Binding of human hemoglobin by Haemophilus influenzae.
Binding of biotinylated human hemoglobin to Haemophilus influenzae was detected when organisms were grown in heme-deplete, but not heme-replete, conditions. Hemoglobin binding was completely inhibited by a 100-fold excess of unlabelled human hemoglobin or human hemoglobin complexed with human haptoglobin. Binding was only partially inhibited by rat hemoglobin, bovine hemoglobin, human globin, and bovine globin, and not at all by heme, human serum albumin, bovine serum albumin, human transferrin, or myoglobin. Hemoglobin binding was saturable at 16-20 ng of hemoglobin per 10(9) cfu. Binding of human hemoglobin was detected in serotypes a-f and serologically non-typable strains of H. influenzae, as well as Haemophilus haemolyticus but not Haemophilus parainfluenzae, Haemophilus aphrophilus, Haemophilus parahaemolyticus, or Escherichia coli.
Department of Pediatrics, Medical College of Pennsylvania, Philadelphia 19129.
M E
ME
Frangipane
D J
DJ
Morton
J A
JA
Wooten
J M
JM
Pozsgay
T L
TL
Stull
D000818:Animals; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D002417:Cattle; D006190:Haemophilus / Q000145:classification / Q000378:metabolism; D006193:Haemophilus influenzae / Q000254:growth & development / Q000378:metabolism*; D006418:Heme / Q000378:metabolism; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D051381:Rats; D013045:Species Specificity
D001425:Bacterial Outer Membrane Proteins; D006454:Hemoglobins; D006418:Heme