@entity68 -Binding Protein Degradation by XXXX Proteases of Naegleria fowleri.

@entity558 @entity462 @entity5422 @entity1372 @entity69 @entity460 @entity3363 @entity68
Naegleria fowleri causes acute and fulminant primary amoebic @entity5422 . This microorganism invades its host by penetrating the olfactory mucosa and then traveling up the mesaxonal spaces and crossing the cribriform plate; finally, the trophozoites invade the olfactory bulbs. During its invasion, the protozoan obtains nutrients such as proteins, lipids, @entity3363 , and cationic ions (e.g., @entity68 , @entity460 , and @entity1372 ) from the host. However, the mechanism by which these ions are obtained, particularly @entity68 , is poorly understood. In the present study, we evaluated the ability of N. fowleri to degrade @entity68 -binding proteins, including hololactoferrin, @entity69 , ferritin, and hemoglobin. Zymography assays were performed for each substrate under physiological conditions (pH 7 at 37  C) employing @entity558 ( @entity558 ) and total crude extracts (TCEs) of N. fowleri. Different degradation patterns with @entity558 were observed for hololactoferrin, @entity69 , and hemoglobin; however, @entity558 did not cause ferritin degradation. In contrast, the TCEs degraded only hololactoferrin and @entity69 . Inhibition assays revealed that @entity462 proteases were involved in this process. Based on these results, we suggest that @entity558 and TCEs of N. fowleri degrade @entity68 -binding proteins by employing @entity462 proteases, which enables the parasite to obtain @entity68 to survive while invading the central nervous system.
