Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Research Article
  • Published:

Enhanced metalloadsorption of bacterial cells displaying poly-His peptides

Nature Biotechnology volume 14, pages 1017–1020 (1996)Cite this article

Abstract

The properties of Escherichia coli cells, acquired by cell surface presentation of one or two hexa-histidine (His) clusters carried by the outer membrane LamB protein, have been examined. Strains producing LamB hybrids with the His chains accumulated greater than 11-fold more Cd2+ than E. coli cells expressing the protein without the His insert. Furthermore, the hexa-His chains on the cell surface caused cells to adhere reversibly to a Ni2+-containing solid matrix in a metal-dependent fashion. Thus, expression of poly-His peptides enables bacteria to act as a metalloaffinity adsorbent. These results open up the possibility for biosorption of heavy ions using engineered microorganisms.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Nriagu, J.O. and Pacyna, J.M. 1989. Quantitative assessment of worldwide contamination of air, water and soils by trace metals. Nature 333: 134–139.

    Article  Google Scholar 

  2. Beveridge, T.J. 1989. Metal ions and bacteria, pp. 21–29 in Metal ions and bacteria. Beveridge, T.J. and Doyle, R.J. (eds.). Willey and Sons, New York.

    Google Scholar 

  3. Gadd, G.M. and White, C. 1993. Microbial treatment of metal pollution—a working biotecnology? Trends Biotech. 11: 353–359.

    Article  CAS  Google Scholar 

  4. Ji, G. and Silver, S. 1995. Bacterial resistance mechanisms for heavy metals of environmetal concern. J. Ind. Microbiol. 14: 61–75.

    Article  CAS  PubMed  Google Scholar 

  5. Torma, A.E. 1988. Leaching of metals, pp. 367–399 in Biotechnology vol. 6b: Special microbial processes. Rehm, H.J. (ed.). VCH Weinheim, Germany.

    Google Scholar 

  6. Lovely, D.R., Phillips, E.J.P., Gorby, Y.A. and Landa, E.R. 1991. Microbial reduction of uranium. Nature 350: 413–416.

    Article  Google Scholar 

  7. Butt, T.R. and Ecker, D.J. 1987. Yeast metallothionein and applications in biotechnology. Microbiol. Rev. 51: 351–364.

    CAS  PubMed  PubMed Central  Google Scholar 

  8. Murooka, Y. and Nagaoka, T. 1987. Expression of cloned monkey metallothionein in Escherichia coli . Appl. Environ. Microbiol. 53: 204–207.

    CAS  PubMed  PubMed Central  Google Scholar 

  9. Jacobs, F.A., Romeyer, P.M., Beaucheim, M., and Brousseau, R. 1989. Human metallothionein-II is synthesized as a stable membrane-localized fusion protein in Escherichia coli . Gene 83: 95–103.

    Article  CAS  PubMed  Google Scholar 

  10. Laib, J.E., Shaw, C.F., Petering, D.H., Eidsness, M.K., Elder, R.C. and Garvey, J.S. 1985. Formation and characterization of aurothioneins: Au, Zn, Cd-thionein and (thimalato-Au)-thionein. Biochemistry 24: 1977–1986.

    Article  CAS  PubMed  Google Scholar 

  11. Hutchins, S.R., Davidson, M.S., Brierley, J.A. and Brierly, C.L. 1986. Microorganisms in reclamation of metals. Ann. Rev. Microbiol. 40: 311–336.

    Article  CAS  Google Scholar 

  12. Hofnung, M. 1991. Expression of foreign polypeptides at the Escherichia coli cell surface. Methods Cell Biol. 4: 77–105.

    Article  Google Scholar 

  13. Geourgiou, G., Poetschke, H., Stathopoulos, C. and Francisco, J.A. 1993. Practical applications of engineering Gram-negative bacterial cell surfaces. Trends Biotech. 11: 6–10.

    Article  Google Scholar 

  14. Francisco, J.A., Campbell, R., Iverson, B.L. and 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.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  15. Fuchs, P., Breitling, F., Dübel, S., Seehaus, T. and Little, M. 1991. Targeting recombinant antibodies to the surface of Eschericha coli: Fusion to a peptidoglycan associated lipoprotein. Bio/Technology 9: 1369–1372.

    Article  CAS  Google Scholar 

  16. Little, M., Fuchs, P., Breitling, F. and Dübel, S. 1993. Bacterial surface presentation of proteins and peptides: an alternative to phage technology. Trends Biotech. 11: 3–5.

