Abstract
Antisera raised in rabbits against RK13 cells infected with herpes simplex virus type 1 were capable of specifically precipitating proteins synthesized after infection of BHK-21 cells with the virus. Analysis of these immune precipitates by polyacrylamide gel electrophoresis demonstrated 15 polypeptides with mol. wt. from 25 to 100000. A number of these polypeptides were not detected in purified preparations of virus particles.
Precipitates formed with two monoprecipitin antisera were also analysed. Antiserum to the structural antigen Band II precipitated a major polypeptide of mol. wt. 47000, which was glycosylated, and corresponded in mobility to a minor component polypeptide of the herpes virus particle. The other monoprecipitin antiserum, to the herpes-specified thymidine kinase, precipitated a polypeptide with a mol. wt. of 44000. The thymidine kinase polypeptide was not glycosylated.
* Present address: Committee on Virology, Department of Microbiology, University of Chicago, 939 East 57th St., Chicago, Illinois 60637, U.S.A.
† Present address: Department of Microbiology, School of Medicine, Leeds LS2 9NL, England.