The profiles of soluble cytokine receptors and cytokines in patients with VRL were different from those with uveitis. In addition, sVEGFR1 and sVEGFR2 levels may be differential diagnostic markers between PVRL/PCNSL and SMRL, and sIL-2Rα levels can anticipate infiltration of VRL cells into the subretina and/or retina.

Ocular herpes, caused by herpes simplex virus type 1 (HSV‐1) and type 2 (HSV‐2) infections, remains an important corneal disease, which may result in loss of vision. Because the frequency of acyclovir resistance in HSV has increased, novel antiviral agents are needed for therapeutic approaches to ocular herpes. Several studies have demonstrated that fusion proteins containing entire ectodomain of HSV glycoprotein D receptors, including herpesvirus entry mediator A (HVEM), nectin‐1 and nectin‐2, and the Fc portion of human IgG (HVEMIg, nectin‐1Ig, and nectin‐2Ig, respectively), can exert antiviral effects in vitro and in vivo. Here, to evaluate the antiviral potential of HVEMIg, nectin‐1Ig, and nectin‐2Ig against ocular infections with HSV, transgenic mice expressing these fusion proteins were ocularly inoculated with HSV‐1 and HSV‐2. Transgenic mouse lines expressing HVEMIg and nectin‐1Ig showed marked resistance to ocular herpes; on the other hand, mouse lines expressing nectin‐2Ig did not. Furthermore, to investigate the therapeutic effects of nectin‐1Ig, which can neutralize HSVs in vitro against ocular disease, transgenic mouse serum containing nectin‐1Ig was dropped into the eyes of wild‐type mice after HSV infection. Reduction of severe symptoms could be observed in mice treated with nectin‐1Ig serum. These results warrant further study of soluble HVEM and nectin‐1 products as preventive and therapeutic agents against ocular herpes caused by HSV‐1 and HSV‐2 infections, especially nectin‐1Ig as a new eye drop.

Murine gammaherpesvirus (MHV) 68, a natural pathogen of field mice, is related to human gammaherpesviruses, Epstein-Barr virus (EBV; human herpesvirus 4) and Kaposi's sarcomaassociated herpesvirus (KSHV; human herpesvirus 8). The ORF35 of MHV-68 and its homologues of EBV and KSHV are located in the gene cluster composed of ORF34-ORF38 in which each gene overlaps with adjacent genes. Although MHV-68 ORF35 was reported to be an essential gene, its function during infection is presently unknown. In this study, we show, by analysing ORF35-transfected cells, that three serine residues in the C terminus are responsible for the phosphorylation and that the ORF35 protein forms homo-oligomers via a predicted coiled-coil motif. The ORF35 protein expressed by transfection was preferentially located in the cytoplasm of cells uninfected or infected with MHV-68. The recombinant virus lacking ORF35 (35S virus) exhibited genome replication and expression of lytic proteins comparable to those of the WT virus, but reduced levels of virus production, suggesting that the ORF35 protein acts at the virion assembly and/or egress step. Lytic replication in the lung after intranasal infection and the frequency of ex vivo reactivation from latency after intraperitoneal infection were lower in 35S virus-infected mice than in mice infected with the WT or marker-reverted virus. Our results indicate that ORF35 is not essential for MHV-68 lytic replication, but plays an important role in efficient viral replication and reactivation from latency.