Open Access

ARTICLE

Glycosylation enhances functional stability of the chemotactic cytokine CCL2

Paolo Ruggiero^1,*, Silvio Flati², Vito Di Cioccio¹, Giovanni Maurizi², Giovanni Macchia¹, Alberto Facchin¹, Roberto Anacardio¹, Antonio Maras³, Marilena Lucarelli⁴, Diana Boraschi⁴

1 Dompé Research Centre, L’Aquila
2 Consorzio Biolaq, L’Aquila
3 Università degli Studi di Roma « La Sapienza »
4 ITB, CNR, Pisa, Italy

* Corresponding Author: Diana Boraschi,

European Cytokine Network 2003, 14(2), 91-96.

Accepted 02 December 2002;

Abstract

The human chemokine CCL2 gene was expressed in the yeast P.pastoris and gave rise to a mixture of differently glycosylated recombinant proteins. In comparison to non-glycosylated E.coli-derived CCL2, glycosylated yeast CCL2L was 4-20 times less active in a chemotactic assay in vitro. However, CCL2L could maintain full activity upon prolonged incubation at 37°C, whereas the non-glycosylated chemokine readily lost activity. It could be hypothesized that glycosylation is a mechanism used by the organism to modulate CCL2 stability. The partial loss of specific activity due to glycosylation is balanced by the advantage of prolonging the effectiveness of chemokine. Thus, differential glycosylation allows one to obtain highly effective short-lived CCL2 or less-effective long-lived CCL2 and may thus represent a novel mechanism of adaptation to pathological versus physiological conditions.

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Keywords

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