# Vimentin Dynamics in Viral Infection: Shield or Sabotage?

## TL;DR

This paper explores how the protein vimentin can both help and hinder viral infections, suggesting it as a potential target for antiviral treatments.

## Contribution

The paper introduces a novel perspective on vimentin's dual role in viral infection through structural and signaling insights.

## Key findings

- Vimentin disassembles into oligomers that act as viral co-receptors at the cell surface.
- Vimentin undergoes post-translational modifications and reassembles into structures that encapsulate viral replication complexes.
- Vimentin's role in viral infection is context-dependent, acting as both a shield and sabotage mechanism.

## Abstract

Vimentin is a type III intermediate filament protein that maintains cellular integrity, organelle positioning, and resilience to mechanical stress, but it is increasingly recognized for its dynamic change in viral infection. Viral infection causes vimentin filament disassembly into soluble oligomers with hydrophobic and acidic interfaces conducive to viral binding. These oligomers are recruited to the cell surface, where they act as viral co-receptors, facilitating viral attachment and entry. Upon entry, the viral protein induces post-translational modifications in intracellular vimentin filaments undergoing rearrangement processes, including disassembly into oligomers and then reassembly into cage-like structures that encapsulate viral replication complexes. Whether these structures promote viral replication or represent a host-imposed defense remains open. Our findings highlight the pro-viral “shield” and anti-viral “sabotage” role, a context-dependent role of vimentin during viral infection. Importantly, we offer a perspective encompassing structural biology and molecular and cellular signaling insights into vimentin dynamics, an approach that has not been explored in the current literature. We further propose that targeting vimentin is an innovative strategy for anti-viral intervention.