Borrelia burgdorferi inhibits human neutrophil functions.

Outer surface proteins OspA and OspB are among the most prominent Borrelia burgdorferi surface molecules. We constructed OspAB and OspA complementation mutants of B. burgdorferi Osp-less strain B313 and investigated the role of these surface proteins in the interactions of B.

Use of CFSE staining of borreliae in studies on the interaction between borreliae and human neutrophils.

Background: Species of the tick-transmitted spirochete group Borrelia burgdorferi sensu lato (B. burgdorferi) cause Lyme borreliosis. Acute borrelial infection of the skin has unusual characteristics with only a mild local inflammatory response suggesting that the interaction between borreliae and the cells of the first-line defence might differ from that of other bacteria.

Sublethal concentrations of complement can effectively opsonize Borrelia burgdorferi.

The fate of borreliae invading a human may depend on the early innate response they induce. The interactions of human complement system and neutrophils with two strains of the Lyme borreliosis spirochete Borrelia burgdorferi were studied. Borrelia burgdorferi sensu stricto B31 (resistant to a 28% concentration of normal human serum (NHS)) and Borrelia garinii Bg A218/98 (sensitive to 7% NHS) were examined.

Borrelia burgdorferi--induced oxidative burst, calcium mobilization, and phagocytosis of human neutrophils are complement dependent.

When Borrelia burgdorferi, the spirochete causing Lyme disease, is transmitted to a human, the complement system is among the first challenges facing the bacterium. Neutrophils are crucial leukocytes in the first line of host defense against bacterial infections. To investigate the role of complement in the Borrelia-induced activation of human neutrophils, oxidative burst, calcium mobilization, and phagocytosis induced by three subspecies of B.