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J. Biol. Chem., Vol. 277, Issue 10, 8545-8550, March 8, 2002

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Cloning and Characterization of Scavidin, a Fusion Protein for the Targeted Delivery of Biotinylated Molecules^*

Pauliina Lehtolainen, Anna Taskinen, Johanna Laukkanen, Kari J. Airenne, Sanna Heino^§, Maarit Lappalainen, Kirsi Ojala^§, Varpu Marjomäki^§, John F. Martin^¶, Markku S. Kulomaa^§, and Seppo Ylä-Herttuala^**

From the  A. I. Virtanen Institute, University of Kuopio, FIN-70211 Kuopio, Finland, the  Department of Medicine, University of Kuopio, and the Gene Therapy Unit, Kuopio University Hospital, Kuopio FIN-70210, Finland, the ^§ Department of Biological and Environmental Science, University of Jyväskylä, Jyväskylä FIN-40351, Finland, and the ^¶ Department of Medicine, University College London, London WC1E 6JJ, United Kingdom

We have constructed a novel fusion protein "Scavidin" consisting of the macrophage scavenger receptor class A and avidin. The Scavidin fusion protein is transported to plasma membranes where the avidin portion of the fusion protein binds biotin with high affinity and forms the basis for the targeted delivery of biotinylated molecules. Subcellular fractionation analysis, immunostaining, and electron microscopy demonstrated endosomal localization of the fusion protein. According to pulse-labeling and cross-linking studies Scavidin is found as monomers (55 kDa), dimers, and multimers, of which the 220-kDa form was the most abundant. The biotin binding capacity and active endocytosis of the biotinylated ligands were demonstrated in rat malignant glioma. Local Scavidin gene transfer to target tissues could have general utility as a universal tool to deliver biotinylated molecules at systemic low concentrations for therapeutic and imaging purposes, whereby high local concentration is achieved.

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