Staphylococcus aureus causes life-threatening disease in humans. The S. aureus surface
protein iron-regulated surface determinant H (IsdH) binds to mammalian hemoglobin (Hb) …

The human pathogen Staphylococcus aureus acquires heme iron from hemoglobin (Hb) via
the action of a series of iron-regulated surface determinant (Isd) proteins. The cell wall …

Streptococcal solute-binding proteins (SBPs) associated with ATP-binding cassette
transporters gained widespread attention first as ostensible adhesins, next as virulence …

Iron is a critical nutrient for the growth and survival of most bacterial species. Accordingly,
much attention has been paid to the mechanisms by which host organisms sequester iron …

Virtually all organisms require iron and have evolved to obtain this element in free or
chelated forms. Under anaerobic or low pH conditions commonly encountered by numerous …

The ability to gain access to iron is pivotal for bacterial pathogens during infection. Although
much is known about iron acquisition systems in Gram‐negative bacteria, comparatively …

The Staphylococcus aureus genome encodes three ferric uptake regulator (Fur)
homologues: Fur, PerR, and Zur. To determine the exact role of PerR, we inactivated the …

Iron is critical for virtually all forms of life. The production of high‐affinity iron chelators,
siderophores, and the subsequent uptake of iron–siderophore complexes are a common …

The Staphylococcus aureus genome encodes three ferric uptake repressor (Fur)
homologues: Fur, PerR, and Zur. To determine the exact role of Fur in S. aureus, we …

During infections the pathogen Staphylococcus aureus procures the essential nutrient iron
from its host using iron-regulated surface determinant (Isd) proteins, which scavenge heme …