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Details on Person Using a reassortant rotavirus A (RV-A) between the human str...
| Class:Id | Summation:9976696 |
|---|---|
| _displayName | Using a reassortant rotavirus A (RV-A) between the human str... |
| _timestamp | 2025-12-15 14:05:27 |
| created | [InstanceEdit:9976698] Orlic-Milacic, Marija, 2025-12-12 |
| literatureReference | [LiteratureReference:9976700] Dissecting rotavirus particle-raft interaction with small interfering RNAs: insights into rotavirus transit through the secretory pathway [LiteratureReference:9976745] Assembly of highly infectious rotavirus particles recoated with recombinant outer capsid proteins [LiteratureReference:9976765] Interactions of rotavirus VP4 spike protein with the endosomal protein Rab5 and the prenylated Rab acceptor PRA1 [LiteratureReference:9976825] Spike protein VP4 assembly with maturing rotavirus requires a postendoplasmic reticulum event in polarized caco-2 cells [LiteratureReference:9976859] Silencing the morphogenesis of rotavirus |
| modified | [InstanceEdit:9976749] Orlic-Milacic, Marija, 2025-12-13 [InstanceEdit:9976777] Orlic-Milacic, Marija, 2025-12-13 [InstanceEdit:9976827] Orlic-Milacic, Marija, 2025-12-14 [InstanceEdit:9976863] Orlic-Milacic, Marija, 2025-12-15 |
| text | Using a reassortant rotavirus A (RV-A) between the human strain D and simian strain RRV, it was shown that the budding of double layer particles (DLP) into the ER is dependent on NSP4, as siRNA-mediated silencing of NSP4 expression results in accumulation of DLPs in the cytoplasm/viroplasm (Cuadras et al. 2006). The manner of entry of VP4 into the ER remains undetermined. During in vitro assembly of the rotavirus virions from recombinant RRV proteins expressed in Sf9 insect cells, NSP4 is not required as a chaperone (Trask and Dormitzer 2006). VP4 does not co-elute with DLPs and the propensity of VP4 to oligomerize and form trimers in the absence of other structural components of the virion is weak, suggesting that any cytosolic interaction between VP4 and DLPs is also weak and does not provide a clear explanation for the entry of VP4 into the ER (Trask and Dormitzer 2006). The fact that, during in vitro assembly, VP4 has to be added to the mixture before VP7 is added supports incorporation of VP4 into virions during ER assembly (Trask and Dormitzer 2006). The reported interaction between free cytosolic VP4, RAB5, and prenylated RAB acceptor RABAC1 (also known as PRA1) may be involved in homeostasis of free VP4 and regulation of its localization (Enouf et al. 2003). The localization of VP4 to the ER was not detectable in the study by Delmas et al. 2004. In the study by Lopez et al. 2005, VP4 was reported to partially localize to the perinuclear region, which overlaps with ER localization, and this localization of VP4 is lost upon NSP4 silencing by siRNA. The loss of VP4 perinuclear localization is similar to the loss of VP6 perinuclear localization upon NSP4 knockdown (Lopez et al. 2005: RRV was used), which suggests that NSP4 may promote translocation of VP4 to the ER either directly, or indirectly through VP6. |
| (summation) | [BlackBoxEvent:9976573] RV-A DLPs bud into rough endoplasmic reticulum [Homo sapiens] |
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