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C3 Binding Proteins of Foreign Origin

  • Conference paper
The Third Component of Complement

Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 153))

Abstract

The generation of C3b from C3 releases the internal thioester and allows C3 to bind covalently to OH and NH2 groups, using the carbonyl group and leaving the SH group unoccupied. The molecules to which C3b binds in this way are commonly referred to as C3 acceptors and range from H2O to large fluid-phase and membrane molecules. C3b and its derivatives—iC3b, C3d,g, and C3d, covalently bound to C3 acceptors—have the potential to interact noncovalently with a number of fluid-phase and membrane-associated molecules (LAMBRIS 1988). Such molecules on pathogens are the subject of this chapter, particularly whether the presence of such C3 binding molecules constitute advantages for the pathogen in coping with the control mechanisms of the host, i.e., whether they can be considered as pathogenicity factors.

The authors’ own work cited in this study was supported by grants from the FWF (P6920 and P6923).

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  1. Institut für Hygiene, University of Innsbruck, Fritz-Pregl-Straβe 3, A-6010, Innsbruck, Austria

    M. P. Dierich, H. P. Huemer & W. M. Prodinger

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  1. M. P. Dierich
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  2. H. P. Huemer
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  3. W. M. Prodinger
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  1. Basel Institute for Immunology, Grenzacherstr. 487, CH-4005, Basel, Switzerland

    John D. Lambris Ph. D.

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Dierich, M.P., Huemer, H.P., Prodinger, W.M. (1990). C3 Binding Proteins of Foreign Origin. In: Lambris, J.D. (eds) The Third Component of Complement. Current Topics in Microbiology and Immunology, vol 153. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-74977-3_9

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  • DOI: https://doi.org/10.1007/978-3-642-74977-3_9

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