[en] 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.
Alcami, A. (2003). Viral mimicry of cytokines, chemokines and their receptors. Nat Rev Immunol 3, 36-50.
Baranowski, E., Keil, G., Lyaku, J., Rijsewijk, F. A., van Oirschot, J. T., Pastoret, P. P. & Thiry, E. (1996). Structural and functional analysis of bovine herpesvirus 1 minor glycoproteins. Vet Microbiol 53, 91-101.
Bryant, N. A., Davis-Poynter, N., Vanderplasschen, A. & Alcami, A. (2003). Glycoprotein G isoforms from some alphaherpesviruses function as broad-spectrum chemokine binding proteins. EMBO J 22, 833-846.
Dower, S. K., Kronheim, S. R., March, C. J., Conlon, P. J., Hopp, T. P., Gillis, S. & Urdal, D. L. (1985). Detection and characterization of high affinity plasma membrane receptors for human interleukin 1. J Exp Med 162, 501-515.
Drummer, H. E., Studdert, M. J. & Crabb, B. S. (1998). Equine herpesvirus-4 glycoprotein G is secreted as a disulphide-linked homodimer and is present as two homodimeric species in the virion. J Gen Virol 79, 1205-1213.
Gaskell, R. (1975). Studies on Feline viral rhinotracheitis with particular reference to the carrier state. PhD thesis, University of Bristol, UK.
Lalani, A. S. & McFadden, G. (1999). Evasion and exploitation of chemokines by viruses. Cytokine Growth Factor Rev 10, 219-233.
Markine-Goriaynoff, N., Gillet, L., Karlsen, O. A., Haarr, L., Minner, F., Pastoret, P. P., Fukuda, M. & Vanderplasschen, A. (2004). The core 2 β-1,6-N-acetylglucosaminyltransferase-M encoded by bovine herpesvirus 4 is not essential for virus replication despite contributing to post-translational modifications of structural proteins. J Gen Virol 85, 355-367.
Murphy, P. M. (1996). Chemokine receptors: structure, function and role in microbial pathogenesis. Cytokine Growth Factor Rev 7, 47-64.
Murphy, P. M. (2001). Viral exploitation and subversion of the immune system through chemokine mimicry. Nat Immunol 2, 116-122.
Richman, D. D., Buckmaster, A., Bell, S., Hodgman, C. & Minson, A. C. (1986). Identification of a new glycoprotein of herpes simplex virus type 1 and genetic mapping of the gene that codes for it. J Virol 57, 647-655.
Roizman, B. & Pellett, P. E. (2001). The family Herpesviridae: a brief introduction. In Fields Virology, 4th edn, pp. 2381-2397. Edited by P. M. Howley & D. M. Knipe. Philadelphia: Lippincott Williams & Wilkins.
Stiles, J. (2003). Feline herpesvirus. Clin Tech Small Anim Pract 18, 178-185.