Ultrastructural organization of recombinant Marburg virus nucleoprotein: comparison with Marburg virus inclusions.
HeLa cells expressing the recombinant Marburg virus (MBGV) nucleoprotein (NP) have been studied by immunoelectron microscopy. It was found that MBGV NPs assembled into large aggregates which were in close association with membranes of the rough endoplasmic reticulum. Further analysis of these aggregates revealed that NPs formed tubule-like structures which were arranged in a hexagonal pattern. A similar pattern of preformed nucleocapsids was detected in intracellular inclusions induced by MBGV infection. Our data indicated that MBGV NP is able to form nucleocapsid-like structures in the absence of the authentic viral genome and other nucleocapsid-associated proteins.
Kolesnikova
L
L
State Scientific Research Center of Virology, Vector Institute of Molecular Biology, Laboratory of Ultrastructure, 633159 Koltsovo, Novosibirsk Region, Russia.
Mühlberger
E
E
Ryabchikova
E
E
Becker
S
S
D000818:Animals; D002522:Chlorocebus aethiops; D006367:HeLa Cells; D006801:Humans; D007181:Inclusion Bodies, Viral / Q000648:ultrastructure*; D029024:Marburgvirus / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure*; D016253:Microscopy, Immunoelectron; D019590:Nucleocapsid Proteins; D009698:Nucleoproteins / Q000235:genetics* / Q000378:metabolism / Q000648:ultrastructure*; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins / Q000378:metabolism / Q000648:ultrastructure; D012261:Ribonucleoproteins; D014709:Vero Cells; D014764:Viral Proteins
D019590:Nucleocapsid Proteins; D009698:Nucleoproteins; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins; D012261:Ribonucleoproteins; D014764:Viral Proteins; C073094:nucleoprotein, Marburg virus