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Published online ahead of print on 4 March 2009 as doi:10.1099/vir.0.009589-0
Journal of General Virology 2009;90:1477.

A more recent version of this article appeared on June 1, 2009 J Gen Virol (2009), DOI 10.1099/vir.0.009589-0
© 2009 Society for General Microbiology
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The orf virus encoded chemokine binding protein is a potent inhibitor of inflammatory monocyte recruitment in a mouse skin model

Zabeen Lateef, Margaret A Baird, Lyn M Wise, Andrew A Mercer and Stephen B Fleming1

Department of Microbiology and Immunology, University of Otago, New Zealand

1 E-mail: stephen.fleming{at}stonebow.otago.ac.nz

The parapoxvirus Orf virus causes pustular dermatitis in sheep and is transmissible to humans. The virus encodes a secreted chemokine binding protein (CBP). We examined the ability of this protein to inhibit migration of murine monocytes in response to CC inflammatory chemokines in chemotaxis assays and its effects on monocyte recruitment into the skin using a mouse model in which inflammation was induced with bacterial lipopolysaccharide. CBP was shown to bind murine chemokines CCL2, CCL3, and CCL5 with high affinity by surface plasmon resonance and completely inhibited chemokine-induced migration of monocytes at a molar ratio of CBP to chemokine of 4:1. In the mouse low levels of CBP potently inhibited the recruitment Gr-1+/CD11b monocytes to the site of inflammation in the skin but had little effect on neutrophil recruitment that suggests that this factor plays a role in disrupting chemokine-induced recruitment of specific immune cell types to sites of infection.

Received 11 December 2008; accepted 16 February 2009.




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