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A point mutation in interleukin-2 that alters ligand internalization

D Z Chang¹, Z Wu, T L Ciardelli

¹Department of Pharmacology and Toxicology, Dartmouth Medical School, Hanover, New Hampshire 03755-3835, USA.

The Journal of Biological Chemistry

|June 7, 1996

Summary

A novel interleukin-2 (IL-2) analog, T51P, shows reduced receptor internalization, leading to prolonged T-cell proliferation. This finding offers a new strategy for developing cytokine analogs with enhanced properties.

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Area of Science:

Immunology
Molecular Biology
Biochemistry

Background:

Interleukin-2 (IL-2) signaling duration is critical for T-cell responses.
Ligand-dependent receptor internalization is a key factor controlling signaling duration.
Previous studies identified an IL-2 analog (T51P) with reduced receptor binding affinity but maintained bioactivity.

Purpose of the Study:

To investigate whether the T51P analog exhibits reduced receptor internalization compared to wild-type IL-2.
To determine if reduced internalization contributes to the enhanced response observed with the T51P analog.

Main Methods:

Compared internalization rates of IL-2 and T51P using three distinct assays.
Analyzed receptor binding kinetics, including rate constants.

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Assessed T-cell proliferation bioassays to evaluate functional effects.

Main Results:

T51P demonstrated a markedly reduced receptor internalization rate compared to wild-type IL-2.
Altered binding kinetics did not account for the decreased internalization.
T51P sustained T-cell proliferation for a longer duration than IL-2.

Conclusions:

The T51P mutation independently reduces IL-2 receptor internalization rate.
This reduced internalization is linked to prolonged T-cell signaling and proliferation.
T51P serves as a potential model for engineering cytokine analogs with modulated agonist/antagonist activities.