title: Both soluble and membrane-anchored forms of Felid herpesvirus 1 glycoprotein G function as a broad-spectrum chemokine-binding protein.
abstract: 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.
authors.affiliation: Immunology-Vaccinology (B43b), Department of Infectious and Parasitic Diseases (B43b), Faculty of Veterinary Medicine, University of Liège, B-4000 Liège, Belgium.
authors.forename: B
authors.initials: B
authors.lastname: Costes
authors.affiliation: Centro de Investigación en Sanidad Animal (INIA), Valdeolmos, 28130 Madrid, Spain.|Department of Medicine, University of Cambridge, Addenbrooke's Hospital, Cambridge CB2 2QQ, UK.
authors.forename: M B
authors.initials: MB
authors.lastname: Ruiz-Argüello
authors.affiliation: Department of Medicine, University of Cambridge, Addenbrooke's Hospital, Cambridge CB2 2QQ, UK.
authors.forename: N A
authors.initials: NA
authors.lastname: Bryant
authors.affiliation: Centro Nacional de Biotecnología (CSIC), Campus de Cantoblanco, 28049 Madrid, Spain.|Department of Medicine, University of Cambridge, Addenbrooke's Hospital, Cambridge CB2 2QQ, UK.
authors.forename: A
authors.initials: A
authors.lastname: Alcami
authors.affiliation: Immunology-Vaccinology (B43b), Department of Infectious and Parasitic Diseases (B43b), Faculty of Veterinary Medicine, University of Liège, B-4000 Liège, Belgium.
authors.forename: A
authors.initials: A
authors.lastname: Vanderplasschen
mesh_terms: D018925:Chemokines / Q000037:antagonists & inhibitors / Q000378:metabolism*; D019744:Chemokines, C / Q000378:metabolism; D019742:Chemokines, CC / Q000378:metabolism; D019743:Chemokines, CXC / Q000378:metabolism; D004279:DNA, Viral / Q000737:chemistry; D008969:Molecular Sequence Data; D011485:Protein Binding; D017422:Sequence Analysis, DNA; D018140:Varicellovirus / Q000502:physiology*; D014759:Viral Envelope Proteins / Q000378:metabolism*
chemical_list: D018925:Chemokines; D019744:Chemokines, C; D019742:Chemokines, CC; D019743:Chemokines, CXC; D004279:DNA, Viral; D014759:Viral Envelope Proteins