Utilization of transferrin-bound iron by Haemophilus species of human and porcine origins.
Haemophilus influenzae and H. haemolyticus acquired iron bound to human transferrin but not to human lactoferrin, ovo- or porcine transferrins. Conversely the swine pathogens H. pleuropneumoniae and H. parasuis used iron bound only to porcine transferrin. Growth under conditions of iron deprivation induced the production of siderophores and iron-repressible outer membrane proteins in H. parainfluenzae, H. paraphrophilus and H. parasuis but not in H. influenzae, H. haemolyticus or H. pleuropneumoniae. The latter 3 Haemophilus species appear to sequester transferrin bound iron via a siderophore-independent mechanism. However, the ability to produce iron chelating compounds did not enable H. parainfluenzae or H. paraphrophilus to utilize transferrin bound iron.
Morton
D J
DJ
Department of Pharmaceutical Sciences, University of Nottingham, U.K.
Williams
P
P
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D006190:Haemophilus / Q000378:metabolism*; D006193:Haemophilus influenzae / Q000378:metabolism*; D006801:Humans; D007501:Iron / Q000378:metabolism*; D007502:Iron Chelating Agents / Q000378:metabolism; D007781:Lactoferrin / Q000378:metabolism; D017262:Siderophores; D013045:Species Specificity; D013552:Swine / Q000382:microbiology; D014168:Transferrin / Q000378:metabolism*
D007502:Iron Chelating Agents; D017262:Siderophores; D014168:Transferrin; D007501:Iron; D007781:Lactoferrin