Inhibition of complement by culture supernatants of Aspergillus fumigatus.
Aspergillus fumigatus produced a water-soluble extracellular material that inhibited the opsonization of fungal cells by normal human serum. Blastospores of Cryptococcus neoformans and conidia from A. fumigatus or Aspergillus niger were used as fungal targets for ingestion by human monocytes. The opsonic inhibitor from A. fumigatus was found to decrease binding of complement component C3b to fungal surfaces by selectively interfering with activation of the alternative complement pathway. Inhibition of complement did not appear to result simply from proteolysis, as judged by the minimal degradation of casein and of purified C3 and C4. The complement-inhibiting activity was partially labile to heating at 100 C and could be concentrated by using dialysis tubing with a 10,000-dalton exclusion limit. Aspergillus flavus, which is also a pathogen for humans, also produced this activity; A. niger did not. We speculate that this material may represent a pathogenesis factor for Aspergillus species.
D001232:Aspergillus fumigatus / Q000276:immunology*; D002614:Chelating Agents / Q000494:pharmacology; D003167:Complement Activation; D003179:Complement C3b / Q000276:immunology; D003169:Complement Inactivator Proteins; D003455:Cryptococcus neoformans / Q000276:immunology; D003956:Dialysis; D006358:Hot Temperature; D006801:Humans; D066298:In Vitro Techniques; D009000:Monocytes / Q000276:immunology; D010447:Peptide Hydrolases / Q000378:metabolism; D010587:Phagocytosis; D013172:Spores, Fungal / Q000276:immunology
D002614:Chelating Agents; D003169:Complement Inactivator Proteins; D003179:Complement C3b; D010447:Peptide Hydrolases