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Identification and characterization of the transferrin receptor from Neisseria meningitidis
Author(s) -
Schryvers A. B.,
Morris L. J.
Publication year - 1988
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1988.tb00029.x
Subject(s) - transferrin , neisseria meningitidis , transferrin receptor , biology , lactoferrin , receptor , western blot , bacterial outer membrane , neisseriaceae , microbiology and biotechnology , iron binding proteins , biochemistry , bacteria , gene , genetics , escherichia coli , antibiotics
Summary Expression of the meningococcal transferrin receptor, detected by assay with human transferrin conjugated to peroxidase, was regulated by the level of iron in the medium. The transferrin receptor was identified by SDS‐PAGE and Western blot analysis, as a 71 000 molecular weight iron‐regulated outer membrane protein in Neisseria meningitidis B16B6. Growth studies with iron‐deficient cells and competition binding experiments demonstrated that the meningococcal receptor was species‐specific for human transferrin. Reciprocal competitive binding experiments and limited proteolysis of intact cells indicated that the transferrin and lactoferrin receptors are distinct.