title: Nutritional Immunity: S100 Proteins at the Host-Pathogen Interface.
abstract: The S100 family of EF-hand calcium (Ca(2+))-binding proteins is essential for a wide range of cellular functions. During infection, certain S100 proteins act as damage-associated molecular patterns (DAMPs) and interact with pattern recognition receptors to modulate inflammatory responses. In addition, these inflammatory S100 proteins have potent antimicrobial properties and are essential components of the immune response to invading pathogens. In this review, we focus on S100 proteins that exhibit antimicrobial properties through the process of metal limitation, termed nutritional immunity, and discuss several recent advances in our understanding of S100 protein-mediated metal sequestration at the site of infection.
authors.affiliation: From the Department of Pathology, Microbiology, and Immunology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232 and.
authors.forename: Joseph P
authors.initials: JP
authors.lastname: Zackular
authors.affiliation: the Departments of Biochemistry and Chemistry, and Center for Structural Biology, Vanderbilt University, Nashville, Tennessee 37232.
authors.forename: Walter J
authors.initials: WJ
authors.lastname: Chazin
authors.affiliation: From the Department of Pathology, Microbiology, and Immunology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232 and Eric.skaar@Vanderbilt.edu.
authors.forename: Eric P
authors.initials: EP
authors.lastname: Skaar
mesh_terms: D000818:Animals; D001424:Bacterial Infections / Q000276:immunology; D054884:Host-Pathogen Interactions; D006801:Humans; D007113:Immunity, Innate; D009418:S100 Proteins / Q000502:physiology*
chemical_list: D009418:S100 Proteins
keywords: S100 proteins; S100A12; S100A7; bacteria; calprotectin; host-pathogen interaction; immunology; microbiology; nutritional immunity