An egg-adapted strain of herpes simplex virus was used in a study of the neutralizing activity of human sera in the embryonated egg. These antigens differed in their particle size, rate of diffusion in agar, density, chromatographic behavior, electrophoretic mobility and susceptibility to the destructive effects of various physical and chemical agents. In the immunized animal peak titers are identical, but the course of infection is compressed into 8 to 10 days. It is suggested that corticosteroids may exert their harmful effect in this infection by interfering with normal reparative processes and with the structural integrity of the cornea. We have used GST pull-down-, surface plasmon resonance-, isothermal titration calorimetry and NMR chemical shift experiments to characterize interactions between Dreb2a and VP16, with the hMed25 and aMed25-ACIDs. In conclusion, our data demonstrate that both TK and TMPK activities encoded by HSV-1 share a common active site which is very tolerant in accepting modified nucleosides, but cannot readily accommodate modified nucleoside monophosphates. B bodies were formed in the majority of cells before the maturation of infectious virus, but the number of B bodies could not be correlated with the amount of virus in the cell or with the multiplicity of the inoculum.
The soluble antigen is relatively heat stable, and does not deteriorate on storage at 4 C. These results are in contradiction to those of most of the earlier workers, but in keeping with the recent reports of Flexner and Amoss.