Modification of cytoskeleton and prosome networks in relation to protein synthesis in influenza A virus-infected LLC-MK2 cells

Arcangeletti, Maria Cristina; Pinardi, Federica; Missorini, S.; Conto, Flora De; Conti, Stefania; Portincasa, P.; Scherer, Katharina M.; Chezzi, Carlo

doi:10.1016/s0168-1702(97)00074-9

Cited by 38 publications

(26 citation statements)

References 54 publications

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“…These can compromise the proteasome activity of cells and also be "remembered" by the cell via protein chaperones (26). IFs provide a scaffold for both protein chaperones (27) and the proteasome (28) as well as stress-activated kinases (29), linking the cellular machineries that refold damaged proteins and dispose of irreparable ones to stress signaling pathways (30). It has been through the study of specialized cells and their tissues that we have discovered these exciting aspects of IF function.…”

Section: Figurementioning

confidence: 99%

Functions of the intermediate filament cytoskeleton in the eye lens

Song¹,

Landsbury²,

Dahm³

et al. 2009

J. Clin. Invest.

143

105

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Intermediate filaments (IFs) are a key component of the cytoskeleton in virtually all vertebrate cells, including those of the lens of the eye. IFs help integrate individual cells into their respective tissues. This Review focuses on the lens-specific IF proteins beaded filament structural proteins 1 and 2 (BFSP1 and BFSP2) and their role in lens physiology and disease. Evidence generated in studies in both mice and humans suggests a critical role for these proteins and their filamentous polymers in establishing the optical properties of the eye lens and in maintaining its transparency. For instance, mutations in both BFSP1 and BFSP2 cause cataract in humans. We also explore the potential role of BFSP1 and BFSP2 in aging processes in the lens.

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Section: Figurementioning

confidence: 99%

Functions of the intermediate filament cytoskeleton in the eye lens

Song¹,

Landsbury²,

Dahm³

et al. 2009

J. Clin. Invest.

143

105

View full text Add to dashboard Cite

show abstract

“…Avalos et al [4] showed the association of vRNPs with actin microfilaments. However, another study [3] demonstrated that actin is not essential for vRNP transport as IFV replication was not affected by disruption of actin polymerization. In addition, there is evidence that vRNPs may be are transported to the plasma membrane through association with the cytoplasmic tails of HA and NA [24].…”

Section: Introductionmentioning

confidence: 98%

Influenza infection modulates vesicular trafficking and induces Golgi complex disruption

et al. 2016

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Influenza A virus (IFV) replicates its genome in the nucleus of infected cells and uses the cellular protein transport system for genome trafficking from the nucleus to the plasma membrane. However, many details of the mechanism of this process, and its relationship to subsequent cytoplasmic virus trafficking, have not been elucidated. We examined the effect of nuclear transport inhibitors Leptomycin B (LB), 5,6 dichloro-1-b-D-ribofuranosyl-benzimidazole (DRB), the vesicular transport inhibitor Brefeldin A (BFA), the caspase inhibitor ZWEHD, and microtubule inhibitor Nocodazole (NOC) on virus replication and intracellular trafficking of viral nucleoprotein (NP) from the nucleus to the ER and Golgi. Also, we carried out complementary studies to determine the effect of IFV on intracellular membranes. Inhibition of the CRM1 and TAP-P15 nuclear transport pathways by DRB and LB blocked completely the export of virus. Inhibition of vesicular trafficking by BFA, NOC, and ZWEHD also affected influenza infection. Interestingly, IFV infection induced fragmentation of the Golgi complex resulting in diffuse distribution of large and small vesicles throughout the cytoplasm. Live-cell microscopy revealed expansion of Golgi localization signals indicating progressive dispersion of Golgi positive structures, resulting in the disassembly of the Golgi ribbon structure. Other vesicular components (Rab1b, ARF1 and GBF1) were also found to be required for IFV infection. Furthermore, the exact step at which IFV infection disrupts vesicle trafficking was identified as the ER-Golgi intermediate compartment. These findings suggest that IFV NP is trafficked from the nucleus via the CRM1 and TAP pathways. IFV modulates vesicular trafficking inducing disruption of the Golgi complex. These studies provide insight on the ways in which IFV affects intracellular trafficking of different host proteins and will facilitate identification of useful pharmaceutical targets to abrogate virus replication.

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“…Cytoplasmic RNPs have been suggested to colocalize with microtubules (34), but although (like actin) tubulin has been found to copurify with RNPs and be present in virions (31,52), direct evidence for a role in trafficking is sparse. In general, pharmacologic interference with the cytoskeleton (after virus entry) has relatively slight effects on influenza A virus replication outside certain drugs that also interfere with viral protein synthesis (4,22,34,45,47,50,53). Thus, this aspect of the virus life cycle has many unresolved questions.…”

mentioning

confidence: 99%