Transition Metal Sequestration by the Host-Defense Protein Calprotectin.
Annu Rev Biochem
; 87: 621-643, 2018 06 20.
Article
em En
| MEDLINE
| ID: mdl-29925260
ABSTRACT
In response to microbial infection, the human host deploys metal-sequestering host-defense proteins, which reduce nutrient availability and thereby inhibit microbial growth and virulence. Calprotectin (CP) is an abundant antimicrobial protein released from neutrophils and epithelial cells at sites of infection. CP sequesters divalent first-row transition metal ions to limit the availability of essential metal nutrients in the extracellular space. While functional and clinical studies of CP have been pursued for decades, advances in our understanding of its biological coordination chemistry, which is central to its role in the host-microbe interaction, have been made in more recent years. In this review, we focus on the coordination chemistry of CP and highlight studies of its metal-binding properties and contributions to the metal-withholding innate immune response. Taken together, these recent studies inform our current model of how CP participates in metal homeostasis and immunity, and they provide a foundation for further investigations of a remarkable metal-chelating protein at the host-microbe interface and beyond.
Palavras-chave
Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Elementos de Transição
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Complexo Antígeno L1 Leucocitário
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Interações entre Hospedeiro e Microrganismos
Tipo de estudo:
Prognostic_studies
Limite:
Animals
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Humans
Idioma:
En
Revista:
Annu Rev Biochem
Ano de publicação:
2018
Tipo de documento:
Article