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Isolation and characterisation of Haemophilus influenzae type b mutants defective in transferrin-binding and iron assimilation

Julie Holland , Kevin J. Towner , Paul Williams
DOI: http://dx.doi.org/10.1111/j.1574-6968.1991.tb04362.x 283-287 First published online: 1 January 1991

Summary

The quinone antibiotic streptonigrin was used to select mutants of Haemophilus influenzae type b defective in human transferrin binding. Compared with the parent wild-type strain (JKP1), mutant JKP5 was unable to bind transferrin whilst mutant JKP4 showed reduced binding. JKP5 appeared to lack an approximately 72 kDa transferrin-binding protein. Unlike JKP1, neither JKP4 nor JKP5 were able to acquire iron from human transferrin but their ability to use a variety of other iron and haem compounds as iron sources was unaffected. Such mutants should prove useful in further elucidating the mechanism of transferrin iron-acquisition and its contribution to the virulence of H. influenzae.

Key words
  • Haemophilus influenzae type b
  • Transferrin
  • Iron
  • Streptonigrin

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