Abstract
Using immunocytochemical procedures in conjunction with electron microscopy we have examined the distribution of the major DNA-binding protein (DBP) of herpes simplex virus (HSV) in infected nuclei. In embedded specimens, DBP was preferentially associated with fibrillar material of electron-translucent viral inclusions, and to a lesser extent with peripheral (marginated) host chromatin. The latter association was sensitive to a non-ionic detergent ('Photo flo'). In chromatin spread by the Miller technique, DBP was found to be a component of the 10 nm 'thick filaments' previously described in HSV infection.