The diverse roles and dynamic rearrangement of vimentin during viral infection

Zhang, Yue; Wen, Zeyu; Shi, Xuemeng; Liu, Yanjun; Eriksson, John E.; Jiu, Yaming

doi:10.1242/jcs.250597

Cited by 51 publications

(56 citation statements)

References 125 publications

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“…The presence of vimentin has been reported to influence cell susceptibility to bacterial and viral pathogens, either in a positive or in a negative way, through various mechanisms, including behaving as an attachment factor at the cell membrane or influencing the replicative cycle [12,20,25,85,86]. Based on previous work on other coronaviruses, the potential role of vimentin in SARS-CoV-2 infection is currently a topic of interest [12,59,60], although the experimental evidence is so far limited.…”

Section: Discussionmentioning

confidence: 99%

Immunolocalization studies of vimentin and ACE2 on the surface of cells exposed to SARS-CoV-2 Spike proteins

Lalioti

González-Sanz

Lois-Bermejo

et al. 2021

Preprint

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The Spike protein from SARS-CoV-2 mediates docking of the virus onto cells and contributes to viral invasion. Several cellular receptors are involved in SARS-CoV-2 Spike docking at the cell surface, including ACE2 and neuropilin. The intermediate filament protein vimentin has been reported to be present at the surface of certain cells and act as a co-receptor for several viruses; furthermore, its potential involvement in interactions with Spike proteins has been proposed. Here we have explored the binding of Spike protein constructs to several cell types using low-temperature immunofluorescence approaches in live cells, to minimize internalization. Incubation of cells with tagged Spike S or Spike S1 subunit led to discrete dotted patterns at the cell surface, which showed scarce colocalization with a lipid raft marker, but consistent coincidence with ACE2. Under our conditions, vimentin immunoreactivity appeared as spots or patches unevenly distributed at the surface of diverse cell types. Remarkably, several observations including potential antibody internalization and adherence to cells of vimentin-positive structures present in the extracellular medium exposed the complexity of vimentin cell surface immunoreactivity, which requires careful assessment. Notably, overall colocalization of Spike and vimentin signals markedly varied with the cell type and the immunodetection sequence. In turn, vimentin-positive spots moderately colocalized with ACE2; however, a particular enrichment was detected at elongated structures positive for acetylated tubulin, consistent with primary cilia, which also showed Spike binding. Thus, these results suggest that vimentin-ACE2 interaction could occur at selective locations near the cell surface, including ciliated structures, which can act as platforms for SARS-CoV-2 docking.

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Section: Discussionmentioning

confidence: 99%

Immunolocalization studies of vimentin and ACE2 on the surface of cells exposed to SARS-CoV-2 Spike proteins

Lalioti

González-Sanz

Lois-Bermejo

et al. 2021

Preprint

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“…In recent years, there has been growing interest in the biological function of vimentin (Menko 2014;Cheng 2016;Ghosh 2018;Patteson 2019;Li and Kuemmerle 2020;Li 2020;Zhang 2020;Suprewicz 2021). As a multifunctional protein, vimentin is differentially expressed in diverse cell types, whereby it may also play a tissue-speci c function.…”

Section: Discussionmentioning

confidence: 99%

“…Interestingly, Su et al (Su 2019) also reported a positive role of vimentin in lymphocyte apoptosis, which may serve as a potential serum biomarker for sepsis prognosis. Moreover, vimentin has also been proposed as a possible cellular target for the treatment of coronavirus disease 19 (COVID-19) (Li 2020;Zhang 2020). Because vimentin is suggested as a co-receptor for the entry of SARS-CoV-2 into cells, drugs that decrease the expression of vimentin can be used to treat patients with COVID-19 (Yu 2016).…”

