Varicella-Zoster Virus Infection Influences Expression and Organization of Actin and α-Tubulin but Does Not Affect Lamin A and Vimentin

Abstract

Objective: The aim of this study was to examine the effects of varicella-zoster virus (VZV) infection on the cytoskeletal components actin, lamin A, α-tubulin and vimentin. Methods: The expression patterns of these four proteins during VZV infection were studied by Northern and Western blotting. The filaments were also studied in their cellular environment by immunofluorescence using confocal microscopy. Treatment with nocodazole and cytochalasin B was performed to examine the effects of the destruction of actin or tubulin networks on the VZV replicative cycle. Results: The amounts of the mRNAs of actin, lamin A, α-tubulin and vimentin decreased slightly at 48 h post infection (p.i.) with VZV. The cellular content of the lamin A protein appeared to remain stable during the time period analyzed, whereas the amounts of actin, α-tubulin and vimentin decreased slightly at 24 h p.i. until the end of the viral cycle. Rearrangement of microfilaments and microtubules was observed at 24 h p.i. The addition of nocodazole or cytochalasin B decreased viral replication. Conclusions: During the VZV replicative cycle, tubulin and actin networks undergo significant changes including fiber elongation. If destroyed intentionally, viral replication is diminished, suggesting that these systems are vital for an efficient infection and viral replication.

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“…Furthermore, the actin cytoskeleton is a potential barrier to exocytosis [ 41 , 42 ], and the cortical actin network may provide a cellular barrier to SFV [ 43 ] and HIV [ 29 ]. PRRSV infection might potentially inhibit the cytoskeleton [ 44 - 46 ], to further promote virus spread in culture. In contrast to the finding with PRRSV, there was no difference between actin expression in LDV-permissive and LDV-non-permissive mouse macrophages.…”

Herpesviruses and Intermediate Filaments: Close Encounters with the Third Type

“…Irrespective of the mechanism used, herpesvirus entry usually leads to MF remodeling, accompanied or not by filament disassembly, while the structural integrity of MT is generally maintained to support capsid transport toward the nucleus [78–87]. Currently available data also point at a remarkable conservation of IF networks [83–85,88,89], suggesting that the integrity of this system may be required for viral entry. In a recent work, we tested this hypothesis using human fibroblasts and two different CMV strains, one entering cells by fusion at the plasma membrane (AD169) [90] and one expected to enter by fusion with both surface and vesicular membranes (TB40/E) [83].…”

Nuclear lamins: key regulators of nuclear structure and activities

“…Another member of the herpesviridae family that its replication affects lamin A is varicella-zoster virus. During varicella-zoster virus infection the amount of lamin A mRNA decreases but the cellular content of the protein appears to remain stable at 48 hrs after infection [217].…”