder ET, Wittrup KD (1997) Yeast surface display for screening combinatorial polypeptide libraries. Nature Biotechnol. 15: 553–557.
Charbit A, Molla A, Saurin W, Hofnung M (1988) Versatility of a vector for expressing foreign polypeptides at the surface of Gram-negative bacteria. Gene 70: 181–189.
Francisco JA, Campbell R, Iverson BL, Georgiou G (1993) Production and fluorescence-activated cell sorting of Escherichia coli expressing a functional antibody fragment on the external surface. Proc. Natl. Acad. Sci. USA 90: 10444–10448.
Georgiou G, Shuler ML, Wilson DB (1988) Release of periplasmic enzymes and other physiological effects of β-lactamase overproduction in Escherichia coli. Biotechnol. Bioeng. 32: 741–748.
Liljeqvist S, Samuelson P, Hansson M, Nguyen TN, Binz H, Stahl S (1997) Surface display of the cholera toxin B subunit on Staphylococcus xylosus and Staphylococcus carnosus. Appl. Environ. Microbiol. 63: 2481–2488.
Martineau P, Charbit A, Leclerc C, Werts C, O'Callaghan D, Hofnung M (1991) A genetic system to elicit and monitor antipeptide antibodies without peptide synthesis. Bio/Technology 9: 170–172.
Murai T, Ueda TM, Kawaguchi T, Arai M, Tanaka A (1998) Assimilation of cellooligosaccharides by a cell surface-engineered yeast expressing β-glucosidase and carboxymethylcellulase from Aspergillus aculeatus. Appl. Environ. Microbiol. 64: 4857–4861.
Nguyen TN, Hansson M, Stahl S, Bachi T, Robert A, Domzig W, Binz H, Uhlen M (1993) Cell-surface display of heterologous epitopes on Staphylococcus xylosus as a potential delivery system for oral vaccination. Gene 128: 89–94.
Nikaido H (1996) Outer membrane. In: Neidhardt FC, ed., Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd edn. Washington, D.C.: American Society for Microbiology, pp. 29–47.
Richins RD, Kaneva I, Mulchandani A, Chen W (1997) Biodegradation of organophosphorus pesticides by surface-expressed organophosphorus hydrolase. Nature Biotechnol. 15: 984–987.
Sousa C, Cebolla A, de Lorenzo V (1996) Enhanced metalloadsorption of bacterial cells displaying poly-His peptides. Nature Biotechnol. 14: 1017–1020.
Sousa C, Kotrba P, Ruml T, Cebolla A, de Lorenzo V (1998) Metalloadsorption by Escherichia coli cells displaying yeast and mammalian metallothioneins anchored to the outer membrane protein LamB. J. Bacteriol. 180: 2280–2284.
Xu Z, Lee SY (1999) Display of poly-His peptides on Escherichia coli cell surface using outer membrane protein C (OmpC) as an anchoring motif. Appl. Environ. Microbiol., in press.
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Xu, Z., Lee, S.Y. & Yu, Z. Physiological characteristics of recombinant Escherichia coli cells displaying poly-His peptides. Biotechnology Letters 21, 1091–1094 (1999). https://doi.org/10.1023/A:1005618025127
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DOI: https://doi.org/10.1023/A:1005618025127