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The orphan mouse receptor interleukin (IL)-8R beta binds N51. Structure-function analysis using N51/IL-8 chimeric

J N Heinrich¹, R Bravo

¹Department of Molecular Biology, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, New Jersey 08543-4000.

The Journal of Biological Chemistry

|March 10, 1995

Summary

The mouse interleukin-8 receptor beta (IL-8R beta) binds the N51 cytokine (KC). Specific regions of N51, particularly from the third cysteine to the C terminus, are crucial for this binding interaction.

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Area of Science:

Immunology
Molecular Biology
Biochemistry

Background:

The interleukin-8 receptor beta (IL-8R beta) plays a key role in inflammatory responses.
Identifying ligands for orphan receptors is crucial for understanding cellular signaling pathways.

Purpose of the Study:

To characterize the binding properties of the mouse homolog of human IL-8R beta.
To identify the specific domains of the N51 cytokine responsible for receptor binding.

Main Methods:

Expression of the mouse IL-8R beta homolog in NIH 3T3 cells.
Radioligand binding assays using 125I-N51.
Competition assays with related chemokines.
Analysis of chimeric IL-8/N51 molecules.

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Main Results:

The mouse IL-8R beta receptor binds the N51 cytokine (KC), MIP-2, and GRO alpha/MGSA, but not human IL-8 or NAP-2.
Chimeric analysis revealed that domain I of N51 does not determine binding specificity.
The region from the third cysteine to the C terminus of N51 is critical for high-affinity binding to the mouse IL-8R beta.

Conclusions:

The mouse IL-8R beta receptor recognizes specific chemokines, including N51 (KC).
The C-terminal region of N51 is essential for its interaction with the mouse IL-8R beta receptor.