Covalent bonding of heme to protein prevents heme capture by nontypeable Haemophilus influenzae
| Autor: | Valerie Sgheiza, Kara L. Bren, Bethany Novick, Jeanetta Pierce, Breanne Kalmeta, Lea Vacca Michel, Melody Frink Holmquist, Sarah Stanton, Kyle Grimaldi |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification Hemeprotein biology Cytochrome c 030106 microbiology Peptide medicine.disease_cause biology.organism_classification General Biochemistry Genetics and Molecular Biology 3. Good health Haemophilus influenzae Microbiology 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology chemistry Biochemistry Covalent bond otorhinolaryngologic diseases medicine biology.protein Hemoglobin Heme Bacteria |
| Zdroj: | FEBS Open Bio. 7:1778-1783 |
| ISSN: | 2211-5463 |
| DOI: | 10.1002/2211-5463.12324 |
| Popis: | Nontypeable Haemophilus influenzae (NTHi) are Gram-negative pathogens that contribute to a variety of diseases, including acute otitis media and chronic obstructive pulmonary disease. As NTHi 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 NTHi, 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 NTHi to use these sources to support growth. Results from this study suggest that NTHi can utilize protein-associated heme only if it is noncovalently attached to the protein. |
| Databáze: | OpenAIRE |
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