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Specific binding of heat shock protein 70 with HN-protein inhibits the HN-protein assembly in Sendai virus-infected Vero cells
- Source :
-
Virus Research . Sep2006, Vol. 120 Issue 1/2, p199-207. 9p. - Publication Year :
- 2006
-
Abstract
- Abstract: The production of hemagglutinating virus of Japan (HVJ; Sendai virus) was inhibited at 41°C, whereas it was normal at 37°C. In the infected Vero cells, viral specific proteins were synthesized even at 41°C, but the synthesized HN protein was not integrated into the cell membrane, resulting in the inhibition of viral production. To investigate the relationship of HSP70 to the inhibition of HN-protein integration, the expression of HSP70 was induced by prostaglandin A1 (PGA1) at 37°C, and the influence on viral infection was examined. The induction of HSP70 at 37°C inhibited the viral production. Viral proteins were also synthesized, even in the presence of PGA1. However, HN protein was not as present on the cell membrane following PGA1-treatment as it was at 41°C, whereas F protein was detected. An immunoprecipitation assay showed that HSP70 was coprecipitated with HN protein, but not with F protein. The results suggested that the specific interaction of HSP70 with HN protein prevented the protein from integrating into the cell membrane. In addition, the abnormal virus-like particles, of which HN protein and nucleocapsid were ablated, were released in the culture medium at 41°C, although the size was smaller than the normal viral virions. The results suggest that HN protein is necessary for viral morphogenesis. [Copyright &y& Elsevier]
- Subjects :
- *SENDAI virus
*VIRAL replication
*HEAT shock proteins
*PROSTAGLANDINS
Subjects
Details
- Language :
- English
- ISSN :
- 01681702
- Volume :
- 120
- Issue :
- 1/2
- Database :
- Academic Search Index
- Journal :
- Virus Research
- Publication Type :
- Academic Journal
- Accession number :
- 21426274
- Full Text :
- https://doi.org/10.1016/j.virusres.2006.03.008