JDS
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Journal of Dairy Science Vol. 74 No. 4 1218-1226
© 1991 by American Dairy Science Association ®
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Naidu, A. S.
Right arrow Articles by Watts, J. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Naidu, A. S.
Right arrow Articles by Watts, J. L.

Bovine Lactoferrin Receptors in Staphylococcus aureus Isolated from Bovine Mastitis

A. S. Naidu 1, M. Anderson 1, J. Miedzobrodzki 1, A. Forsgren 1, and J. L. Watts 2

1 Department of Medical Microbiology, University of Lund, Malmö General Hospital, S-21401 Malmö Sweden
2 Hill Farm Research Station, Louisiana Agricultural Experiment Station, Louisiana State University Agricultural Center, Homer 71040

A total of 103 Staphylococcus aureus strains isolated from bovine mastitis were tested for bovine lactoferrin binding in a 125I-labeled protein binding assay. More than 85% of the strains demonstrated high to moderate and a few showed little or no binding. Bovine lactoferrin binding to S. aureus cells was high when grown on blood, nutrient, or proteose-peptone agar, but the binding capacity was low with cells grown on salt rich media, in skim milk, or in broth. The kinetics of 125I-labeled bovine lactoferrin binding required approximately 90 min for complete saturation with optimal interaction in the pH range 4.0 to 7.0. The lactoferrin-staphylococci interaction was specific with a high affinity (association constant, Ka 14 x 106 L/mol). Scatchard plot analysis estimated the number of binding sites per cell at 7200 on strain SA-340. Unlabeled bovine lactoferrin effectively displaced the binding of the labeled ligand to strain SA-340 in a dose-dependent manner. Bovine lactoferrin binding was inhibited or displaced by human lactoferrin. Various plasma, connective tissue, or mucosal secretory proteins tested did not inhibit lactoferrin-staphylococci interaction. Bovine lactoferrin binding components on SA-340 were resistant to glycolytic enzymes and moderately susceptible to proteolytic digestion. Two proteins with an estimated molecular weight of approximately 92 and 67 kDa were identified as bovine lactofenin binding components of S. aureus strain SA-340.

Key Words: lactoferrin • binding • Staphylococcus aureus

Submitted on June 18, 1990
Accepted on November 1, 1990




This article has been cited by other articles:


Home page
J DAIRY SCIHome page
M. S. Diarra, D. Petitclerc, and P. Lacasse
Response of Staphylococcus aureus Isolates from Bovine Mastitis to Exogenous Iron Sources
J Dairy Sci, September 1, 2002; 85(9): 2141 - 2148.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1991 by the American Dairy Science Association ®.