Specificity of the lactoferrin and transferrin receptors in Neisseria gonorrhoeae
- 1 November 1988
- journal article
- research article
- Published by Wiley in Molecular Microbiology
- Vol. 2 (6), 827-829
- https://doi.org/10.1111/j.1365-2958.1988.tb00095.x
Abstract
Lactoferrin (LF) and transferrin (TF) are postulated to be important physiological sources of iron for Neisseria gonorrhoeae. A dot binding assay involving the use of gonococcal total membranes derived from cell grown in iron-limited conditions demonstrated the presence of separate receptors for LF and TF. The ligand and functional specificities of these receptors were examined in competition-binding and growth experiments. The results indicate that the LF and TF receptors are highly specific for the human protein, suggesting that this property may be partially responsible for conferring the human host specificity of N. gonorrhoeae.This publication has 18 references indexed in Scilit:
- Identification and characterization of the human lactoferrin-binding protein from Neisseria meningitidisInfection and Immunity, 1988
- Identification and characterization of the transferrin receptor from Neisseria meningitidisMolecular Microbiology, 1988
- Improved technique utilizing nonfat dry milk for analysis of proteins and nucleic acids transferred to nitrocelluloseGene Analysis Techniques, 1984
- Iron withholding: a defense against infection and neoplasia.Physiological Reviews, 1984
- THE IgA1 PROTEASES OF PATHOGENIC BACTERIAAnnual Review of Microbiology, 1983
- Role of Iron in Microbe-Host InteractionsClinical Infectious Diseases, 1983
- Microbial Envelope Proteins Related to IronAnnual Review of Microbiology, 1982
- The Significance of Iron in InfectionClinical Infectious Diseases, 1981
- Secretory Immunity and the Bacterial IgA ProteasesClinical Infectious Diseases, 1981
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951