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Herpesvirus chemokine-binding glycoprotein G (gG) efficiently inhibits neutrophil chemotaxis in vitro and in vivo

(2007) JOURNAL OF IMMUNOLOGY. 179(6). p.4161-4169
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Abstract
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.
Keywords
CELLS, INDUCTION, PROTEIN, EHV-1, STRAIN RACL11, VIRULENCE FACTOR, GENE-EXPRESSION, EQUINE HERPESVIRUS-4, MAREKS-DISEASE VIRUS, NECROSIS-FACTOR-ALPHA

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Citation

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Chicago
Van de Walle, Gerlinde, Maeva L May, Woraporn Sukhumavasi, Jens von Einem, and Nikolaus Osterrieder. 2007. “Herpesvirus Chemokine-binding Glycoprotein G (gG) Efficiently Inhibits Neutrophil Chemotaxis in Vitro and in Vivo.” Journal of Immunology 179 (6): 4161–4169.
APA
Van de Walle, Gerlinde, May, M. L., Sukhumavasi, W., von Einem, J., & Osterrieder, N. (2007). Herpesvirus chemokine-binding glycoprotein G (gG) efficiently inhibits neutrophil chemotaxis in vitro and in vivo. JOURNAL OF IMMUNOLOGY, 179(6), 4161–4169.
Vancouver
1.
Van de Walle G, May ML, Sukhumavasi W, von Einem J, Osterrieder N. Herpesvirus chemokine-binding glycoprotein G (gG) efficiently inhibits neutrophil chemotaxis in vitro and in vivo. JOURNAL OF IMMUNOLOGY. 2007;179(6):4161–9.
MLA
Van de Walle, Gerlinde, Maeva L May, Woraporn Sukhumavasi, et al. “Herpesvirus Chemokine-binding Glycoprotein G (gG) Efficiently Inhibits Neutrophil Chemotaxis in Vitro and in Vivo.” JOURNAL OF IMMUNOLOGY 179.6 (2007): 4161–4169. Print.
@article{934025,
  abstract     = {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.},
  author       = {Van de Walle, Gerlinde and May, Maeva L and Sukhumavasi, Woraporn and von Einem, Jens and Osterrieder, Nikolaus},
  issn         = {0022-1767},
  journal      = {JOURNAL OF IMMUNOLOGY},
  keyword      = {CELLS,INDUCTION,PROTEIN,EHV-1,STRAIN RACL11,VIRULENCE FACTOR,GENE-EXPRESSION,EQUINE HERPESVIRUS-4,MAREKS-DISEASE VIRUS,NECROSIS-FACTOR-ALPHA},
  language     = {eng},
  number       = {6},
  pages        = {4161--4169},
  title        = {Herpesvirus chemokine-binding glycoprotein G (gG) efficiently inhibits neutrophil chemotaxis in vitro and in vivo},
  url          = {http://www.jimmunol.org/cgi/content/abstract/179/6/4161},
  volume       = {179},
  year         = {2007},
}

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