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Infection and Immunity, April 2006, p. 2468-2472, Vol. 74, No. 4
0019-9567/06/$08.00+0     doi:10.1128/IAI.74.4.2468-2472.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Human Neutrophil Calprotectin Reduces the Susceptibility of Borrelia burgdorferi to Penicillin

Ruth R. Montgomery,* Kimberly Schreck, Xiaomei Wang, and Stephen E. Malawista

Department of Internal Medicine, Yale University School of Medicine, New Haven, Connecticut 06510

Received 23 December 2005/ Returned for modification 18 January 2006/ Accepted 31 January 2006

Borrelia burgdorferi, the spirochetal agent of Lyme disease, is susceptible to killing by a variety of polymorphonuclear leukocyte (PMN) components. Some are most effective against metabolically active B. burgdorferi. The abundant PMN cytoplasmic protein calprotectin, elevated 10- to 100-fold in inflammation, inhibits the growth of spirochetes through chelation of the essential cation, Zn. Since the action of some therapeutic antibiotics depends on bacterial division, we investigated the antibiotic sensitivities of spirochetes in calprotectin. In physiologic calprotectin, B. burgdorferi is not eliminated by therapeutic doses of penicillin G; in contrast, doxycycline is effective. Calprotectin may modify the clearance of spirochetes at sites of inflammation.

* Corresponding author. Mailing address: Department of Internal Medicine, Yale University School of Medicine, 300 Cedar Street/TAC S413, New Haven, CT 06520-8031. Phone: (203) 785-7039. Fax: (203) 785-7053. E-mail: ruth.montgomery{at}yale.edu.

Editor: J. B. Bliska

Infection and Immunity, April 2006, p. 2468-2472, Vol. 74, No. 4
0019-9567/06/$08.00+0     doi:10.1128/IAI.74.4.2468-2472.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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  • Cornell, K. A., Primus, S., Martinez, J. A., Parveen, N. (2009). Assessment of methylthioadenosine/S-adenosylhomocysteine nucleosidases of Borrelia burgdorferi as targets for novel antimicrobials using a novel high-throughput method. J Antimicrob Chemother 63: 1163-1172 [Abstract] [Full Text]  
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