Abstract |
Semliki forest virus (SFV) was biosynthetically labeled with pyrene phospholipids and used to investigate two alternative routes of entry of SFV into BHK-21 cells: (1) receptor-mediated endocytosis followed by fusion of the viral envelope with the endosomal membrane and (2) direct fusion of SFV with the plasma membrane induced by low pH treatment. The selective inhibitor of the vacuolar proton- ATPase, concanamycin A, abolished fusion and subsequent infection only when the virus utilized the endocytic route to enter cells. The inhibitory effect of this macrolide antibiotic was bypassed by low pH treatment of cells. However, the ionophore nigericin was inhibitory irrespective of the route used by the virus to infect cells, suggesting the necessity of a transmembrane pH gradient for the entry process. According to our results, concanamycin A emerges as a suitable tool for selectively investigating the involvement of endosomal function in animal virus entry.
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Authors | A Irurzun, J L Nieva, L Carrasco |
Journal | Virology
(Virology)
Vol. 227
Issue 2
Pg. 488-92
(Jan 20 1997)
ISSN: 0042-6822 [Print] United States |
PMID | 9018148
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Anti-Bacterial Agents
- Antiviral Agents
- Macrolides
- Receptors, Virus
- Viral Envelope Proteins
- concanamycin A
- Nigericin
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Topics |
- Animals
- Anti-Bacterial Agents
(pharmacology)
- Antiviral Agents
(pharmacology)
- Cell Line
- Cricetinae
- Endocytosis
- Endosomes
(physiology, virology)
- Hydrogen-Ion Concentration
- Kidney
- Kinetics
- Macrolides
- Membrane Fusion
(drug effects)
- Nigericin
(pharmacology)
- Receptors, Virus
(physiology)
- Semliki forest virus
(drug effects, pathogenicity, physiology)
- Time Factors
- Viral Envelope Proteins
(metabolism)
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