Antibody Inhibition of a Viral Type 1 Interferon Decoy Receptor Cures a Viral Disease by Restoring Interferon Signaling in the Liver

Type 1 interferons (T1-IFNs) play a major role in antiviral defense, but when or how they protect during infections that spread through the lympho-hematogenous route is not known. Orthopoxviruses, including those that produce smallpox and mousepox, spread lympho-hematogenously. They also encode a decoy receptor for T1-IFN, the T1-IFN binding protein (T1-IFNbp), which is essential for virulence. We demonstrate that during mousepox, T1-IFNs protect the liver locally rather than systemically, and that the T1-IFNbp attaches to uninfected cells surrounding infected foci in the liver and the spleen to impair their ability to receive T1-IFN signaling, thus facilitating virus spread. Remarkably, this process can be reversed and mousepox cured late in infection by treating with antibodies that block the biological function of the T1-IFNbp. Thus, our findings provide insights on how T1-IFNs function and are evaded during a viral infection in vivo, and unveil a novel mechanism for antibody-mediated antiviral therapy

Attemp of a more precise estimation of interlayer adhesion of lacquer coatings on wood

В труде определяли свободную поверхностную энергию обеих сторон лаковых оболочек, одна из которых была изготовлена в контакте с газовой, а другая - с твердной фазой. Работу адгезии исчисляли между подкладочной нитроцеллюлозным покрытием, поверхностными химоотверди- тельными покрытиями типа Пластлак и целлюлозо-уретановыми типа Цеюр, а также между лаковым покрытием и древесиной. Установлено, что значения работы адгезии исчисленные с учетом дифференциации свободной поверхностной энергии обеих сторон лаковых покрытий лучше характеризуют взаимодействие покрытий в лаковом покрытии и покрытия и древесины, чем значения работы адгезии исчисленные исключительно на основе свободной поверхностной энергии определяемой на поверхности образованной в контакте с газовой фазой. Работа адгезии между- слоями лакового покрытия более сильная, чем работа адгезии между лаковым покрытием и древесиной.A free surface energy of both sides of lacquer coatings, one of which was formed in the contact with gaseous and another with the solid phase is determined in the paper. The adhesion work was calculated between nitrocellulose ground and surface chemohardening coats of the Plastlak type and cellulose-urethan coats of the Celur type as well as between the lacquer coating and wood. It has been found that the adhesion work value calculated taking into consideration differentiation of the free surface energy of both sides of the lacquer coatings characterize better the interaction of coatings in the lacquer coat and coat with wood than the adhesion work values calculated exclusively on the basis of free surface energy determined for the area formed in the contact with the gaseous phase. Ihe adhesion work between lacquer coatings is higher than the adhesion work between lacquer coating and wood

Vaccinia Virus Blocks Gamma Interferon Signal Transduction: Viral VH1 Phosphatase Reverses Stat1 Activation

We have analyzed the effects of vaccinia virus (VV) on gamma interferon (IFN-γ) signal transduction. Infection of cells with VV 1 to 2 h prior to treatment with IFN-γ inhibits phosphorylation and nuclear translocation of Stat1 and consequently blocks accumulation of mRNAs normally induced by IFN-γ. While phosphorylation of other proteins in the IFN-γ pathway was not affected, activation of Stat1 by other ligand-receptor systems was also blocked by VV. This block of Stat1 activation was dose dependent, and although viral protein synthesis was not required, entry and uncoating of viral cores appear to be needed to block the accumulation of phosphorylated Stat1. These results suggest that a virion component is responsible for the effect. VV virions contain a phosphatase (VH1) that is sensitive to the phosphatase inhibitor Na(3)VO(4) but not to okadaic acid. Addition of Na(3)VO(4) but not okadaic acid restored normal Stat1 phosphorylation levels in VV-infected cells. Moreover, virions containing reduced levels of VH1 were unable to block the IFN-γ signaling pathway. In vitro studies show that the phosphatase can bind and dephosphorylate Stat1, indicating that this transcription factor can be a substrate for VH1. Our results reveal a novel mechanism by which VV interferes with the onset of host immune responses by blocking the IFN-γ signal cascade through the dephosphorylating activity of the viral phosphatase VH1