Borrelia burgdorferi are susceptible to killing by a variety of human polymorphonuclear leukocyte components

J Infect Dis. 2002 Mar 15;185(6):797-804. doi: 10.1086/339341. Epub 2002 Feb 20.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antimicrobial Cationic Peptides / physiology
  • Blood Bactericidal Activity*
  • Blood Proteins / physiology
  • Borrelia burgdorferi / immunology*
  • Carrier Proteins / physiology
  • Cathelicidins
  • Humans
  • Lactoferrin / physiology
  • Leukocyte Elastase / physiology
  • Membrane Proteins*
  • Muramidase / physiology
  • Myeloblastin
  • Neutrophils / immunology*
  • Nitric Oxide / physiology
  • Serine Endopeptidases / physiology
  • alpha-Defensins / physiology

Substances

  • Antimicrobial Cationic Peptides
  • Blood Proteins
  • Carrier Proteins
  • Cathelicidins
  • Membrane Proteins
  • alpha-Defensins
  • bactericidal permeability increasing protein
  • cationic antimicrobial protein CAP 37, human
  • human neutrophil peptide 1
  • CAP18 lipopolysaccharide-binding protein
  • Nitric Oxide
  • Muramidase
  • Lactoferrin
  • Serine Endopeptidases
  • Leukocyte Elastase
  • Myeloblastin