The C-terminal extension of calprotectin mediates zinc chelation and modulates Staphylococcus aureus biomass accumulation.

ABSTRACT: Calprotectin (CP) is an S100A8/S100A9 heterodimer that plays an important role in nutritional immunity at the host-microbe interface. CP combats Staphylococcus aureus growth by sequestration of zinc and other trace transition metals; however, questions remain about whether CP antimicrobial activity strictly relies on metal sequestration. Moreover, the precise mechanism for how zinc binds at the two distinct transition metal binding sites of CP is not known. High-resolution X-ray crystal structures reveal tetracoordinate binding in the canonical His₃Asp site and hexacoordinate binding in the His₆ site similar to the binding of manganese and nickel in this site. The S100A9 C-terminal extension (tail) contributes two of the His residues in the His₆ metal-bindi

SUBMITTER: Perera YR 

PROVIDER: S-EPMC12432413 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature