Herpesvirus infections have already been developed for use in horses, and for the prevention of the closely related BTV in sheep. Vaccination of horses with recombinant MVA based vectors has also been shown to be an effective means of inducing protective immunity to influenza virus infection. Wnt signaling plays key roles in embryogenesis and in adult tissue homeostasis of metazoan animals. The extracellular Wnt signal stimulates numerous intracellular signal transduction cascades, including the canonical Wnt/b-catenin pathway, which regulates gene expression in the nucleus, and a number of noncanonical pathways, which regulate many other aspects of cell biology including cell migration, adhesion, and polarity. Mutations of the genes involved in Wnt signaling cause congenital defects in humans, and inappropriate activation of the Wnt/b-catenin pathway has been linked to the development of human cancer. An increasing number of studies have shown that Wnt/b-catenin signaling regulates the self-renewal and differentiation of adult stem cells, raising the possibility that this process is subverted in cancer. Activation of the Wnt/b-catenin pathway is initiated by the binding of Wnt proteins to cell surface receptors composed of a member of the Frizzled protein family and one of the two lowdensity lipoprotein receptor-related proteins, LRP5 or LRP6. Signaling from Wnt receptors leads to inactivation of a cytoplasmic protein complex that normally catalyzes the phosphorylation and subsequent destruction of b-catenin. A recent study comparing recombinant canarypox and MVA vectors has demonstrated that antigen production by recombinant MVA was greater than that from recombinant canarypox virus in certain mammalian cell lines and primary human cells tested. Apart from the localization of PLEKHA7 in the outer limiting membrane of the retina, which contains heterotypic junctions between glial and neuronal cells, our observations suggest that the distribution of PLEKHA7 is essentially confined to epithelial junctions. The lack of PLEKHA7 labeling in heart intercalated disks, that contain cadherin and afadin was unexpected, considering that PLEKHA7 mRNA and protein were detected in heart tissue by northern and western blotting. One possibility to explain this observation is that the epitopes recognized by our antibodies are NVP-BKM120 molecular weight modified in heart tissue, in a way that negatively affects immunofluorescent labeling. In summary, our observations indicate that PLEKHA7 is an AJ protein with a unique combination of subcellular localization and tissue distribution, since it is absent from puncta adherentia along the lateral walls of epithelial cells, and its pattern of tissue distribution is different from that of afadin. This observation was primarily due to a longer duration of antigen production in recombinant MVA-infected cells.