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Trudy Hartford, Seamus O'Brien, Peter W. Andrew, Dorothy Jones, Ian S. Roberts, Utilization of transferrin-bound iron by Listeria monocytogenes, FEMS Microbiology Letters, Volume 108, Issue 3, April 1993, Pages 311–318, https://doi.org/10.1111/j.1574-6968.1993.tb06121.x
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Abstract
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.
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