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CX3C chemokine mimicry by respiratory syncytial virus G glycoprotein

Abstract

Chemokines are chemoattractant proteins that are divided into subfamilies based upon cysteine signature motifs termed C, CC, CXC and CX3C. Chemokines have roles in immunity and inflammation that affect cell trafficking and activation of T cells as well as cells of the innate immune system. We report here CX3C chemokine mimicry for the G glycoprotein of respiratory syncytial virus (RSV) and show binding to CX3CR1—the specific receptor for the CX3C chemokine fractalkine—and induction of leukocyte chemotaxis. We also show that CX3CR1 facilitates RSV infection of cells. Thus, G glycoprotein interaction with CX3CR1 probably plays a key role in the biology of RSV infection.

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Figure 1: G glycoprotein and Fkn binding to 293 and 293.CX3CR1 cells.
Figure 2: Characterization of the G glycoprotein preparations.
Figure 3: Radioligand inhibition studies of a Fkn polypeptide by G glycoprotein and Fkn.
Figure 4: The chemotactic indices.

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Acknowledgements

We thank D. Moore, L. Kirsch and J. DeYonker for help preparing reagents and technical support.

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Correspondence to Ralph A. Tripp.

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Tripp, R., Jones, L., Haynes, L. et al. CX3C chemokine mimicry by respiratory syncytial virus G glycoprotein. Nat Immunol 2, 732–738 (2001). https://doi.org/10.1038/90675

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