Ultrastructural Effects of Lactoferrin Binding on Giardia lamblia Trophozoites

Authors

  • JILL MARIE TURCHANY,

    1. Department of Pathology, Division of Infectious Deseases
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    • Current address: Rock Valley College, 3301 North Mulford Road, Rockford, Illinois 61 I14.

  • J. MICHAEL MCCAFFERY,

    1. Division of Cellular and Molecular medicine
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  • STEPHEN B. ALEY,

    1. Department of Pathology, Division of Infectious Deseases
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    • Current address: Rock Valley College, 3301 North Mulford Road, Rockford, Illinois 61 I14.

  • FRANCES D. GILLIN

    Corresponding author
    1. Center for Molecular Genetics, University of California at San Diego, California 92103-8416
      To whom correspondence should be addressed at: Department of Pathology, Mail Code 8416, UCSD Medical Center, 214 Dickinson Street, San doegp. Ca;ofprmoa 92103-8416. Telephone: 619-543-6146, Fax: 619-543-6614, Email: fgillin@ucsd.edu
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  • Current address: Department of Biological Sciences, University oj Texas, El Paso, El Paso Texas 79968-0590.

To whom correspondence should be addressed at: Department of Pathology, Mail Code 8416, UCSD Medical Center, 214 Dickinson Street, San doegp. Ca;ofprmoa 92103-8416. Telephone: 619-543-6146, Fax: 619-543-6614, Email: fgillin@ucsd.edu

Abstract

ABSTRACT. Lactoferrin and its derived N-terminal peptide may be important host defenses against Giardia lamblia. We showed earlier that lactoferrin and the derived peptides have potent giardicidal activity in vitro. Using indirect immunofluorescence, we now demonstrate binding of lactoferrin and the peptides to the live trophozoite surface. Iron strongly inhibited binding of lactoferrin, and decreased binding of the peptides, while certain divalent metal ions decreased binding of all forms by about half. Lactoferrin and the peptedes caused striking and complex morphologic changes in the trophozoite plasmalemma, endomembranes and cytoskeleton, and increases the electron density of the lysosome-like peripheral vacuoles.

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