ID: 198: Discovery of a novel chemokine binding activity in varicella zoster virus

详细信息    查看全文

• 作者：Victor Gonzalez-Motos¹ ; Birgit Ritter¹ ; Tihana Lenac² ; Stipan Jonjic² ; Fernando Arenzana-Seisdedos³ ; Ulrich Kalinke⁴ ; Abel Viejo-Borbolla¹ ;
• 刊名：Cytokine
• 出版年：2015
• 出版时间：November 2015
• 年：2015
• 卷：76
• 期：1
• 页码：100
• 全文大小：40 K

文摘

Varicella zoster virus (VZV) is a highly prevalent human neurotropic herpesvirus that establishes latency in sensory ganglia. During primary infection it causes varicella and, upon reactivation, herpes zoster, which may be followed by extreme pain. Following replication in epithelial cells of the respiratory mucosa VZV infects T cells at the regional lymph node and spreads systemically. Colonization of sensory ganglia and modulation of the immune system, including T cell migration, are required for VZV mediated pathogenicity. The viral and cellular factors involved in these processes are not well characterized. Chemokines orchestrate the migration of leukocytes to the site of infection playing essential roles in the antiviral response. To carry out their action chemokines are presented to their receptors through binding to glycosaminoglycans (GAGs). Some related viruses express proteins that act as secreted or transmembrane chemokine receptors interfering with chemokine activity, sometimes through GAG interaction. However, until present, none of these proteins have been described in VZV. We have addressed the immunomodulatory role of VZV glycoprotein C (gC). Our data show that VZV gC interacts with GAGs and chemokines with nanomolar affinity as shown by surface plasmon resonance. This binding results in enhanced migration of T cells. The domains involved in the interaction are currently being identified. This constitutes the discovery of the first VZV protein that modulates chemokine activity and points to VZV gC as a relevant factor in the modulation of T cell migration by VZV.