Abstract |
Translocation of baculovirus nucleocapsids (45 nm in diameter, approximate length of 280-300 nm) from nucleoplasm to cytoplasm was studied morphologically using cryofixation and gold labeled wheat germ agglutinin ( WGA-gold) during recombinant Autographa californica nuclear polyhedrosis virus infection in Sf9 cells. Nucleocapsids formed in the nucleoplasm migrated into protrusions of the nuclear envelope, but not into nuclear pore complexes. We found cross-like membranous structures. Small pores seemed to be in the protruding nuclear double membranes. The middle piece of a nucleocapsid was located within the small pore whereas the upper part was in the cytoplasm. Other nucleocapsids were situated within pores without colocalization of WGA-gold in the nuclear envelope. These results suggest that baculovirus nucleocapsids use small pores in the nuclear-derived membranes or incomplete nuclear pores in the nuclear envelope to migrate from the nucleoplasm to the cytoplasm, but not complete nuclear pore complexes proper.
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Authors | T Nishimura, D Favre, M Dürrenberger, M R Michel, I Ichihara, H Koblet |
Journal | Okajimas folia anatomica Japonica
(Okajimas Folia Anat Jpn)
Vol. 71
Issue 2-3
Pg. 83-97
(Aug 1994)
ISSN: 0030-154X [Print] Japan |
PMID | 7808726
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Gold Colloid
- Recombinant Proteins
- Wheat Germ Agglutinins
- wheat germ agglutinin-gold
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Topics |
- Animals
- Capsid
(metabolism)
- Cell Line
- Cell Membrane
(metabolism, ultrastructure, virology)
- Cell Nucleus
(metabolism, ultrastructure, virology)
- Cryopreservation
- Cytoplasm
(metabolism, ultrastructure, virology)
- Gold Colloid
- Microscopy, Electron
- Nuclear Envelope
(metabolism, ultrastructure, virology)
- Nucleopolyhedroviruses
(chemistry, physiology, ultrastructure)
- Recombinant Proteins
(metabolism)
- Spodoptera
- Wheat Germ Agglutinins
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