Temperature Dependence of Fusion by Sendai Virus
Studies of the temperature dependence of liposome fusion by Sendai virus indicate that fusion occurs maximally at 55°C. The fusion capacity of the virus is also inactivated maximally by preincubation at this temperature and, under the same conditions, the F glycoprotein becomes resistant to proteoly...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 2000-05, Vol.271 (1), p.71-78 |
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| container_title | Virology (New York, N.Y.) |
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| creator | Wharton, S.A. Skehel, J.J. Wiley, D.C. |
| description | Studies of the temperature dependence of liposome fusion by Sendai virus indicate that fusion occurs maximally at 55°C. The fusion capacity of the virus is also inactivated maximally by preincubation at this temperature and, under the same conditions, the F glycoprotein becomes resistant to proteolysis. By analogy with the activation at elevated temperatures of fusion by influenza virus our results suggest that temperature is also a variable in the activation of fusion by paramyxoviruses and possibly in the activation of other members of the group of viruses that includes myxo-, paramyxo-, retro-, and filoviruses, which all contain cleaved, trimeric fusion glycoproteins. |
| doi_str_mv | 10.1006/viro.2000.0280 |
| format | Article |
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The fusion capacity of the virus is also inactivated maximally by preincubation at this temperature and, under the same conditions, the F glycoprotein becomes resistant to proteolysis. 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| ispartof | Virology (New York, N.Y.), 2000-05, Vol.271 (1), p.71-78 |
| issn | 0042-6822 1096-0341 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Animals Chick Embryo Electrophoresis, Polyacrylamide Gel Glycoproteins - metabolism Liposomes Membrane Fusion Respirovirus - physiology Sendai virus Temperature Viral Fusion Proteins - metabolism |
| title | Temperature Dependence of Fusion by Sendai Virus |
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