Barbara Campanini

CD163 is a macrophage scavenger receptor central to the clearance of haptoglobin-hemoglobin (HpHb) complexes and the resolution of inflammation. In a remarkable example of near-simultaneous scientific progress, three complementary studies published in Nature Communications1,2,3 have resolved the near-atomic resolution structure of the full extracellular domain of human CD163 complexed with HpHb, primarily utilizing cryo-electron microscopy (cryo-EM).

Abstract Infections caused by Staphylococcus aureus depend on its ability to acquire nutrients. One essential nutrient is iron, which is obtained from the heme of the human host hemoglobin (Hb) through a protein machinery called Iron-regulated surface determinant (Isd) system. IsdB is the protein in charge of heme extraction from Hb, which is the first step of the chain of events leading to iron transfer to the bacterium cell interior.

1 Introduction Pseudomonas aeruginosa (PA) is a Gram-negative organism characterised by an exceptionally diverse metabolism and a predilection for colonising anthropic niches (Brinkman et al., 2021). With a genome comprising over 5,500 open-reading frames, the organism displays remarkable phenotypic plasticity, which, at least partially, accounts for its ubiquity in the built environment.