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Applied and Environmental Microbiology, January 2006, p. 465-471, Vol. 72, No. 1
0099-2240/06/$08.00+0     doi:10.1128/AEM.72.1.465-471.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Efficient and Stable Display of Functional Proteins on Bacterial Magnetic Particles Using Mms13 as a Novel Anchor Molecule

Tomoko Yoshino1,2 and Tadashi Matsunaga1*

Department of Biotechnology, Tokyo University of Agriculture and Technology, 2-24-16, Naka-cho, Koganei, Tokyo 184-8588, Japan,1 Consolidated Research Institute for Advanced Science and Medical Care, Waseda University, 513 Wasedatsurumaki-cho, Shinjuku-ku, Tokyo 162-0041, Japan2

Received 21 June 2005/ Accepted 18 October 2005

Magnetic particles are increasingly used for various biomedical applications because they are easy to handle and separate from biological samples. In this work, a novel anchor molecule was used for targeted protein display onto magnetic nanoparticles. The magnetic bacterium Magnetospirillum magneticum AMB-1 synthesizes intracellular bacterial magnetic particles (BMPs) covered with a lipid bilayer membrane. In our recent research, an integral BMP membrane protein, Mms13, was isolated and used as an anchor molecule to display functional proteins onto BMPs. The anchoring properties of Mms13 were confirmed by luciferase fusion studies. The C terminus of Mms13 was shown to be expressed on the surface of BMPs, and Mms13 was bound to magnetite directly and tightly permitting stable localization of a large protein, luciferase (61 kDa), on BMPs. Consequently, luminescence intensity obtained from BMPs using Mms13 as an anchor molecule was >400 or 1,000 times higher than Mms16 or MagA, which previously were used as anchor molecules. Furthermore, the immunoglobulin G-binding domain of protein A (ZZ) was displayed uniformly on BMPs using Mms13, and antigen was detected by transmission electron microscopy using antibody-labeled gold nanoparticles on a single BMP displaying the ZZ-antibody complex. The results of this study demonstrated the utility of Mms13 as a molecular anchor, which will facilitate the assembly of other functional proteins onto BMPs in the near feature.

* Corresponding author. Mailing address: Department of Biotechnology, Tokyo University of Agriculture and Technology, 2-24-16, Naka-cho, Koganei, Tokyo 184-8588, Japan. Phone: 81-42-388-7020. Fax: 81-42-385-7713. E-mail: tmatsuna{at}cc.tuat.ac.jp

Applied and Environmental Microbiology, January 2006, p. 465-471, Vol. 72, No. 1
0099-2240/06/$08.00+0     doi:10.1128/AEM.72.1.465-471.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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