Structural proteins of Herpesvirus saimiri

Analysis of herpesvirus saimiri structural proteins with monoclonal antibodies.

Herpesvirus saimiri is a lymphotrophic virus isolated from squirrel monkeys that causes highly malignant lymphomas in owl monkeys, marmosets, and rabbits, but not in its natural host. We have been interested in exploring immunological and biological aspects of this phenomenon and describe in this report the isolation of 27 monoclonal antibodies (MCAs) to herpesvirus saimiri which were grouped i...

Isolation and characterization of monoclonal antibodies to structural and nonstructural herpesvirus saimiri proteins.

An improved screening procedure was applied to identify hybridomas secreting antibodies to herpesvirus saimiri-specified polypeptides among the products of fusions between SP2/0 myeloma cells and spleen cells from mice immunized with purified virus particles or virus-specific DNA-binding proteins. Twenty-four monoclonal antibodies were isolated with specificities for 13 different virus-specifie...

Immediate-early transcription of Herpesvirus saimiri.

Transcription of Herpesvirus saimiri was characterized during the initial phases of productive infection by Northern blot analyses and hybridizations of radioactive cDNA with cloned fragments of virion L-DNA. Under conditions of immediate-early transcription, e.g., blocking of viral protein synthesis by cycloheximide, a single cytoplasmic polyadenylated viral RNA of 2.7 kilobases was found in i...

Preventive vaccination against Herpesvirus saimiri-induced neoplasia.

In this paper we discuss the use of Herpesvirus saimiri as a model for the development of vaccines against herpesvirus-induced neoplasia in primates. Attempts at protection against the oncogenicity of H. saimiri have centered on the inactivation of virus by heat and formalin, the production of temperature-sensitive H. saimiri mutants, and the attenuation of the virus. Each of these approaches h...

Characterization of proteins induced by Herpesvirus saimiri: comparative immunoprecipitation and analysis of glycosylation.