Siderocalins: Siderophore binding proteins evolved for primary pathogen host defense

AK Sia, BE Allred, KN Raymond - Current opinion in chemical biology, 2013 - Elsevier
AK Sia, BE Allred, KN Raymond
Current opinion in chemical biology, 2013Elsevier
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 …
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.
Elsevier