Borrelia burgdorferi are susceptible to killing by a variety of human polymorphonuclear leukocyte components.
Lusitani. Denise D; Malawista. Stephen E SE; Montgomery. Ruth R RR
Key Findings
- Intact neutrophils (PMNL) efficiently kill B. burgdorferi, especially when the bacteria are coated with specific antibodies.
- LL‑37, along with elastase and a few other neutrophil proteins, directly kills B. burgdorferi in vitro.
- Other neutrophil components like lysozyme have limited effect, and some (azurocidin, proteinase 3, lactoferrin) do not kill the spirochete.
Practical Outcomes
- LL‑37 shows promise as an anti‑Lyme agent in the lab, but there’s no dosage, delivery method, or safety data for human use yet. For now, it’s a piece of basic science that may guide future drug development rather than a ready‑to‑apply protocol for biohackers.
Summary
The study shows that the human antimicrobial peptide LL‑37 can kill the Lyme disease bacteria Borrelia burgdorferi in lab tests, but it’s just an early‑stage finding and doesn’t tell you how to use it in people.
Abstract
The killing of Borrelia burgdorferi by intact human polymorphonuclear leukocytes (PMNL) and by individual PMNL components was compared. Intact PMNL killed B. burgdorferi 6.5-fold more efficiently and 5-fold more completely when spirochetes were opsonized with specific antibodies. U-cytoplasts, which have activatable oxidase, killed opsonized B. burgdorferi with an efficiency similar to that of intact PMNL in killing unopsonized B. burgdorferi. Although B. burgdorferi were susceptible to H(2)O(2) and nitric oxide, PMNL lysates killed B. burgdorferi nearly as well as intact PMNL killed opsonized B. burgdorferi, suggesting a critical role for granule contents. B. burgdorferi were killed by the PMNL antimicrobial components elastase, LL-37, bactericidal/permeability-increasing protein, and human neutrophil peptide-1. B. burgdorferi had limited susceptibility to killing by lysozyme and were not killed by azurocidin, proteinase 3, or lactoferrin. The efficient killing of B. burgdorferi by a variety of PMNL mechanisms highlights the paradoxical persistence of spirochetes in vivo.
Study Information
pubmed
2002
2002-02-20T00:00:00.000Z
10.1086/339341
71
48