Ultrastructural analysis of the interaction between F-actin and respiratory syncytial virus during virus assembly.
During respiratory syncytial virus (RSV) infection there is a close physical interaction between the filamentous actin (F-actin) and the virus, involving both inclusion bodies and the virus filaments. This interaction appears to occur relatively early in the replication cycle, and can be detected from 8 h post-infection. Furthermore, during virus assembly we obtained evidence for the participation of an F-actin-associated signalling pathway involving phosphatidyl-3-kinase (PI3K). Treatment with the PI3K inhibitor LY294002 prevented the formation of virus filaments, although no effect was observed either on virus protein expression, or on trafficking of the virus glycoproteins to the cell surface. Inhibition of the activity of Rac GTPase, a down-stream effector of PI3K, by treatment with the Rac-specific inhibitor NSC23766 gave similar results. These data suggest that an intimate interaction occurs between actin and RSV, and that actin-associated signalling pathway, involving PI3K and Rac GTPase, may play an important role during virus assembly.
Jeffree
Chris E
CE
School of Biological Sciences, Daniel Rutherford Building, King's Buildings, Mayfield Road, University of Edinburgh Edinburgh, EH9 3JH, UK.
Brown
Gaie
G
Aitken
Jim
J
Su-Yin
Dawn Yeo
DY
Tan
Boon-Huan
BH
Sugrue
Richard J
RJ
D000199:Actins / Q000502:physiology*; D000634:Aminoquinolines / Q000494:pharmacology; D002460:Cell Line; D002867:Chromones / Q000494:pharmacology; D003599:Cytoskeleton / Q000648:ultrastructure / Q000821:virology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006801:Humans; D007181:Inclusion Bodies, Viral / Q000502:physiology / Q000648:ultrastructure; D008855:Microscopy, Electron, Scanning; D046529:Microscopy, Electron, Transmission; D009025:Morpholines / Q000494:pharmacology; D019869:Phosphatidylinositol 3-Kinases / Q000502:physiology; D000081082:Phosphoinositide-3 Kinase Inhibitors; D011743:Pyrimidines / Q000494:pharmacology; D018113:Respiratory Syncytial Virus, Human / Q000502:physiology* / Q000648:ultrastructure*; D015398:Signal Transduction; D019065:Virus Assembly / Q000502:physiology*; D020744:rac GTP-Binding Proteins / Q000037:antagonists & inhibitors / Q000502:physiology