Isolation and characterisation of Haemophilus influenzae type b mutants defective in transferrin-binding and iron assimilation.
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.
Holland
J
J
Department of Microbiology, University Hospital, Nottingham, U.K.
Towner
K J
KJ
Williams
P
P
D002352:Carrier Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006193:Haemophilus influenzae / Q000187:drug effects / Q000235:genetics* / Q000302:isolation & purification / Q000502:physiology; D015151:Immunoblotting; D007501:Iron / Q000378:metabolism*; D033862:Iron-Binding Proteins; D007700:Kinetics; D008970:Molecular Weight; D009154:Mutation; D013308:Streptonigrin / Q000494:pharmacology; D014168:Transferrin / Q000378:metabolism* / Q000494:pharmacology; D033863:Transferrin-Binding Proteins
D002352:Carrier Proteins; D033862:Iron-Binding Proteins; D014168:Transferrin; D033863:Transferrin-Binding Proteins; D013308:Streptonigrin; D007501:Iron