A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Borrelia burgdorferi inhibits human neutrophil functions
Tekijät: Hartiala P, Hytonen J, Suhonen J, Lepparanta O, Tuominen-Gustafsson H, Vijanen MK
Kustantaja: ELSEVIER SCIENCE BV
Julkaisuvuosi: 2008
Journal: Microbes and Infection
Tietokannassa oleva lehden nimi: MICROBES AND INFECTION
Lehden akronyymi: MICROBES INFECT
Vuosikerta: 10
Numero: 1
Aloitussivu: 60
Lopetussivu: 68
Sivujen määrä: 9
ISSN: 1286-4579
DOI: https://doi.org/10.1016/j.micinf.2007.10.004
Tiivistelmä
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. burgdorferi, human neutrophils and the complement system. We found that (1) OspB inhibits the phagocytosis and oxidative burst of human neutrophils at low serum concentrations, whereas OspA induces the oxidative burst in neutrophils; (2) OspB may have an inhibiting role in serum sensitivity and complement activation; (3) all studied strains inhibit the chemotaxis of human neutrophils specifically towards fMLP but not towards C5a, regardless of their Osp expression. These results suggest that although OspA and OspB are co-ordinately transcribed, they differ in their effects on human neutrophil functions. Our findings suggest that B. burgdorferi exploits a wide variety of immune evasion mechanisms, besides previously documented complement resistance, to survive in the vertebrate host. (c) 2007 Elsevier Masson SAS. All fights reserved.
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. burgdorferi, human neutrophils and the complement system. We found that (1) OspB inhibits the phagocytosis and oxidative burst of human neutrophils at low serum concentrations, whereas OspA induces the oxidative burst in neutrophils; (2) OspB may have an inhibiting role in serum sensitivity and complement activation; (3) all studied strains inhibit the chemotaxis of human neutrophils specifically towards fMLP but not towards C5a, regardless of their Osp expression. These results suggest that although OspA and OspB are co-ordinately transcribed, they differ in their effects on human neutrophil functions. Our findings suggest that B. burgdorferi exploits a wide variety of immune evasion mechanisms, besides previously documented complement resistance, to survive in the vertebrate host. (c) 2007 Elsevier Masson SAS. All fights reserved.
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