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hgewurz@rush.edu

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My laboratory has had a longstanding interest in innate (nonspecific) immunity, inflammation, and the acute phase response. The structure and function of the acute phase pentraxin, C-reactive protein (CRP), particularly in its ability to activate the complement system at the level of the first component (C1q), has been explored in detail, and continues to be an area of interest. Our recent studies have focused on another molecule that acts as an innate activator of the complement system, mannose binding lectin (MBL). This acute phase protein, acting in concert with two associated serine proteases, activates complement at the level of C4 and C2 following its calcium-dependent binding to surfaces containing exposed mannose residues. Our investigations have shown that an intact alternative complement pathway, as well as C4 and C2 of the classical pathway are necessary for MBL-mediated hemolysis of a mannan sensitized target. We are now exploring the possibility that one acute phase protein (CRP) might modulate the ability of another (MBL) to activate complement.

Selected Publications:
Suankratay, C., Zhang, X.-H., Zhang, Y., Lint, T.F., and Gewurz, H. (1998). Requirement of the alternative pathway as well as C4 and C2 for complement-dependent hemolysis via the lectin pathway. J. Immunol., 160: In press.

Gewurz, H., Zhang, X. H., and Lint, T. F. (1995). Structure and function of the pentraxins. Curr Opinion Immunol., 7:54-64.

Ying, S.C., Gewurz, A.T., Jiang, H., and Gewurz, H. (1993). Human serum amyloid P component oligomers bind and activate the classical complement pathway via residues 14-26 and 76-92 of the A chain collagen-like region of C1q. J. Immunol. 150:169-176.

Gewurz, H., Ying, S.C., Jiang, H., and Lint, T.F. (1993). Nonimmune activation of the classical complement pathway. Behring Inst Mitt 93:138-147.

Jiang, H., Cooper, B., Robey, F.A., and Gewurz, H. (1992). DNA binds and activates complement via residues 14-26 of the human C1q A chain. J. Biol. Chem. 267:25597-25601.