Objective:To observe the effect of spectral-domain OCT with different subfoveal choroidal areas on choroid vascular index (CVI) in normal healthy eyes.Methods:Retrospective clinical study. From October 2017 to May 2018, 174 eyes of 87 healthy people who visited in the Ophthalmology Department of Beijing Friendship Hospital and had no eye abnormalities were included in the study. All patients received single line scan of macular fovea by enhanced depth imaging OCT. After binary processing of the collected choroidal images, CVI as the center radius of 750, 1500, 3000 and 4500 μm were calculated. Repeated measurement analysis of variance was performed for comparison of CVI between groups.Results:The mean values of CVI in the 750, 1500, 3000 and 4500 μm groups were 0.681±0.003, 0.678±0.002, 0.677±0.002 and 0.676±0.002, respectively. The difference between the 750 μm group and the 4500 μm group was 0.005±0.002 ( P=0.009). The other pairwise comparison results showed no statistically significant difference ( P>0.05). Conclusion:The CVI is different in healthy eyes with the different distance from macular fovea.

In light of the scarcity of reports on the interaction between HSV-1 nucleocapsid protein UL25 and its host cell proteins,the purpose of this study is to use yeast two-hybrid screening to search for cellular proteins that can interact with the UL25 protein.C9orf69,a protein of unknown function was identified.The interaction between the two proteins under physiological conditions was also confirmed by biological experiments including co-localization by fluorescence and immunoprecipitation.A preliminary study of the function of C9orf69 showed that it promotes viral proliferation.Further studies showed that C9orf69 did not influence viral multiplication efficiency by transcriptional regulation of viral genes,but indirectly promoted proliferation via interaction with UL25.

An interaction between the HSV-1 UL25 capsid protein and cellular microtubule-associated protein was found using a yeast two-hybrid screen and β-D-galactosidase activity assays. Immunofluorescence microscopy of the UL25 protein demonstrated its co-localization with cellular microtubule-associated protein in the plasma membrane. Further investigations with deletion mutants suggest that UL25 is likely to have a function in the nucleus.