Surface vimentin is critical for the cell entry of SARS-CoV

Yu, Yvonne Ting-Chun; Chien, Ssu-Chia; Chen, I-Yin; Lai, Chia-Tsen; Tsay, Yeou Guang; Chang, Shih‐Chieh; Chang, Shan‐Chwen

doi:10.1186/s12929-016-0234-7

Cited by 140 publications

(163 citation statements)

References 42 publications

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“…Secreted vimentin could also be detected in vitro in astrocyte-conditioned medium (Greco, Seeholzer, Mak, Spruce, & Ischiropoulos, 2010) and has been described for other cell types like macrophages and neutrophils (Moisan & Girard, 2006;Mor-Vaknin, Punturieri, Sitwala, & Markovitz, 2003). Functionally, extracellular vimentin is involved in binding to bacterial or viral pathogens (Ghosh et al, 2018;Yu et al, 2016). In the context of astrocyte-neuron interactions, it was shown that C-terminal residues of secreted vimentin can bind to the neuronal insulin-like growth factor 1 receptor, thereby stimulating its phosphorylation and axonal outgrowth of cultured neocortical neurons (Shigyo, Kuboyama, Sawai, Tada-Umezaki, & Tohda, 2015).…”

mentioning

confidence: 88%

Release of astroglial vimentin by extracellular vesicles: Modulation of binding and internalization of C3 transferase in astrocytes and neurons

Adolf

Rohrbeck

Münster-Wandowski

et al. 2018

Glia

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Clostridium botulinum C3 transferase (C3bot) ADP‐ribosylates rho proteins to change cellular functions in a variety of cell types including astrocytes and neurons. The intermediate filament protein vimentin as well as transmembrane integrins are involved in internalization of C3bot into cells. The exact contribution, however, of these proteins to binding of C3bot to the cell surface and subsequent cellular uptake remains to be unraveled. By comparing primary astrocyte cultures derived from wild‐type with Vim−/− mice, we demonstrate that astrocytes lacking vimentin exhibited a delayed ADP‐ribosylation of rhoA concurrent with a blunted morphological response. This functional impairment was rescued by the extracellular excess of recombinant vimentin. Binding assays using C3bot harboring a mutated integrin‐binding RGD motif (C3bot‐G89I) revealed the involvement of integrins in astrocyte binding of C3bot. Axonotrophic effects of C3bot are vimentin dependent and postulate an underlying mechanism entertaining a molecular cross‐talk between astrocytes and neurons. We present functional evidence for astrocytic release of vimentin by exosomes using an in vitro scratch wound model. Exosomal vimentin+ particles released from wild‐type astrocytes promote the interaction of C3bot with neuronal membranes. This effect vanished when culturing Vim−/− astrocytes. Specificity of these findings was confirmed by recombinant vimentin propagating enhanced binding of C3bot to synaptosomes from rat spinal cord and mouse brain. We hypothesize that vimentin+ exosomes released by reactive astrocytes provide a novel molecular mechanism constituting axonotrophic (neuroprotective) and plasticity augmenting effects of C3bot after spinal cord injury.

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mentioning

confidence: 88%

Release of astroglial vimentin by extracellular vesicles: Modulation of binding and internalization of C3 transferase in astrocytes and neurons

Adolf

Rohrbeck

Münster-Wandowski

et al. 2018

Glia

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“…Moreover, VP1 caused the vimentin rearrangement in astrocyte cells, facilitating virus infection in the CNS (Haolong et al 2013). In the consideration that endothelial cells, vimentin is utilized by various viruses, including at least cowpea mosaic virus (Koudelka et al 2009), dengue virus (Yang et al 2016), and severe acute respiratory syndrome coronavirus (Yu et al 2016), we speculated that VP1 may exploit endothelial cells and vimentin. In the accordance with the above speculation, VP1 activated TGF-β/Smad-3/NF-κB pathways, leading to the increased expression of vimentin in brain endothelial cells.…”

Section: Discussionmentioning

confidence: 99%

Enterovirus A71 capsid protein VP1 increases blood–brain barrier permeability and virus receptor vimentin on the brain endothelial cells

et al. 2019

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Enterovirus A71 (EV-A71) is the major cause of severe hand-foot-and-mouth diseases (HFMD), especially encephalitis and other nervous system diseases. EV-A71 capsid protein VP1 mediates virus attachment and is the important virulence factor in the EV-A71pathogenesis. In this study, we explored the roles of VP1 in the permeability of blood-brain barrier (BBB). Sera albumin, Evans blue, and dextran leaked into brain parenchyma of the 1-week-old C57BL/6J mice intracranially injected with VP1 recombinant protein. VP1 also increased the permeability of the brain endothelial cells monolayer, an in vitro BBB model. Tight junction protein claudin-5 was reduced in the brain tissues or brain endothelial cells treated with VP1. In contrast, VP1 increased the expression of virus receptor vimentin, which could be blocked with VP1 neutralization antibody. Vimentin expression in the VP1-treated brain endothelial cells was regulated by TGF-β/Smad-3 and NF-κB signal pathways. Moreover, vimentin over-expression was accompanied with compromised BBB. From these studies, we conclude that EV-A71 virus capsid protein VP1 disrupted BBB and increased virus receptor vimentin, which both may contribute to the virus entrance into brain and EV-A71 CNS infection.

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“…Vimentin is part of a cytoskeleton structure that has the role of a receptor for virus entering the cell, especially as a viral receptor or attachment receptor. For example, the direct interaction between vimentin and SARS-CoV spike protein during viral entry and as the virus enters the receptor (Yu et al, 2016). Cell surface vimentin is an attachment receptor for enterovirus 7 and increases the infectivity of EV71 (Du et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

Vimentin modulates infectious porcine circovirus type 2 in PK-15 cells

Wang

Song

et al. 2018

Virus Research

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Porcine circovirus type 2 (PCV2) is the pathogen that causes postweaning multisystemic wasting syndrome, which leads to significant economic losses for swine farms worldwide. However, the infection mechanism of PCV2 is not completely understood yet. Vimentin is a part of the cytoskeleton network and plays an important role in several virus infections. It is not clear whether vimentin has a role in PCV2 infection nor how it affects PCV2 infection. In this study, the function of vimentin in PK-15 cells infected with PCV2 has been elucidated. We found that vimentin had a restrictive effect on the replication of PCV2 in PK-15 cells. Overexpression of vimentin by transferred pCAGGS-vimentin and down-regulation by the respective scrambled small interfering RNA showed that vimentin restricted the replication and virion production of PCV2. A special interaction between vimentin and PCV2 Cap protein was observed using laser confocal microscopy and immunoprecipitation assay. Moreover, overexpression of vimentin could decrease NF-κB activity and increase PCV2-induced caspase-3 activity in PK-15 cells. These data suggest that vimentin is involved in the replication of PCV2 and has a restrictive effect on it, which is helpful in the study of the replication mechanism of PCV2.

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Surface vimentin is critical for the cell entry of SARS-CoV

Cited by 140 publications

References 42 publications

Release of astroglial vimentin by extracellular vesicles: Modulation of binding and internalization of C3 transferase in astrocytes and neurons

Release of astroglial vimentin by extracellular vesicles: Modulation of binding and internalization of C3 transferase in astrocytes and neurons

Enterovirus A71 capsid protein VP1 increases blood–brain barrier permeability and virus receptor vimentin on the brain endothelial cells

Vimentin modulates infectious porcine circovirus type 2 in PK-15 cells

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