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A protein encoded by the B8R open reading frame of vaccinia virus. B8R possesses a hydrophobic amino-terminal signal sequence but lacks a discernible membrane anchor domain, suggesting that the proteins may be secreted. B8R has sequence similarity to the extracellular binding domain of cellular IFN-gamma receptors and binds IFN-gamma.

Expression of the B8R gene appears to affect virulence. In rabbits, skin lesions produced by virus mutants lacking B8R are smaller and tend to disappear earlier than those caused by wild-type virus (Sroller et al, 2001). Vaccinia virus vectors with an inactivated B8R gene are attenuated in vivo without a concomitant reduction in immunogenicity (Verardi et al, 2001). The IFN-gamma soluble receptors encoded by vaccinia virus, cowpox virus, and camelpox virus bind and inhibit the biological activity of human, bovine, rat, chicken IFN-gamma but not mouse IFN-gamma (Alcami and Smith, 1995; Puehler et al, 1998).

For another protein encoded by the vaccinia virus genome encoding a receptor for IFN see also: B18R.

For another protein with functions of cytokines, encoded by the vaccinia virus genome, see also: B15R, VVGF. For other virus-encoded proteins with immunomodulatory/immune evasion activities and/or functions of cytokines or cytokine receptors see also the Virulence Factors Dictionary section of this encyclopedia. For other examples of microbial or parasitic gene products interfering with host cell functions see also: Modulins.

Copyright 2012 by H IBELGAUFTS. All rights reserved.


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