Siderocalins: Siderophore binding proteins evolved for primary pathogen host defense
| Autor: | Allyson K. Sia, Benjamin E. Allred, Kenneth N. Raymond |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Siderophore
Host (biology) Iron Binding pocket Siderophores Plasma protein binding Bacterial Infections Lipocalin Biology Biochemistry DNA-binding protein Lipocalins Article Analytical Chemistry Microbiology Lipocalin-2 Host-Pathogen Interactions Animals Humans Carrier Proteins Pathogen Iron acquisition Protein Binding |
| Zdroj: | Current Opinion in Chemical Biology |
| ISSN: | 1367-5931 |
| DOI: | 10.1016/j.cbpa.2012.11.014 |
| Popis: | Bacterial pathogens use siderophores to obtain iron from the host in order to survive and grow. The host defends against siderophore-mediated iron acquisition by producing siderocalins. Siderocalins are a siderophore binding subset of the lipocalin family of proteins. The design of the siderophore binding pocket gives siderocalins the ability to bind a wide variety of siderophores and protect the host against several pathogens. Siderocalins have been identified in humans, chickens, and quail, among other animals. The differences in the respective siderocalins suggest that each was developed in response to the most serious pathogens encountered by that animal. Additionally, siderocalins have been observed in many roles unrelated to pathogen defense including differentiation, embryogenesis, inflammation, and cancer. |
| Databáze: | OpenAIRE |
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