Acid-active neuraminidases in the growth media from cultures of pathogenic Naegleria fowleri and in sonicates of rabbit alveolar macrophages.
Using bovine mucin and isolated human myelin as sources of sialic acid, we demonstrate the presence of neuraminidase activities in the growth media of pathogenic, but not nonpathogenic, Naegleria sp. and in sonicates of rabbit alveolar macrophages. Neuraminidase activity was maximal at pH 4.5 and 5.0, and the specific activity for sialic acid release was up to 13-fold greater with mucin than with human myelin. Activity in the growth media from cultures of pathogenic Naegleria fowleri was ion-independent, while that of macrophage sonicates required divalent cation; optimal activity was noted with 2.5 mM Zn2+, while Mg2+ and Mn2+ supported activity to a lesser extent. Such acid-active neuraminidases may contribute to the reported glycolipid alterations associated with demyelinating diseases.
D000656:Amoeba / Q000201:enzymology* / Q000472:pathogenicity; D000818:Animals; D002413:Cations, Divalent; D006863:Hydrogen-Ion Concentration; D008264:Macrophages / Q000201:enzymology*; D009439:Neuraminidase / Q000378:metabolism*; D011650:Pulmonary Alveoli / Q000166:cytology; D011817:Rabbits; D013379:Substrate Specificity
D002413:Cations, Divalent; D009439:Neuraminidase