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Robust time-resolved volumetric imaging studies of intracellular dynamics of viral and host proteins have been limited due to competing requirements on imaging speed, photodamage, and spatial resolution using conventional confocal microscopy. These data suggest a reduction in Rab11A–vRNP association and the existence of an alternative, Rab11A and microtubule-independent, mode of transport for vRNP segments. Intriguingly, using FISH and immunostaining in fixed cells, we have observed a marked decrease in diffraction-limited colocalization between Rab11A and vRNP in the absence of an intact microtubule network 22. We and others have shown that depolymerization of the microtubule network fails to significantly abrogate viral replication 13, 21, 22. Thus, IAV vRNP segments are thought to transport to the plasma membrane along cytoskeletal filaments via Rab11A-RE, but the details of transport to the viral budding sites are poorly understood. Rab11-FIPs can associate with both actin and microtubule-associated motor proteins, indicating that Rab11A-RE can use multiple cytoskeletal networks for transport 17, 18, 19, 20. Rab11A recruits various molecular motors to RE through interactions with its corresponding family interacting proteins (Rab11-FIPs) 16. Rab11A specifically marks recycling endosomes (RE), which sort and transport cargo slated for release from the apical cell membrane 14, 15. Intracellular transport of vRNP from the nucleus to the plasma membrane is thought to be mediated by Rab11A, a host-cell small GTPase 9, 10, 11, via direct protein–protein interaction with the PB2 subunit of the polymerase 12, 13. We and others have used immunostaining and fluorescence in situ hybridization (FISH) to demonstrate that vRNP segments are sequentially assembled in the cytoplasm on their way to the plasma membrane 7, 8. Together, the RNA, NP scaffold, and viral polymerase form one viral ribonucleoprotein complex (vRNP) per segment 6. Viral RNA is bound by the virally encoded nucleoprotein (NP) and the heterotrimeric viral polymerase, composed of PA, PB1, and PB2, at the 5′ and 3′ ends to form a pan-handle structure. The segmented genome requires assembly of all eight segments prior to release of progeny virions from the plasma membrane of an infected cell 3, 4, 5. Replication of each IAV genome segment occurs in the nucleus independently of each other 1, 2. Influenza A virus (IAV) is a negative-strand RNA virus with a segmented genome. The mechanism of altered Rab11A movement is likely related to a decrease in dynein motors bound to Rab11A vesicles during IAV infection.
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Using two-color imaging we demonstrate co-transport of Rab11A and IAV vRNA in infected cells and provide direct evidence that vRNA-associated Rab11A have altered transport. Unexpectedly, infection with respiratory syncytial virus alters Rab11A motion in a manner opposite to IAV, suggesting that Rab11A is a common host component that is differentially manipulated by respiratory RNA viruses. Here, using high spatiotemporal resolution light-sheet microscopy (~1.4 volumes/second, 330 nm isotropic resolution), we quantify Rab11A and vRNA movement in live cells during IAV infection and report that IAV infection decreases speed and increases arrest of Rab11A. Rab11A-containing recycling endosomes have been identified as a platform for intracellular transport of viral RNA (vRNA). Assembly of infectious influenza A viruses (IAV) is a complex process involving transport from the nucleus to the plasma membrane.