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

Costes, Bérénice; Ruiz-Argüello, M. Begoña; Bryant, Neil; Alcamı́, Antonio; Vanderplasschen, Alain

doi:10.1099/vir.0.81388-0

Cited by 27 publications

(34 citation statements)

References 12 publications

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“…Conserved in related alphaherpesviruses such as PrV, EHV-1 and HSV-1, this evasion mechanism is mediated by the interaction of gC with the third complement component (C3), the key mediator of complement activation [79]. Another immunomodulatory function conserved in alphaherpesvirus has been identified through the interaction of gG with several chemokines [19,32]. Both soluble and membrane-anchored forms of BoHV-1 gG function as broad-spectrum chemokine binding proteins.…”

Section: Immune Response and Immune Evasion Strategiesmentioning

confidence: 99%

Bovine herpesvirus 1 infection and infectious bovine rhinotracheitis

et al. 2007

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-Bovine herpesvirus 1 (BoHV-1), classified as an alphaherpesvirus, is a major pathogen of cattle. Primary infection is accompanied by various clinical manifestations such as infectious bovine rhinotracheitis, abortion, infectious pustular vulvovaginitis, and systemic infection in neonates. When animals survive, a life-long latent infection is established in nervous sensory ganglia. Several reactivation stimuli can lead to viral re-excretion, which is responsible for the maintenance of BoHV-1 within a cattle herd. This paper focuses on an updated pathogenesis based on a molecular characterization of BoHV-1 and the description of the virus cycle. Special emphasis is accorded to the impact of the latency and reactivation cycle on the epidemiology and the control of BoHV-1. Several European countries have initiated BoHV-1 eradication schemes because of the significant losses incurred by disease and trading restrictions. The vaccines used against BoHV-1 are described in this context where the differentiation of infected from vaccinated animals is of critical importance to achieve BoHV-1 eradication.

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Section: Immune Response and Immune Evasion Strategiesmentioning

confidence: 99%

Bovine herpesvirus 1 infection and infectious bovine rhinotracheitis

et al. 2007

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“…These proteins are generally known as viral chemokinebinding proteins (vCKBPs). One of them, gG from some non-human alphaherpesvirus, binds to chemokines with high affinity and inhibits chemokine function (Bryant et al, 2003;Costes et al, 2005). We have shown chemokine-binding activity for the gG of bovine herpesvirus (BHV)-1, BHV-5, equine herpesvirus (EHV)-1 and felid herpesvirus 1 (FeHV-1) (Bryant et al, 2003;Costes et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

“…One of them, gG from some non-human alphaherpesvirus, binds to chemokines with high affinity and inhibits chemokine function (Bryant et al, 2003;Costes et al, 2005). We have shown chemokine-binding activity for the gG of bovine herpesvirus (BHV)-1, BHV-5, equine herpesvirus (EHV)-1 and felid herpesvirus 1 (FeHV-1) (Bryant et al, 2003;Costes et al, 2005). Chemokine-binding activity could not be demonstrated for the gG of EHV-4, or supernatant from cells infected with herpes simplex virus (HSV) or varicella-zoster virus (VZV) (Bryant et al, 2003;Van de Walle et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Glycoprotein G from pseudorabies virus binds to chemokines with high affinity and inhibits their function

Viejo‐Borbolla

Muñoz

Tabarés

et al. 2009

Journal of General Virology

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Pseudorabies virus (PRV), also known as suid herpesvirus, is the aetiological agent of Aujeszky's disease in swine. In other animals, except higher-order primates, PRV infection is often fatal. The mechanisms of PRV pathogenesis and immune modulation are largely unknown. PRV codes for 11 glycoproteins. Among them, glycoprotein G (gG) is the most abundant PRV protein found in the supernatant of PRV-infected cell cultures. PRV-gG has low amino acid sequence similarity with gG from other animal alphaherpesviruses and its function is unknown. gG from other animal alphaherpesviruses, with the exception of at least equine herpesvirus 4, binds to chemokines. We show here that PRV-gG binds to the human chemokine CL1 and several CC and CXC human chemokines with high affinity. Chemokine-binding activity can be detected in the supernatants of PRV-infected cell cultures, and insertional inactivation of the gene encoding gG from the PRV genome results in loss of chemokine-binding activity. Binding of PRV-gG to chemokines inhibits chemokine-mediated cell migration, suggesting a role for PRV-gG in immune evasion.

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“…R ecently, glycoprotein G (gG) 3 of several alphaherpesviruses has been described to function as a broad-spectrum chemokine-binding protein (1,2). As chemokines play central roles in mediating inflammatory responses during viral infection, it is not surprising that viruses have adopted strategies to evade or modulate their activity.…”

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confidence: 99%

Herpesvirus Chemokine-Binding Glycoprotein G (gG) Efficiently Inhibits Neutrophil Chemotaxis In Vitro and In Vivo

Walle

May

Sukhumavasi

et al. 2007

The Journal of Immunology

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Glycoprotein G (gG) of alphaherpesviruses has been described to function as a viral chemokine-binding protein (vCKBP). More recently, mutant viruses devoid of gG have been shown to result in increased virulence, but it remained unclear whether the potential of gG to serve as a vCKBP is responsible for this observation. In this study, we used equine herpesvirus type 1 (EHV-1) as a model to study the pathophysiological importance of vCKBP activity. First, in vitro chemotaxis assays studying migration of immune cells, an important function of chemokines, were established. In such assays, supernatants of EHV-1-infected cells significantly inhibited IL-8-induced chemotaxis of equine neutrophils. Identification of gG as the responsible vCKBP was achieved by repeating similar experiments with supernatants from cells infected with a gG-negative mutant, which were unable to alter IL-8-induced equine neutrophil migration. Furthermore, rEHV-1 gG was able to significantly reduce neutrophil migration, establishing gG as a bona fide vCKBP. Second, and importantly, in vivo analyses in a murine model of EHV-1 infection showed that neutrophil migration in the target organ lung was significantly reduced in the presence of gG. In summary, we demonstrate for the first time that EHV-1 gG not only binds to chemokines but is also capable of inhibiting their chemotactic function both in vitro and in vivo, thereby contributing to viral pathogenesis and virulence.

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

Cited by 27 publications

References 12 publications

Bovine herpesvirus 1 infection and infectious bovine rhinotracheitis

Bovine herpesvirus 1 infection and infectious bovine rhinotracheitis

Glycoprotein G from pseudorabies virus binds to chemokines with high affinity and inhibits their function

Herpesvirus Chemokine-Binding Glycoprotein G (gG) Efficiently Inhibits Neutrophil Chemotaxis In Vitro and In Vivo

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