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Both soluble and membrane-anchored forms of Felid herpesvirus 1 glycoprotein G function as a broad-spectrum chemokine-binding protein

¹ Immunology-Vaccinology (B43b), Department of Infectious and Parasitic Diseases (B43b), Faculty of Veterinary Medicine, University of Liège, B-4000 Liège, Belgium
² Department of Medicine, University of Cambridge, Addenbrooke's Hospital, Cambridge CB2 2QQ, UK
³ Centro de Investigación en Sanidad Animal (INIA), Valdeolmos, 28130 Madrid, Spain
⁴ Centro Nacional de Biotecnología (CSIC), Campus de Cantoblanco, 28049 Madrid, Spain

Correspondence
A. Vanderplasschen
A.vdplasschen{at}ulg.ac.be

Recently, glycoprotein G (gG) of several alphaherpesviruses infecting large herbivores was shown to belong to a new family of chemokine-binding proteins (vCKBPs). In the present study, the function of Felid herpesvirus 1 (FeHV-1) gG as a vCKBP was investigated and the following conclusions were reached: (i) FeHV-1 secreted gG is a high-affinity broad-spectrum vCKBP that binds CC, CXC and C chemokines; (ii) gG is the only vCKBP expressed by FeHV-1 that binds CCL3 and CXCL1; (iii) secreted gG blocks chemokine activity by preventing their interaction with high-affinity cellular receptors; (iv) the membrane-anchored form of gG expressed on the surface of infected cells is also able to bind chemokines; and (v) the vCKBP activity is conserved among different field isolates of FeHV-1. Altogether, these data demonstrate that FeHV-1 gG is a new member of the vCKBP-4 family. Moreover, this study is the first to demonstrate that gG expressed at the surface of FeHV-1-infected cells can also bind chemokines.

The GenBank/EMBL/DDBJ accession number for the nucleotide sequence reported in this paper is AY740677 [GenBank] .

Supplementary figures showing real-time binding data of human chemokines to purified soluble gG, and a schematic of the construction of a recombinant Felid herpesvirus 1 lacking gG and a derived revertant virus are available as supplementary material in JGV Online.

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