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Accueil du site > Production scientifique > The disulfide bond between cysteine 10 and cysteine 34 is required for CCL18 activity.

The disulfide bond between cysteine 10 and cysteine 34 is required for CCL18 activity.

Date de publication: 1er octobre 2013

B. Legendre, C. Tokarski, Y. Chang, N. De Freitas Caires, H. Lortat-Jacob, P. D. Nadaï, C. Rolando, C. Duez, A. Tsicopoulos, P. Lassalle.
Cytokine 64 463-470 (2013). DOI

Travail réalisé sur le site de l’Université de Lille 1, Sciences et Technologies.


Asthma is a Th2-mediated disease that involves Th2 cell and eosinophil migration into the bronchial mucosa which is dependent upon the expression of a specific set of chemokines within the lung. Among them, CCL18 seems to play a key role because of its preferential expression in the lung, and its up-regulation by Th2 cytokines. Here, we show that the optimal naïve T cell and basophil chemotaxis, and basophil histamine release induced by rhCCL18 occurred at a 100 time lower concentration with CHO-derived rhCCL18 than with E. coli-derived rhCCL18. FT-ICR mass spectrometry of the intact chemokines showed that the rhCCL18 produced by CHO cells contained the 2 disulfide bonds Cys10-Cys34 and Cys11-Cys50, in clear contrast to the rhCCL18 derived from E. coli where the Cys10-Cys34 bond was absent. We found that reduction of the Cys10-Cys34 of the CHO-derived rhCCL18 resulted in a shift of its activity, reaching the same level as the E. coli-derived rhCCL18. These results demonstrate that the Cys10-Cys34 disulfide bond is involved in the function of CCL18.