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PMID: 2032551 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Effects of Brefeldin A on the Golgi complex, endoplasmic reticulum and viral envelope glycoproteins in murine erythroleukemia cells.

European journal of cell biology ·Vol. 54 ·No. 1 ·1991-02-00 ·Pages 38-54

Ulmer JB, Palade GE

Abstract

This report concerns the effects of Brefeldin A (BFA): i) on the Golgi complex and the ER of retrovirus-transformed murine erythroleukemia (MEL) cells and, ii) on the viral proteins these cells express. Golgi complexes were extensively disorganized by BFA. Within 5 min, most stacked cisternae were converted to vesicles scattered throughout the centrosphere region. By 30 min, the Golgi complexes were completely disassembled. Only clusters of small vesicles ("Golgi remnants") persisted in the vicinity of the centrioles and microtubule-organizing centers. Some of these small vesicles had a simple coat structure on their membranes. Over the next 1 to 2 h of BFA treatment, the number of vesicles in the Golgi area decreased concomitantly with the expansion of a predominantly smooth membrane portion of the ER, consisting of a network of dilated tubules in continuity with regular RER cisternae, annulate lamellae and the nuclear envelope. By electron microscopy, viral glycoproteins appeared to accumulate on the membranes of this network, and immature virions were found to bud preferentially into its cisternal space. Viral accumulations increased with time under BFA. The rest of the RER appeared normal, apparently unaffected by the drug. Preferential virion budding suggests that this expanding network is a chemically differentiated part of the ER. By immunofluorescence, antibodies to viral envelope proteins gave a punctate staining at the surface of control cells, presumably in the areas of virion budding, whereas relatively large intracellular masses of antigens were found in BFA-treated cells. We assume that these masses represent the differentiated parts of the ER. Taken together, these findings suggest that BFA blocks intracellular transport of newly synthesized cellular and viral proteins immediately distal to the distinct compartment of the ER in which virion budding preferentially occurs. BFA effects are rapidly and fully reversible. Within 1 min of the removal of the drug, stacks of Golgi cisternae began to reappear in the vicinity of the centrioles, and by 30 min, Golgi complexes regained their normal structural appearance.

MeSH Terms
Animals Antiviral Agents/pharmacology Brefeldin A Cyclopentanes/pharmacology Endoplasmic Reticulum/drug effects,metabolism,ultrastructure Golgi Apparatus/drug effects,metabolism,ultrastructure Leukemia, Erythroblastic, Acute Mice Microscopy, Electron Retroviridae/drug effects,metabolism Tumor Cells, Cultured Viral Envelope Proteins/drug effects,metabolism,ultrastructure
Chemicals
Antiviral Agents Cyclopentanes Viral Envelope Proteins Brefeldin A
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ulmer J B
Department of Cell Biology, Yale University School of Medicine, New Haven, CT.
Palade G E
Article Info
Journal
European journal of cell biology
Abbr.
Eur J Cell Biol
ISSN
0171-9335
Published
1991-02-00
Pages
38-54
Language
English
Region
Germany
NLM ID
7906240
Subset
IM
Grants
NCI NIH HHS · 1 PO1 CA 46128-01 · United States
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