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The Journal of Immunology, 2004, 173: 5540-5545.
Copyright © 2004 by The American Association of Immunologists

Complement Inactivation by Recombinant Human C3 Derivatives

Johanna Kölln1, Edzard Spillner1, Jörg Andrä2, Katrin Klensang and Reinhard Bredehorst3

Institut für Biochemie und Lebensmittelchemie, Abteilung für Biochemie, und Molekularbiologie, Universität Hamburg, Hamburg, Germany

From the implications of the complement system in a large number of diseases, an urgent need for therapeutics effecting reduced complement activity in vivo has emerged. In this study we report the design of a novel class of enzymes of human origin that obliterate functional complement by a noninhibitory, catalytic mechanism. Combining the framework of human C3 and the enzymatic mechanism of cobra venom factor, a nontoxic snake venom protein, we established molecules capable of forming stable C3 convertase complexes. Although the half-life of naturally occurring C3 convertase complexes ranges between 1 and 2 min, these complexes exhibit a half-life of up to several hours. Because the overall identity to human C3 could be extended to >90%, the novel C3 derivatives can be assumed to exhibit low immunogenicity and, therefore, represent promising candidates for therapeutic reduction of complement activity in vivo.




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E. Torreira, A. Tortajada, T. Montes, S. R. de Cordoba, and O. Llorca
3D structure of the C3bB complex provides insights into the activation and regulation of the complement alternative pathway convertase
PNAS, January 20, 2009; 106(3): 882 - 887.
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