@article{mbs:/content/journal/jgv/10.1099/vir.0.81388-0, author = "Costes, B. and Ruiz-Argüello, M. B. and Bryant, N. A. and Alcami, A. and Vanderplasschen, A.", title = "Both soluble and membrane-anchored forms of Felid herpesvirus 1 glycoprotein G function as a broad-spectrum chemokine-binding protein", journal= "Journal of General Virology", year = "2005", volume = "86", number = "12", pages = "3209-3214", doi = "https://doi.org/10.1099/vir.0.81388-0", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.81388-0", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", 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.", }