Host cytoskeleton in respiratory syncytial virus assembly and budding

Shahriari, Shadi; Gordon, James D.; Ghildyal, Reena

doi:10.1186/s12985-016-0618-z

Cited by 31 publications

(27 citation statements)

References 97 publications

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“…A significant challenge to RSV treatment and prevention is absence of available antiviral drugs and vaccines that effectively target infections [ 1 , 4 ]. RSV is an enveloped virus with a negative-sense single-stranded RNA genome, belonging to the Pneumovirus genus of the Pneumoviridae family [ 5 , 6 ]. The RSV genome encodes 11 proteins and is tightly encapsidated with the nucleocapsid, which is composed of the nucleocapsid (N) protein, RNA polymerase (L) and its cofactor phosphoprotein (P), as well as the M2-1 protein [ 5 , 7 ].…”

Section: Introductionmentioning

confidence: 99%

“…RSV is an enveloped virus with a negative-sense single-stranded RNA genome, belonging to the Pneumovirus genus of the Pneumoviridae family [ 5 , 6 ]. The RSV genome encodes 11 proteins and is tightly encapsidated with the nucleocapsid, which is composed of the nucleocapsid (N) protein, RNA polymerase (L) and its cofactor phosphoprotein (P), as well as the M2-1 protein [ 5 , 7 ]. In addition to these, the genome also encodes the envelope glycoproteins fusion protein (F), glycoprotein (G) and small hydrophobic protein (SH), two non-structural proteins (NS1 and NS2), the M2-2 protein, and the matrix protein (M).…”

Section: Introductionmentioning

confidence: 99%

“…The M protein is a non-glycosylated phosphorylated protein located external to the nucleocapsid layer, where it acts as a bridge between the lipid bilayer envelope and the nucleocapsid [ 5 , 7 , 8 , 9 , 10 , 11 , 12 ]. By bridging the lipid bilayer envelope and the nucleocapsid, the M protein plays a role in driving the coordinated interplay between the viral structural components to facilitate viral assembly [ 13 ].…”

Section: Introductionmentioning

confidence: 99%

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Respiratory Syncytial Virus Matrix (M) Protein Interacts with Actin In Vitro and in Cell Culture

Shahriari

Wei

Ghildyal

2018

Viruses

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The virus–host protein interactions that underlie respiratory syncytial virus (RSV) assembly are still not completely defined, despite almost 60 years of research. RSV buds from the apical surface of infected cells, once virion components have been transported to the budding sites. Association of RSV matrix (M) protein with the actin cytoskeleton may play a role in facilitating this transport. We have investigated the interaction of M with actin in vitro and cell culture. Purified wildtype RSV M protein was found to bind directly to polymerized actin in vitro. Vero cells were transfected to express full-length M (1–256) as a green fluorescent protein-(GFP) tagged protein, followed by treatment with the microfilament destabilizer, cytochalasin D. Destabilization of the microfilament network resulted in mislocalization of full-length M, from mostly cytoplasmic to diffused across both cytoplasm and nucleus, suggesting that M interacts with microfilaments in this system. Importantly, treatment of RSV-infected cells with cytochalasin D results in lower infectious virus titers, as well as mislocalization of M to the nucleus. Finally, using deletion mutants of M in a transfected cell system, we show that both the N- and C-terminus of the protein are required for the interaction. Together, our data suggest a possible role for M–actin interaction in transporting virion components in the infected cell.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Respiratory Syncytial Virus Matrix (M) Protein Interacts with Actin In Vitro and in Cell Culture

Shahriari

Wei

Ghildyal

2018

Viruses

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“…Upregulation of these genes was expected considering the morphological changes that cells experience after infection and the clustering we observed, all changes that should require signals for cytoskeleton rearrangement. It is known that the virus must need the cell cytoskeleton to allow assembly of viral proteins and genome and liberation from host cells (budding), therefore, knowing that in our cell model, there is a greater viral replication associated with greater viral particles release between 72 and 96 hpi, it is highly possible that the virus modulates the signals in order to be released (Shahriari et al, 2016).…”

Section: Discussionmentioning

confidence: 99%

Time-course of transcriptome response to respiratory syncytial virus infection in lung epithelium cells

Ampuero¹,

Andaur²,

Milano³

et al. 2018

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Respiratory syncytial virus (RSV) is the major cause of acute lower respiratory tract infection in infants. Winter outbreaks in Chile result in 5% of infected children hospitalized, with 0.01% mortality. Increased evidence indicates that viral and host factors modulate the severity of infection. Using DNA microarrays, we characterized the genome-wide transcriptional response of lung mucoepidermoid cells (NCI-H292) at 0, 24, 48, 72 and 96 hours post-infection (hpi) with a single dose of RSV/A. During the whole studied period, a bi-phasic gene expression profile was observed by a total of 330 differentially expressed genes. About 60% of them were up-regulated between 24-72 hpi and then turned-off at 96 hpi. This transient, early gene expression pattern was significantly enriched in biological processes like interferon signaling, antigen processing and presentation, double-stranded RNA binding and chemokine activity. We detected 27 common genes up-regulated between 24-72 hpi, from which IFIT1, IFI44, MX1, CXCL11 and OAS1 had the highest expression. The second pattern comprised over 120 genes, which remained silenced until 72 hpi, but were steeply up-regulated by 96 hpi. Biological processes of this late-response profile included cell cycle division and microtubule cytoskeleton organization. Conversely, the genes belonging to virus response pathway showed a decreased expression at 96 hpi. We conclude that RSV induces an early innate immune activation profile response until 72 hpi. Thereafter, the viral response is inhibited, leading to host cell recovery. The presented cellular model allows to study the specific pathways involved in elimination of infection at prolonged time intervals and their subsequent analysis in severe RSV disease of infants and/or older adults.

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“…Therefore, downregulation of cortactin can be a potential strategy usurped by IAV for viral release. In addition, HDAC6 may regulate actin remodelling under the plasma membrane to restrict viral assembly and budding [93,94], when considering that actin cytoskeleton has been shown to associate with IAV infection [95][96][97].…”

Section: Assembly and Egressmentioning

confidence: 99%

Cellular defence or viral assist: the dilemma of HDAC6

Zheng

Jiang

et al. 2017

Journal of General Virology

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Histone deacetylase 6 (HDAC6) is a unique cytoplasmic deacetylase that regulates various important biological processes by preventing protein aggregation and deacetylating different non-histone substrates including tubulin, heat shock protein 90, cortactin, retinoic acid inducible gene I and b-catenin. Growing evidence has indicated a dual role for HDAC6 in viral infection and pathogenesis: HDAC6 may represent a host defence mechanism against viral infection by modulating microtubule acetylation, triggering antiviral immune response and stimulating protective autophagy, or it may be hijacked by the virus to enhance proinflammatory response. In this review, we will highlight current data illustrating the complexity and importance of HDAC6 in viral pathogenesis. We will summarize the structure and functional specificity of HDAC6, and its deacetylaseand ubiquitin-dependent activity in key cellular events in response to virus infection. We will also discuss how HDAC6 exerts its direct or indirect histone modification ability in viral lytic-latency switch.

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Host cytoskeleton in respiratory syncytial virus assembly and budding

Cited by 31 publications

References 97 publications

Respiratory Syncytial Virus Matrix (M) Protein Interacts with Actin In Vitro and in Cell Culture

Respiratory Syncytial Virus Matrix (M) Protein Interacts with Actin In Vitro and in Cell Culture

Time-course of transcriptome response to respiratory syncytial virus infection in lung epithelium cells

Cellular defence or viral assist: the dilemma of HDAC6

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