Open AccessCovalent bonding of heme to protein prevents heme capture by nontypeable Haemophilus influenzae
Author(s) -
Sgheiza Valerie,
Novick Bethany,
Stanton Sarah,
Pierce Jeanetta,
Kalmeta Breanne,
Holmquist Melody Frink,
Grimaldi Kyle,
Bren Kara L.,
Michel Lea Vacca
Publication year - 2017
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.12324
Subject(s) - heme , haemophilus influenzae , hemoglobin , chemistry , biochemistry , hemeprotein , bacteria , microbiology and biotechnology , biology , enzyme , genetics , antibiotics
Nontypeable Haemophilus influenzae ( NTH i) are Gram‐negative pathogens that contribute to a variety of diseases, including acute otitis media and chronic obstructive pulmonary disease. As NTH i have an absolute requirement for heme during aerobic growth, these bacteria have to scavenge heme from their human hosts. These heme sources can range from free heme to heme bound to proteins, such as hemoglobin. To test the impact of heme structural factors on heme acquisition by NTH i, we prepared a series of heme sources that systematically vary in heme exposure and covalent binding of heme to peptide/protein and tested the ability of NTH i to use these sources to support growth. Results from this study suggest that NTH i can utilize protein‐associated heme only if it is noncovalently attached to the protein.