Giardicidal activity of lactoferrin and N-terminal peptides

Author:

Turchany J M1,Aley S B1,Gillin F D1

Affiliation:

1. Division of Infectious Diseases, University of California at San Diego 92103-8416, USA.

Abstract

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.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Reference24 articles.

1. Killing of Giardia lamblia by cryptdins and cationic neutrophil peptides;Aley S. B.;Infect. Immun.,1994

2. Bactericidal activity of human lactoferrin: sensitivity of a variety of microorganisms;Arnold R. R.;Infect. Immun.,1980

3. A bactericidal effect for human lactoferrin;Arnold R. R.;Science,1977

4. Bactericidal activity of human lactoferrin: influence of physical conditions and metabolic state of the target microorganism;Arnold R. R.;Infect. Immun.,1981

5. Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin;Bellamy W.;J. Appl. Bacteriol.,1992

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