Appearance of host-specific nucleolar proteins in intranuclear "dense bodies" following herpes simplex infection.
Nucleolar modifications induced by herpes simplex virus type 1 (HSV1) infection were studied at the ultrastructural level with special attention to the fate of a family of proteins serologically related to the nucleolar 100 kDa protein. Immunocytochemical techniques revealed that antigenic sites related to these proteins were associated with nucleoli in a pattern similar to that observed with non-infected cells. In addition, the "dense bodies" induced by HSV infection were heavily decorated by antibodies to the 100 kDa protein. Neither DNA nor RNA was detectable in the latter by cytochemical techniques. Therefore, it appears that "dense bodies" are exclusively proteinaceous and contain at least one host protein implicated in ribosomal RNA synthesis. An accumulation of 100 kDa protein in extra-nucleolar structures might account for previously reported defects in ribosomal RNA expression during HSV infection.
Puvion-Dutilleul
F
F
Pichard
E
E
Sheldrick
P
P
Amalric
F
F
Puvion
E
E
D000818:Animals; D001345:Autoradiography; D002467:Cell Nucleus / Q000032:analysis / Q000648:ultrastructure*; D002478:Cells, Cultured; D005347:Fibroblasts / Q000378:metabolism / Q000648:ultrastructure; D006561:Herpes Simplex / Q000378:metabolism* / Q000473:pathology; D008854:Microscopy, Electron; D008970:Molecular Weight; D009687:Nuclear Proteins; D009697:Nucleolus Organizer Region / Q000032:analysis / Q000378:metabolism* / Q000648:ultrastructure; D000090243:Nucleophosmin; D011817:Rabbits; D012261:Ribonucleoproteins / Q000032:analysis / Q000378:metabolism*; D013194:Staining and Labeling
D009687:Nuclear Proteins; D012261:Ribonucleoproteins; D000090243:Nucleophosmin