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Volume 271, Number 25, Issue of June 21, 1996 pp. 14717-14721
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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A Cytolytic Function for a Sialic Acid-binding Lectin That Is a Member of the Pentraxin Family of Proteins

(Received for publication, November 22, 1995, and in revised form, March 7, 1996)

Peter B. Armstrong ^§ , Snehasikta Swarnakar ^§ , Subita Srimal ^§ , Sandra Misquith ^§ , Elizabeth A. Hahn , Ronald T. Aimes ^§'' and James P. Quigley ^§

From the  Department of Molecular and Cellular Biology, University of California, Davis, California 95616-8755, the ^§ Marine Biological Laboratory, Woods Hole, Massachusetts 02543, and the Departments of  Pathology and ^'' Biochemistry, School of Medicine, State University of New York, Stony Brook, New York 11794-8691

A variety of invertebrates possess plasma lectins with sialic acid recognition capabilities. One of the best studied of these lectins is limulin, which is a member of the pentraxin family of proteins and is found in the plasma of the American horseshoe crab, Limulus polyphemus. We find that limulin is one of several sialic acid-binding lectins of Limulus plasma and is present at a much lower abundance than Limulus C-reactive protein, the other plasma pentraxin. Limulin was purified by sequential affinity chromatography on phosphorylethanolamine-agarose, which isolates the pentraxins and separates limulin from the other sialic acid-binding lectins of the plasma, followed by fetuin-Sepharose, which binds limulin and separates it from Limulus C-reactive protein, the most abundant pentraxin of the plasma. We show here that limulin is the mediator of the Ca⁺²-dependent hemolytic activity found in the plasma of Limulus. Plasma that was depleted in the pentraxins by passage over phosphorylethanolamine-agarose or was depleted in the sialic acid-binding lectins by passage over fetuin-Sepharose lacked hemolytic activity. Purified limulin was hemolytic at concentrations of 3-5 nM. The other sialic acid-binding lectins of Limulus plasma and Limulus C-reactive protein were nonhemolytic. Foreign cell cytolysis by limulin represents a novel function for a plasma lectin and is the first documented function for limulin.

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