Utilization of transferrin-bound iron by Listeria monocytogenes.
It has been demonstrated that under iron-restricted conditions, Listeria monocytogenes can utilize iron-loaded transferrin (Tf) from a range of species as its sole source of iron for growth. Human transferrin conjugated to horseradish-peroxidase (HRP-Tf) bound directly to whole cells of L. monocytogenes. This binding was blocked by apotransferrin indicating that the receptor can bind transferrin in either the iron-bound or iron-free form. Transferrin-binding was not host specific because both bovine and equine transferrin inhibited the binding of HRP-conjugated human transferrin. SDS-PAGE and Western blotting of bacterial surface extracts revealed the presence of a transferrin-binding protein of approximately 126 kDa.
Department of Microbiology, University of Leicester, UK.
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T
Hartford
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S
O'Brien
P W
PW
Andrew
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Jones
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Roberts
D000818:Animals; D001059:Apoproteins / Q000494:pharmacology; D002417:Cattle; D006736:Horses; D007501:Iron / Q000378:metabolism*; D008089:Listeria monocytogenes / Q000378:metabolism*; D010084:Oxidation-Reduction; D014168:Transferrin / Q000378:metabolism* / Q000494:pharmacology
D001059:Apoproteins; D014168:Transferrin; C028284:apotransferrin; D007501:Iron