14 May 2024
Roland Immler, Markus Sperandio and colleagues provide evidence that sialylation of CCR3 by the sialyltranferase ST3Gal-IV is crucial for CCL11-binding to CCR3.
In a study published in PNAS, Roland Immler, Markus Sperandio and colleagues have uncovered a key mechanism that drives allergic and helminthic diseases, shedding light on potential new therapeutic avenues.
Eosinophils are granulocytes developing in the bone marrow from myeloid progenitors. Similar to neutrophils, eosinophils are released from the bone marrow into the blood circulation and are mainly involved in allergic diseases and helminthic diseases. Interestingly, recent evidence sheds light on eosinophil function as an immune-modulatory cell regulating a whole variety of biological processes.
Several eosinophil targeting chemokines including CCL11 (eotaxin-1) have been identified to bind to the eosinophil-expressed chemokine receptor CCR3.
The research team discovered that sialylation of CCR3 by the sialyltransferase ST3Gal-IV is fundamental for the receptor's binding to CCL11, thereby facilitating eosinophil migration under both normal and inflammatory conditions. Consequently, the inhibition of ST3Gal-IV in eosinophils might be an interesting therapeutic strategy to reduce eosinophil-dependent tissue damage in disorders with unwanted eosinophil recruitment including allergic airway diseases.
Immler et al.: CCR3-dependent eosinophil recruitment is regulated by sialyltransferase ST3Gal-IV, PNAS 2024