Endothelial Targeting of Cowpea Mosaic Virus (CPMV) via Surface Vimentin

Koudelka, Kristopher J.; Destito, Giuseppe; Plummer, Emily M.; Trauger, Sunia A.; Siuzdak, Gary; Manchester, Marianne

doi:10.1371/journal.ppat.1000417

Cited by 167 publications

(202 citation statements)

References 49 publications

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“…It is involved in the process of viral entry of cowpea mosaic virus (17) and Japanese encephalitis virus (18) and in the viral egress of bluetongue virus (19). It has also been implicated in the process of viral replication of vaccinia virus (20) and dengue virus (21).…”

mentioning

confidence: 99%

Foot-and-Mouth Disease Virus Modulates Cellular Vimentin for Virus Survival

Gladue

O’Donnell

Baker-Branstetter

et al. 2013

J Virol

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Foot-and-mouth disease virus (FMDV), the causative agent of foot-and-mouth disease, is an Aphthovirus within the Picornaviridae family. During infection with FMDV, several host cell membrane rearrangements occur to form sites of viral replication. FMDV protein 2C is part of the replication complex and thought to have multiple roles during virus replication. To better understand the role of 2C in the process of virus replication, we have been using a yeast two-hybrid approach to identify host proteins that interact with 2C. We recently reported that cellular Beclin1 is a natural ligand of 2C and that it is involved in the autophagy pathway, which was shown to be important for FMDV replication. Here, we report that cellular vimentin is also a specific host binding partner for 2C. The 2C-vimentin interaction was further confirmed by coimmunoprecipitation and immunofluorescence staining to occur in FMDV-infected cells. It was shown that upon infection a vimentin structure forms around 2C and that this structure is later resolved or disappears. Interestingly, overexpression of vimentin had no effect on virus replication; however, overexpression of a truncated dominant-negative form of vimentin resulted in a significant decrease in viral yield. Acrylamide, which causes disruption of vimentin filaments, also inhibited viral yield. Alanine scanning mutagenesis was used to map the specific amino acid residues in 2C critical for vimentin binding. Using reverse genetics, we identified 2C residues that are necessary for virus growth, suggesting that the interaction between FMDV 2C and cellular vimentin is essential for virus replication.

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confidence: 99%

Foot-and-Mouth Disease Virus Modulates Cellular Vimentin for Virus Survival

Gladue

O’Donnell

Baker-Branstetter

et al. 2013

J Virol

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“…Vimentin and several of the other proteins identified in this study are known autoantigens associated with rheumatoid arthritis (Table 2) (38 -40). Cell surface vimentin is a target for picornaviruses (41) and bacterial pathogens, including the Escherichia coli virulence factor IbeA (42), and necrotizing Group A Streptococci (43,44). Remarkably, in the latter studies, the extracellular vimentin form that associated with Streptococci was a fragment FIGURE 8.…”

