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The IL-10R2 binding hot spot on IL-22 is located on the N-terminal helix and is dependent on N-linked glycosylation.

Abstract：

:IL-22 is a class 2 alpha-helical cytokine involved in the generation of inflammatory responses. These activities require IL-22 to engage the cell surface receptors IL-22R1 and the low-affinity signaling molecule IL-10R2. IL-10R2 also interacts with five other class 2 cytokines: IL-10, IL-26, and the interferon-like cytokines IL-28A, IL-28B, and IL-29. Here, we define the IL-10R2 binding site on IL-22 using surface plasmon resonance (SPR) and site-directed mutagenesis. Surprisingly, the binding hot spot on IL-22 includes asparagine 54 (N54), which is post-translationally modified by N-linked glycosylation. Further characterization of the glycosylation reveals that only a single fucosylated N-acetyl glucosamine on N54 is required for maximal IL-10R2 binding. Biological responses of IL-22 mutants measured in cell-based luciferase assays correlate with the in vitro SPR studies. Together, these data suggest that IL-22 activity may be modulated via changes in the glycosylation state of the ligand during inflammation.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Logsdon NJ,Jones BC,Allman JC,Izotova L,Schwartz B,Pestka S,Walter MR

doi

10.1016/j.jmb.2004.07.069

keywords:

subject

Has Abstract

pub_date

2004-09-10 00:00:00

pages

503-14

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(04)00909-X

journal_volume

342

pub_type

杂志文章

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