Properdin: New roles in pattern recognition and target clearance

Claudia Kemper, Dennis E. Hourcade*

*Corresponding author for this work
74 Citations (Scopus)


Properdinwas first described over 50 years ago by Louis Pillemer and his collaborators as a vitalcomponent of an antibody-independent complement activation pathway. In the 1970s properdin was shown to be a stabilizing component of the alternative pathway convertases, the central enzymes of the complement cascade. Recently we have reported that properdin can also bind to target cells and microbes, provide a platform for convertase assembly and function, and promote target phagocytosis. Evidence is emerging that suggests that properdin interacts with a network of target ligands, phagocyte receptors, and serum regulators. Here we review the new findings and their possible implications.

Original languageEnglish
JournalMolecular Immunology
Issue number16
Pages (from-to)4048-4056
Number of pages9
Publication statusPublished - 10.2008

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


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