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Título: | Both soluble and membrane-anchored forms of Felid herpesvirus 1 glycoprotein G function as a broad-spectrum chemokine-binding protein |
Autor: | Costes, Berenice; Ruiz-Argüello, M. Begoña CSIC; Bryant, N. A.; Alcamí, Antonio CSIC ORCID; Vanderplasschen, A. | Fecha de publicación: | 2005 | Editor: | Microbiology Society | Citación: | Journal of General Virology 86: 3209-3214 (2005) | Resumen: | 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. © 2005 SGM. | URI: | http://hdl.handle.net/10261/295210 | DOI: | 10.1099/vir.0.81388-0 | ISSN: | 0022-1317 | E-ISSN: | 1465-2099 |
Aparece en las colecciones: | (INIA) Artículos |
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