Section: Discussionmentioning

confidence: 99%

“…In recent years, there has been growing evidence that, during pathological condition such as tissue injury, in ammation, or cancers, vimentin could also be localized outside the cell (Yu 2018). These ndings demonstrate that VIM may be a potential diagnostic biomarker not only in cancer, but also in autoimmune disorders (e.g., Crohn's disease), viral infections (e.g., human immunode ciency virus (HIV)), and severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) (Fernandez-Ortega 2016;Yu 2016;Li and Kuemmerle 2020;Li 2020;Zhang 2020;Suprewicz 2021). As an IF protein, vimentin is expressed in many different cells and tissues with a diverse expression abundance.…”

Section: Introductionmentioning

confidence: 88%

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Pan-Cancer Analysis of VIM Expression in Human Cancer Tissues

Blatkiewicz

Białas

Taryma-Leśniak

et al. 2021

Preprint

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In 2020, more than 19 million cancer cases were diagnosed. One of the best paths to more effective treatment with a chance of being cured for patients is early detection. Vimentin (VIM), as an intermediate filament protein, is broadly expressed in mesenchymal cells. VIM is responsible for several biological processes such as cellular component organization and biogenesis, metabolic processes, and biological regulation. A growing body of literature indicates that expression of the VIM gene (VIM) is disrupted in carcinomas during epithelial–mesenchymal transition. Herein, we broadly analyzed the gene expression and promoter methylation profile of VIM in 19 cancer types across The Cancer Genome Atlas (TCGA). Furthermore, the protein–protein interactions (GeneMANIA and Search Tool for the Retrieval of Interacting Genes (STRING) database) and the alteration frequency of mutations (cBioPortal database) in VIM were analyzed. We proved that VIM is overexpressed in seven of the 19 studied cancer types. For two of them, we observed an association of VIM expression with gene promoter methylation. It must be emphasized that VIM overexpression can be a potential diagnostic biomarker in selected types of cancers.

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“…Vimentin is a major intermediate filament and provides a cytoplasmic scaffold for the organization and functions of cellular organelles, and other cellular processes such as cell spreading, migration and signal transduction [ 177 ]. In addition, vimentin has been reported to actively support viral infections [ 178 ]. FMDV 3A has been identified as a binding partner for vimentin from mass spectrometry analysis of proteins that co-purified with 3A (using an anti-3A antibody) from FMDV-infected primary fetal bovine kidney (FBK) cells [ 179 ].…”

Section: Interactions With Cellular Proteinsmentioning

confidence: 99%

Picornaviruses: A View from 3A

Jackson

Belsham

2021

Viruses

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Picornaviruses are comprised of a positive-sense RNA genome surrounded by a protein shell (or capsid). They are ubiquitous in vertebrates and cause a wide range of important human and animal diseases. The genome encodes a single large polyprotein that is processed to structural (capsid) and non-structural proteins. The non-structural proteins have key functions within the viral replication complex. Some, such as 3Dpol (the RNA dependent RNA polymerase) have conserved functions and participate directly in replicating the viral genome, whereas others, such as 3A, have accessory roles. The 3A proteins are highly divergent across the Picornaviridae and have specific roles both within and outside of the replication complex, which differ between the different genera. These roles include subverting host proteins to generate replication organelles and inhibition of cellular functions (such as protein secretion) to influence virus replication efficiency and the host response to infection. In addition, 3A proteins are associated with the determination of host range. However, recent observations have challenged some of the roles assigned to 3A and suggest that other viral proteins may carry them out. In this review, we revisit the roles of 3A in the picornavirus life cycle. The 3AB precursor and mature 3A have distinct functions during viral replication and, therefore, we have also included discussion of some of the roles assigned to 3AB.

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The diverse roles and dynamic rearrangement of vimentin during viral infection

Cited by 51 publications

References 125 publications

Immunolocalization studies of vimentin and ACE2 on the surface of cells exposed to SARS-CoV-2 Spike proteins

Immunolocalization studies of vimentin and ACE2 on the surface of cells exposed to SARS-CoV-2 Spike proteins

Pan-Cancer Analysis of VIM Expression in Human Cancer Tissues

Picornaviruses: A View from 3A

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