    Article  CAS  Google Scholar 

  17. Hofnung, M. 1995. An intelligent channel (and more). Science 267: 473–474.

    Article  CAS  PubMed  Google Scholar 

  18. Boulain, J.-C., Charbit, A. and Hofnung, M. 1986. Mutagenesis by random linker insertion into lamB gene of E. coli K-12. Mol. Gen. Genet. 205: 339–348.

    Article  CAS  PubMed  Google Scholar 

  19. Charbit, A., Ronco, J., Michel, V., Werts, C. and Hofnung, M. 1991. Permissive sites and topology of an outer membrane protein with a reporter epitope. J. Bacteriol. 173: 262–275.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  20. Hochuli, E., Döbeli, H. and Schacher, A. 1987. New metal chelate adsorbents selective for proteins and peptide containing neighbouring histidine residues. J. Chromatography 411: 177–184.

    Article  CAS  Google Scholar 

  21. Qiagen Inc. 1992. Qiaexpress, the high level expression and protein purification system. Qiagen Inc., Chatsworth, California.

  22. Kemper, M.A., Urrutia, M.M., Beveridge, T.J., Koch, A.L. and Doyle, R.J. 1993. Proton motive force may regulate cell wall-associated enzymes of Bacillus subtillis . J. Bacteriol. 175: 5690–5696.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  23. Krämer, U., Cotter-Howells, J.D., Charnock, J.M., Bakers, A.J.M. and Smith, J.A. 1996. Free histidine as a metal chelator in plants that accumulate nickel. Nature 379: 635–638.

    Article  Google Scholar 

  24. Brown, S. 1992. Engineered iron oxide-adhesion mutants of the Escherichia coli phage λ receptor. Proc. Natl. Acad. Sci. USA 89: 8651–8655.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  25. Su, G.-F., Brahmbhatt, H., Wehland, J., Rohde, M. and Timmis, K. 1992. Construction of stable LamB-shiga toxin B subunit hybrids: analysis of the expression in Salmonella typhimurium aroA strains and stimulation of B subunit-specific mucosal and serum antibody responses. Infect. Immun. 60: 3345–3359.

    CAS  PubMed  PubMed Central  Google Scholar 

  26. Cebolla, A., Guzmán, C. and de Lorenzo, V. 1996. Nondisruptive detection of activity of catabolic promoters of Pseudomonas putida with an antigenic surface reporter system. Appl. Environ. Microbiol. 62: 214–220.

    CAS  PubMed  PubMed Central  Google Scholar 

  27. Miller, J.H. 1972. pp. 201–205 in Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.

    Google Scholar 

  28. Sambrook, J., Frisch, E.F. and Maniatis, T. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.

    Google Scholar 

  29. Läemmli, U.K. 1970. Cleavage of structural proteins during the assembly of head of the bacteriophage T4. Nature 277: 680–685.

    Article  Google Scholar 

  30. Towbin, H., Staehelin, T. and Gordon, J. 1979. Electrophoretic transfer of proteins from polyacrilamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76: 4350–4354.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  31. Romeyer, F.M., Jacobs, F.A., Masson, L., Hanna, Z., and Brousseau, R. 1988. Bioaccumulation of heavy metals in Escherichia coli expressing an inducible synthetic human metallothionein gene. J. Biotechnol. 8: 207–220.

    Article  CAS  Google Scholar 

  32. Janknecht, R., de Martynoff, G., Lou, J., Hipskind, R.A., Nordheim, A., and Stunnenberg, H.G. 1991. Rapid and efficient purification of native histidine tagged protein expressed by recombinant vaccinia virus. Proc. Natl. Acad. USA 88: 8972–8976.

    Article  CAS  Google Scholar 

Download references

Author information

Author notes

  1. Víctor de Lorenzo: vdlorenzo@samba.cnb.uam,es

Authors and Affiliations

  1. Centra National de Biotecnología-CSIC, Campus de Cantoblanco, Madrid, 28049, Spain

    Carolina Sousa, Angel Cebolla & Víctor de Lorenzo

Authors
  1. Carolina Sousa
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Angel Cebolla
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Víctor de Lorenzo
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Sousa, C., Cebolla, A. & de Lorenzo, V. Enhanced metalloadsorption of bacterial cells displaying poly-His peptides. Nat Biotechnol 14, 1017–1020 (1996). https://doi.org/10.1038/nbt0896-1017

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/nbt0896-1017

This article is cited by

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing