Inactivation of vesicular stomatitis virus through inhibition of membrane fusion by chemical modification of the viral glycoprotein

Membrane fusion is an essential step in the entry of enveloped viruses into their host cells triggered by conformational changes in viral glycoproteins. We have demonstrated previously that modification of vesicular stomatitis virus (VSV) with diethylpyrocarbonate (DEPC) abolished conformational cha...

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Bibliographic Details
Published in:Antiviral research 2007-01, Vol.73 (1), p.31-39
Main Authors: Stauffer, Fausto, De Miranda, Joari, Schechter, Marcos C., Carneiro, Fabiana A., Salgado, Leonardo T., Machado, Gisele F., Da Poian, Andrea T.
Format: Article
Language:English
Subjects:
Animals
Antibiotics. Antiinfectious agents. Antiparasitic agents
Antiviral agents
Biological and medical sciences
Cricetinae
Diethyl Pyrocarbonate - pharmacology
Diethylpyrocarbonate
Disease Models, Animal
Humans
Medical sciences
Membrane fusion
Membrane Fusion - drug effects
Membrane Glycoproteins - chemistry
Membrane Glycoproteins - drug effects
Mice
Mice, Inbred BALB C
Pharmacology. Drug treatments
Vesicular stomatitis Indiana virus - drug effects
Vesicular stomatitis Indiana virus - pathogenicity
Vesicular stomatitis Indiana virus - physiology
Vesicular stomatitis virus
Viral Envelope Proteins - chemistry
Viral Envelope Proteins - drug effects
Viral inactivation
Virus Inactivation - drug effects
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Summary:Membrane fusion is an essential step in the entry of enveloped viruses into their host cells triggered by conformational changes in viral glycoproteins. We have demonstrated previously that modification of vesicular stomatitis virus (VSV) with diethylpyrocarbonate (DEPC) abolished conformational changes on VSV glycoprotein and the fusion reaction catalyzed by the virus. In the present study, we evaluated whether treatment with DEPC was able to inactivate the virus. Infectivity and viral replication were abolished by viral treatment with 0.5mM DEPC. Mortality profile and inflammatory response in the central nervous system indicated that G protein modification with DEPC eliminates the ability of the virus to cause disease. In addition, DEPC treatment did not alter the conformational integrity of surface proteins of inactivated VSV as demonstrated by transmission electron microscopy and competitive ELISA. Taken together, our results suggest a potential use of histidine (His) modification to the development of a new process of viral inactivation based on fusion inhibition.
ISSN:0166-3542
1872-9096
DOI:10.1016/j.antiviral.2006.07.007