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Infection and Immunity, August 2003, p. 4711-4716, Vol. 71, No. 8
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.8.4711-4716.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Calprotectin, an Abundant Cytosolic Protein from Human Polymorphonuclear Leukocytes, Inhibits the Growth of Borrelia burgdorferi

Department of Internal Medicine, Yale University School of Medicine, New Haven, Connecticut 06520

Received 9 April 2003/ Returned for modification 1 May 2003/ Accepted 15 May 2003

We previously showed that numerous polymorphonuclear leukocyte (PMN) granule components efficiently kill Borrelia burgdorferi, the agent of Lyme disease. In addition, motile, granule-poor cytoplasts (U-Cyt) from human blood PMN can exert anti-Borrelia activity against opsonized B. burgdorferi independently of oxidative mechanisms. Here we show that lysates of U-Cyt also possess anti-Borrelia activity, a portion of which comes from the abundant cytosolic protein calprotectin. The anti-Borrelia activity of U-Cyt lysates and recombinant calprotectin was partially or completely reversed by specific antibody to calprotectin and by Zn²⁺, a cation essential for the growth of B. burgdorferi and known to inhibit the antimicrobial activity of calprotectin. Quantitative microscopic and regrowth assays revealed that calprotectin acted in a bacteriostatic fashion against B. burgdorferi. We conclude that calprotectin, a potent bacteriostatic agent from a cell primarily recognized for its oxidative and granular antibacterial mechanisms, may play a modulatory role in infection by the Lyme spirochete, particularly at sites of acute inflammation.

Editor: W. A. Petri, Jr.

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