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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Cellular and molecular biology (Noisy-le-Grand, France)

Characterization of an IL-2 mimetic with therapeutic potential

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Cellular and molecular biology (Noisy-le-Grand, France) - 01 Jun 2001

Eckenberg R, Rose T, Moreau JL, Weil R, Gesbert F, Dubois S, Tello D, Bossus M, Gras H, Tartar A, Bertoglio J, Chouaïb S, Jacques Y, Alzari PM, Thèze J

Link to Pubmed [PMID] – 11502078

Cell. Mol. Biol. (Noisy-le-grand) 2001 Jun;47(4):703-7

Human interleukin-2 (IL-2) interacts with two types of functional receptors (IL-2R alpha betagamma and IL-2R betagamma) and acts on a broad range of target cells involved in inflammatory reactions and immune responses. IL-2 is also used in different clinical trials aimed at improving the treatment of some cancers and the recovery of CD4 lymphocytes by HIV patients. The therapeutic index of IL-2 is limited by various side effects dominated by the vascular leak syndrome. We have shown that a chemically synthesised fragment of the IL-2 sequence can fold into a helical tetramer likely mimicking the quatemary structure of an hemopoietin. Indeed, peptide p1-30 (containing amino acids 1 to 30, including the sequence corresponding to the entire alpha helix A of IL-2) spontaneously folds into an alpha-helical homotetramer and stimulates the growth of T-cell lines expressing human IL-2R beta, whereas shorter versions of the peptide lack helical structure and are inactive. At the cellular level, p1-30 induces lymphokine-activated killer (LAK) cells and preferentially activates CD8 low lymphocytes and natural killer cells, which constitutively express IL-2R beta. A significant IFN-gamma production is also detected following p1-30 stimulation. A mutant form of p1-30 (Asp20–>Lys) which is likely unable to induce vascular leak syndrome remains capable to generate LAK cells like the original p1-30 peptide. Altogether our data suggest that p1-30 has therapeutic potential.

http://www.ncbi.nlm.nih.gov/pubmed/11502078