Abstract

Virus particles are probably the most precisely defined nanometre-sized objects that can be formed by protein self-assembly. Although their natural function is the storage and transport of genetic material, they have more recently been applied as scaffolds for mineralization and as containers for the encapsulation of inorganic compounds1,2. The reproductive power of viruses has been used to develop versatile analytical methods, such as phage display, for the selection and identification of (bio)active compounds3. To date, the combined use of self-assembly and reproduction has not been used for the construction of catalytic systems. Here we describe a self-assembled system based on a plant virus that has its coat protein genetically modified to provide it with a lipase enzyme. Using single-object and bulk catalytic studies, we prove that the virus-anchored lipase molecules are catalytically active. This anchored biocatalyst, unlike man-made supported catalysts, has the capability to reproduce itself in vivo, generating many independent catalytically active copies.

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Acknowledgements

The authors acknowledge the financial support provided through the European Community's Human Potential Programme under contract HPRN-CT-2001-00188 (SMASHYBIO). R.N. acknowledges financial support from the Royal Netherlands Academy of Sciences. We thank S. Chapman (Scottish Crop Research Institute, Invergowrie, Dundee, UK) for providing us with the pTXS.GFP-CP vector. We are indebted to H. Rogniaux for mass spectroscopy analysis.

Author information

Affiliations

  1. Interactions Plante Virus, UMR GDPP, IBVM, INRA, BP 81, F-33883, Villenave d'Ornon, France

    • Noëlle Carette
    •  & Thierry Michon
  2. Institute for Molecules and Materials, Radboud University Nijmegen, PO Box 9010, 6500 GL, Nijmegen, The Netherlands

    • Hans Engelkamp
    • , Eric Akpa
    • , Peter C. M. Christianen
    • , Jan C. Maan
    • , Alan E. Rowan
    • , Roeland J. M. Nolte
    •  & Jan C. M. Van Hest
  3. DSM Research, PO Box 18, 6160 MD, Geleen, The Netherlands

    • Sebastien J. Pierre
    •  & Jens C. Thies
  4. University of Durham, Department of Chemistry, South Road, Durham DH1 3LE, UK

    • Neil R. Cameron
  5. Technische Universität München, Chemie Department, Lehrstuhl für Makromolekulare Stoffe, Lichtenbergstrasse 4, 85747 Garching, Germany

    • Ralf Weberskirch

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Contributions

T.M., J.H., N.R.C., J.T., and R.W. conceived and designed the experiments. N.C., H.E., E.A. and S.P. performed the experiments. N.C., H.E., P.C., R.N., T.M., and J.K. analysed the data. P.C., J.M., and A.R., contributed analysis tools. N.C., H.E., R.M., T.M., and J.K., co-wrote the paper. All authors discussed the results and commented on the manuscript.

Competing interests

The authors declare no competing financial interests.

Corresponding authors

Correspondence to Thierry Michon or Jan C. M. Van Hest.

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    Supplementary Information

    Supplementary figures S1—S3 and Table S1

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DOI

https://doi.org/10.1038/nnano.2007.76

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