Binding affinity key to anti-inflammatory protein IL-10 biological effects
Published on 16 September 2020
Latest research led by Ignacio Moraga’s lab in the School has shown how binding affinity is key to anti-inflammatory protein Interleukin-10’s (IL-10) biological effects.
This work is published today in Science Signaling.
IL-10 is a protein secreted by immune cells. Alongside its potent anti-inflammatory effects, recent research has described its potential anti-cancer effects. IL-10 enhances the activity of tumour targeting CD8 T cells which play an important role in killing cancerous cells. This new study provides new information about how IL-10’s binding affinity affects its biological activities.
Claire Gorby, first author of the study and PhD student from the Moraga lab in the Division of Cell Signalling and Immunology, said, “We have generated a mutant variant of IL-10 which has hugely increased binding affinity for one of its receptor subunits. This high affinity IL-10 was able to act more effectively than the wild type at low concentrations in two different immune cell populations, as well as increasing the killing activity of tumour targeting T cells.”
The work gives new options for exploring the use of IL-10 as therapies both for inflammatory disorders and as a cancer therapeutic.
This research was undertaken with collaborators in the Universities of Lille, Osnabruck, Bourgogne Franche-Comté and Alabama.