The Journal of Experimental Medicine
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Published online
doi:10.1084/jem.20072689
The Journal of Experimental Medicine, Vol. 205, No. 9, 2019-2031
The Rockefeller University Press, 0022-1007 $30.00
© Déruaz et al.
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ARTICLE

 Ticks produce highly selective chemokine binding proteins with antiinflammatory activity

Maud Déruaz1, Achim Frauenschuh1, Ana L. Alessandri2, João M. Dias1, Fernanda M. Coelho2, Remo C. Russo2, Beatriz R. Ferreira3, Gerard J. Graham4, Jeffrey P. Shaw1, Timothy N.C. Wells1, Mauro M. Teixeira2, Christine A. Power1, and Amanda E.I. Proudfoot1

1 Merck Serono Geneva Research Centre, 1202 Geneva, Switzerland
2 Departamento de Bioquimica e Imunologia, Instituto de Ciencias Biologicas, Universidade Federal de Minas Gerais, Belo Horizonte, MG, Brazil
3 Departamento de Bioquímica e Imunologia, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, SP, Brazil
4 Division of Immunology, Infection and Inflammation, University of Glasgow, Glasgow, G12 8TA, Scotland, UK

CORRESPONDENCE Amanda E.I. Proudfoot: amanda.proudfoot{at}merckserono.net OR Chrstine A. Power: christine.power{at}merckserono.net

Bloodsucking parasites such as ticks have evolved a wide variety of immunomodulatory proteins that are secreted in their saliva, allowing them to feed for long periods of time without being detected by the host immune system. One possible strategy used by ticks to evade the host immune response is to produce proteins that selectively bind and neutralize the chemokines that normally recruit cells of the innate immune system that protect the host from parasites. We have identified distinct cDNAs encoding novel chemokine binding proteins (CHPBs), which we have termed Evasins, using an expression cloning approach. These CHBPs have unusually stringent chemokine selectivity, differentiating them from broader spectrum viral CHBPs. Evasin-1 binds to CCL3, CCL4, and CCL18; Evasin-3 binds to CXCL8 and CXCL1; and Evasin-4 binds to CCL5 and CCL11. We report the characterization of Evasin-1 and -3, which are unrelated in primary sequence and tertiary structure, and reveal novel folds. Administration of recombinant Evasin-1 and -3 in animal models of disease demonstrates that they have potent antiinflammatory properties. These novel CHBPs designed by nature are even smaller than the recently described single-domain antibodies (Hollinger, P., and P.J. Hudson. 2005. Nat. Biotechnol. 23:1126–1136), and may be therapeutically useful as novel antiinflammatory agents in the future.

Abbreviations used: CHPB, chemokine binding protein; mBSA, methylated BSA; SELDI, surface enhanced laser desorption ionization; SPR, surface plasmon resonance.

A. Frauenschuh's present address is Novartis Pharma AG, 4056 Basel, Switzerland.

© 2008 Déruaz et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jem.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).


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