Section: Discussionmentioning

confidence: 96%

A Plasma Membrane Wound Proteome

Mellgren

2010

Journal of Biological Chemistry

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Cells in mechanically active tissues undergo constant plasma membrane damage that must be repaired to allow survival. To identify wound-associated proteins, a cell-impermeant, thiolreactive biotinylation reagent was used to label and subsequently isolate intracellular proteins that become exposed on the surface of cultured cells after plasma membrane damage induced by scraping from substratum or crushing with glass beads. Scrape-damaged cells survived injury and were capable of forming viable colonies. Proteins that were exposed to the cell surface were degraded or internalized a few seconds to several minutes after damage, except for vimentin, which was detectable on the cell surface for at least an hour after injury. Seven major biotinylated protein bands were identified on SDS-PAGE gels. Mass spectrometric studies identified cytoskeletal proteins (caldesmon-1 and vimentin), endoplasmic reticulum proteins (ERp57, ERp5, and HSP47), and nuclear proteins (lamin C, heterogeneous nuclear ribonucleoprotein F, and nucleophosmin-1) as major proteins exposed after injury. Although caldesmon was a major wound-associated protein in calpain small subunit knock-out fibroblasts, it was rapidly degraded in wildtype cells, probably by calpains. Lamin C exposure after wounding was most likely the consequence of nuclear envelope damage. These studies document major intracellular proteins associated with the cell surface of reversibly damaged somatic cells. The studies also show that externalization of some proteins reported to have physiologic or pathologic roles on the cell surface can occur in cells undergoing plasma membrane damage and subsequent repair.Cells in tissues of multicellular organisms are often subjected to mechanical stresses that result in PM 2 damage (1-4). It is therefore not surprising that mechanisms have evolved to rapidly repair breaches in the PM that would otherwise rapidly lead to cell death. The currently accepted model posits calcium-dependent homotypic fusion of intracellular vesicles to provide a large membrane "patch" that rapidly (within seconds) seals the opening in the PM, maintaining cell viability. The nature of the intracellular membrane component(s) required for repair is a matter of speculation (5, 6). Few other details of the PM repair process are known, although some proteins, including membrane fusion proteins (5), myosin motor proteins (5), dysferlin (7), annexin A1 (8), calpains (9), and MG53 (10), have been shown to participate in repair in various model systems. To my knowledge, a systematic search for a "plasma membrane repairome," i.e. proteins required for repair of mechanically damaged membrane, has only been carried out in marine oocytes. Several high molecular weight yolk granule proteins were found to comprise a complex that facilitated vesicle patch formation (11).The entire chronologic sequence of repair and subsequent remodeling of the wound site is another area that requires further exploration, because an expeditious, full resolution of PM damage must be essential in tis...

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“…This implied that the amount of virus attaching to the cell surface might not solely determine the infection efficiency. Various reports suggest that vimentin may have roles in virus attachment and internalization but not in uncoating (34,37). It is possible that the virus captured by PSGL-1 and vimentin could be uncoated either by SCARB2 in human cells that expressed these receptors or by other unknown molecules.…”

Section: Discussionmentioning

confidence: 99%

“…Vimentin is the major intermediate filament protein of astrocyte cells and cells adapted to tissue culture (33). An increasing number of reports recognized an important role for cell surface vimentin as a component of the pathogen attachment and endocytotic pathways (34)(35)(36)(37)(38)(39). In this study, we further demonstrate that EV71 VP1 specifically binds to the vimentin intermediate filament located on the cell surface and that the vimentin expressed on the cell surface is involved in the attachment of EV71 to host cells.…”

mentioning

confidence: 99%

Cell Surface Vimentin Is an Attachment Receptor for Enterovirus 71

Cong

Tian

et al. 2014

J Virol

131

143

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Enterovirus 71 (EV71) is a highly transmissible pathogenic agent that causes severe central nervous system diseases in infected infants and young children. Here, we reported that EV71 VP1 protein could bind to vimentin intermediate filaments expressed on the host cell surface. Soluble vimentin or an antibody against vimentin could inhibit the binding of EV71 to host cells. Accompanied with the reduction of vimentin expression on the cell surface, the binding of EV71 to cells was remarkably decreased. Further evidence showed that the N terminus of vimentin is responsible for the interaction between EV71 and vimentin. These results indicated that vimentin on the host cell surface may serve as an attachment site that mediated the initial binding and subsequently increased the infectivity of EV71. IMPORTANCEThis study delivers important findings on the roles of vimentin filaments in relation to EV71 infection and provides information that not only improves our understanding of EV71 pathogenesis but also presents us with potentially new strategies for the treatment of diseases caused by EV71 infections.

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Endothelial Targeting of Cowpea Mosaic Virus (CPMV) via Surface Vimentin

Cited by 167 publications

References 49 publications

Foot-and-Mouth Disease Virus Modulates Cellular Vimentin for Virus Survival

Foot-and-Mouth Disease Virus Modulates Cellular Vimentin for Virus Survival

A Plasma Membrane Wound Proteome

Cell Surface Vimentin Is an Attachment Receptor for Enterovirus 71

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