Binding of human hemoglobin by Haemophilus influenzae |
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Authors: | Margaret E. Frangipane Daniel J. Morton James A. Wooten Judith M. Pozsgay Terrence L. Stull |
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Affiliation: | Division of Infectious Disease, Department of Pediatrics and Department of Microbiology and Immunology, Medical College of Pennsylvania, 3300 Henry Avenue, Philadelphia, PA 19129, USA |
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Abstract: | Abstract 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 109 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 . |
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Keywords: | Haemophilus influenzae Hemoglobin Iron uptake Heme uptake |
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