Role of the complement-lectin pathway in anaphylactoid reaction induced with lipopolysaccharide in mice.
We show that Proteus vulgaris O25 (PO25) lipopolysaccharide (LPS) induced an anaphylactoid reaction not only in wild-type and in lipid A non-responding mice but also in recombinase-activating gene-2-deficient (RAG-2(-/-)) and in mast cell-deficient (W/Wv) animals. Western blot analysis indicated that PO25 LPS bound to Ra-reactive factor (RaRF), the complex of mannan-binding lectins (MBL) and MBL-associated serine proteases. Binding of RaRF to PO25 LPS led to the activation of C4 component without participation of either C1 or Ig, via the lectin pathway. Relative concentration of RaRF and hemolytic activity in mouse serum decreased rapidly during the process of anaphylactoid reaction. A significant drop of MBL-A, but not MBL-C level was observed. Administrationwith antiserum to RaRF prevented animals from death as a consequence of the inhibition of interaction of RaRF with the carbohydrate target and complement activation. These results indicate that complement-lectin pathway activation is responsible for the anaphylactoid reaction induced with LPS in muramyldipeptide-primed mice. RaRF also activated fibrinogen in vitro suggesting the involvement of the coagulation system in the process investigated.
D000707:Anaphylaxis / Q000209:etiology*; D000818:Animals; D003167:Complement Activation; D005340:Fibrinogen / Q000378:metabolism; D008070:Lipopolysaccharides / Q000633:toxicity*; D037601:Mannose-Binding Lectin / Q000502:physiology*; D050606:Mannose-Binding Protein-Associated Serine Proteases; D051379:Mice; D008807:Mice, Inbred BALB C; D008809:Mice, Inbred C3H; D012697:Serine Endopeptidases / Q000502:physiology*
D008070:Lipopolysaccharides; D037601:Mannose-Binding Lectin; D005340:Fibrinogen; D050606:Mannose-Binding Protein-Associated Serine Proteases; D012697:Serine Endopeptidases