Research Article: Structural Basis of Chemokine Sequestration by a Tick Chemokine Binding Protein: The Crystal Structure of the Complex between Evasin-1 and CCL3

Date Published: December 30, 2009

Publisher: Public Library of Science

Author(s): João M. Dias, Christophe Losberger, Maud Déruaz, Christine A. Power, Amanda E. I. Proudfoot, Jeffrey P. Shaw, Andreas Hofmann.

Abstract: Chemokines are a subset of cytokines responsible for controlling the cellular migration of inflammatory cells through interaction with seven transmembrane G protein-coupled receptors. The blocking of a chemokine-receptor interaction results in a reduced inflammatory response, and represents a possible anti-inflammatory strategy, a strategy that is already employed by some virus and parasites. Anti-chemokine activity has been described in the extracts of tick salivary glands, and we have recently described the cloning and characterization of such chemokine binding proteins from the salivary glands, which we have named Evasins.

Partial Text: Chemokines (chemotactic cytokines) are a subset of cytokines primarily responsible for controlling the cellular migration of various inflammatory cells. They compose a large family (approximately 40 known members in the human system)[1] of small proteins which share a relatively low level of sequence identity, but which display a remarkable structural homology, since they all contain the same monomeric fold. Chemokines control the migration of leukocytes through interaction with members of the G protein-coupled receptor family which possess seven transmembrane helices. The pairing of the chemokines to their receptors has been carried out, mainly by receptor binding assays, and has identified receptors that are specific (bind to a single ligand) or shared (bind more than one ligand). The association of certain receptors and ligands with disease has come from many studies of their expression in biopsy samples and body fluids, animal models and genetically engineered mice.



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