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Infection and Immunity, April 2000, p. 1753-1759, Vol. 68, No. 4
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Serum Amyloid P Component Bound to Gram-Negative Bacteria Prevents Lipopolysaccharide-Mediated Classical Pathway Complement Activation

Carla J. C. de Haas,* Ester M. M. van Leeuwen, Toon van Bommel, Jan Verhoef, Kok P. M. van Kessel, and Jos A. G. van Strijp

Department of Inflammation, Eijkman Winkler Institute, University Medical Center, 3584 CX Utrecht, The Netherlands

Received 3 May 1999/Returned for modification 1 September 1999/Accepted 12 January 2000

Although serum amyloid P component (SAP) is known to bind many ligands, its biological function is not yet clear. Recently, it was demonstrated that SAP binds to lipopolysaccharide (LPS). In the present study, SAP was shown to bind to gram-negative bacteria expressing short types of LPS or lipo-oligosaccharide (LOS), such as Salmonella enterica serovar Copenhagen Re and Escherichia coli J5, and also to clinical isolates of Haemophilus influenzae. It was hypothesized that SAP binds to the bacteria via the lipid A part of LPS or LOS, since the htrB mutant of the nontypeable H. influenzae strain NTHi 2019-B29-3, which expresses a nonacetylated lipid A, did not bind SAP. This was in contrast to the parental strain NTHi 2019. The binding of SAP resulted in a clear inhibition of the deposition of complement component C3 on the bacteria. SAP inhibited only the activation of the classical complement pathway; the alternative route remained unaffected. In the classical route, SAP prevented the deposition of the first complement component, Clq, probably by interfering with the binding of Clq to LPS. Since antibody-mediated Clq activation was not inhibited by SAP, SAP seems to inhibit only the LPS-induced classical complement pathway activation. The SAP-induced inhibition of C3 deposition strongly diminished the complement-mediated lysis as well as the phagocytosis of the bacteria. The binding of SAP to gram-negative bacteria, therefore, might influence the pathophysiology of an infection with such bacteria.

* Corresponding author. Mailing address: Eijkman Winkler Institute, Dept. of Inflammation, G04.614, University Medical Center, Heidelberglaan 100, 3584 CX Utrecht, The Netherlands. Phone: (31) 30-2507627. Fax: (31) 30-2541770. E-mail: c.j.c.dehaas{at}lab.azu.nl.

Infection and Immunity, April 2000, p. 1753-1759, Vol. 68, No. 4
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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