Giardicidal activity of lactoferrin and N-terminal peptides.
Human and bovine lactoferrins and their derived N-terminal peptides were giardicidal in vitro. Fe3+, but not Fe2+, protected trophozoites from both native lactoferrin and peptides, although the latter lack iron-binding sites. Other divalent metal ions protected only against native lactoferrin. Log-phase cells were more resistant to killing than stationary-phase cells. These studies suggest that lactoferrin, especially in the form of the N-terminal peptides, may be an important nonimmune component of host mucosal defenses against Giardia lamblia.
Turchany
J M
JM
Division of Infectious Diseases, University of California at San Diego 92103-8416, USA.
Aley
S B
SB
Gillin
F D
FD
D000818:Animals; D000981:Antiprotozoal Agents / Q000494:pharmacology*; D002413:Cations, Divalent; D002417:Cattle; D016829:Giardia lamblia / Q000187:drug effects* / Q000254:growth & development; D005873:Giardiasis / Q000276:immunology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007781:Lactoferrin / Q000494:pharmacology*; D008670:Metals / Q000494:pharmacology; D010446:Peptide Fragments / Q000494:pharmacology
D000981:Antiprotozoal Agents; D002413:Cations, Divalent; D008670:Metals; D010446:Peptide Fragments; D007781:Lactoferrin