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

被引:27
作者
Costes, B
Ruiz-Argüello, MB
Bryant, NA
Alcami, A
Vanderplasschen, A [1 ]
机构
[1] Univ Liege, Fac Med Vet, Dept Infect & Parasit Dis B43B, B-4000 Liege, Belgium
[2] Univ Cambridge, Addenbrookes Hosp, Dept Med, Cambridge CB2 2QQ, England
[3] INIA, Ctr Invest Sanidad Anim, Madrid, Spain
[4] CSIC, Ctr Nacl Biotecnol, E-28049 Madrid, Spain
基金
英国惠康基金;
关键词
D O I
10.1099/vir.0.81388-0
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
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.
引用
收藏
页码:3209 / 3214
页数:6
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