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Protein Engineering, Vol. 14, No. 10, 769-774, October 2001
© 2001 Oxford University Press

Binding of external ligands onto an engineered virus capsid

Uli Schmidt1,3,4, Rainer Rudolph1 and Gerald Böhm1,2

1 Institut für Biotechnologie, Martin-Luther-Universität Halle-Wittenberg, Kurt-Mothes-Str. 3, 06120 Halle and 2 ACGT Progenomics AG, Weinbergweg 22, 06120 Halle, Saale, Germany

The development of novel delivery systems for therapeutic substances includes targeting of the carriers to a specific site or tissue within the body of the recipient. This can be accomplished by appropriate receptor-binding domains and requires linking of these domains to the carrier. We have used recombinantly expressed polyomavirus-like particles as a model system and inserted the sequence of a WW domain into different surface loops of the viral capsid protein VP1. In one variant, the WW domain maintained its highly selective binding properties of proline-rich ligands and showed an increased affinity but also an accelerated association/dissociation equilibrium compared to the isolated WW domain, thus allowing a short-term coupling of external ligands onto the surface of the virus-like particles.


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