Open AccessUtilization of transferrin‐bound iron by Listeria monocytogenes
Author(s) -
Hartford Trudy,
O'Brien Seamus,
Andrew Peter W.,
Jones Dorothy,
Roberts Ian S.
Publication year - 1993
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1993.tb06121.x
Subject(s) - transferrin , listeria monocytogenes , transferrin receptor , biochemistry , horseradish peroxidase , chemistry , iron binding proteins , binding site , biology , microbiology and biotechnology , bacteria , enzyme , genetics
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.