NDLI: The Role of Properdin in Zymosan- and Escherichia coli-Induced Complement Activation

Content Provider	PubMed Central
Author	Harboe, Morten Garred, Peter Lindstad, Julie K. Pharo, Anne Müller, Fredrik Stahl, Gregory L. Lambris, John D. Mollnes, Tom Eirik
Abstract	Properdin is well-known as enhancer of the alternative complement amplification loop when C3 is activated, whereas its role as recognition molecule of exogenous pathogen-associated molecular patterns and initiator of complement activation is less understood. We therefore studied the role of properdin in activation of complement in normal human serum (NHS) by zymosan and various Escherichia coli strains. In ELISA, microtiter plates coated with zymosan induced efficient complement activation with deposition of C4b and TCC on the solid phase. Virtually no deposition of C4b or TCC was observed with MBL deficient serum. Reconstitution with purified MBL showed distinct activation in both readouts. In ELISA, NHS-induced deposition of properdin by zymosan was abolished by the C3 inhibiting peptide compstatin. Flow cytometry was used to further explore whether properdin acts as initial recognition molecule reacting directly with zymosan and three E. coli strains. Experiments reported by other authors were made with EGTA Mg++ buffer permitting auto-activation of C3. We found inhibition by compstatin on these substrates indicating that properdin deposition depended on initial C3b deposition followed by properdin in a second step. Properdin released from human polymorphonuclear cells (PMN) stimulated with phorbol-myristate acetate did not bind to zymosan or E. coli, but when incubated in properdin-depleded serum this form of properdin bound efficiently to both substrates in a strictly C3-dependent manner, since the binding was abolished by compstatin. Collectively, these data indicate that properdin in serum as well as PMN-released properdin is unable to bind and initiate direct alternative pathway activation on these substrates.
Related Links	http://dx.doi.org/10.4049/jimmunol.1200269
Ending Page	2613
Page Count	8
Starting Page	2606
File Format	PDF
ISSN	00221767
e-ISSN	15506606
Journal	Journal of immunology (Baltimore, Md. : 1950)
Issue Number	5
Volume Number	189
Language	English
Publisher Date	2012-09-01
Access Restriction	Open
Subject Keyword	Medicine(all) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology

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