Role of Matrix and Fusion Proteins in Budding of Sendai Virus

Takimoto, Toru; Murti, K.G.; Bousse, Tatiana; Scroggs, Ruth Ann; Portner, Allen

doi:10.1128/jvi.75.23.11384-11391.2001

Cited by 108 publications

(118 citation statements)

References 43 publications

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“…3C). This density range was consistent with the density reported for SeV and NDV VLPs (99,121,123), as well as authentic NiV (see below). To examine the contribution of each viral protein to overall protein release, NiV proteins were expressed in different combinations and their release was quantified.…”

Section: Mva Expression Of Nivsupporting

confidence: 79%

“…6A), which suggests that the observed release of NiV M was specific to its biological properties and not due to a non-specific mechanism such as cell lysis. In this respect, NiV M was similar to the M proteins of SeV, NDV, and hPIV1, all of which have been reported to form VLPs in the absence of other viral proteins (31,99,121,123). release, but then readily detected at 4 h with 1.7% release (Fig.…”

Section: Fig 6amentioning

confidence: 89%

“…In addition to self-association, certain M proteins have also been shown to interact with the viral envelope glycoproteins as well as the viral nucleocapsids (viral RNA genomes associated with N protein). Although its interaction with cellular proteins has remained relatively unexplored and may differ according to viral species, there is evidence that SeV and NDV M interacts with actin (43,123), and the discovery of a late budding domain in SV5 M (115) strongly suggests an interaction with cellular multivesicular body proteins. It is likely that additional undiscovered interactions between M and cellular proteins exist.…”

Section: Henipaviru5 Genomementioning

confidence: 99%

“…The M protein is thought to mediate this association, however the details of this process remain poorly understood and appear to vary among viral species [reviewed in (114)]. (121,123), the G protein of RV and VSV (82,107), and the envelope glycoprotein (GP) of Ebola virus (5,92,130). In contrast, SV5 requires expression of M along with N and at least one of its envelope glycoproteins in order for efficient budding to occur (116).…”

Section: Paramyxovirus Assemblymentioning

confidence: 99%

“…To determine whether the protein release we observed was an accurate reflection of NiV biology or an artifact resulting from poxvirus infection, we employed a transfection plasmid-based expression system using the pCAGGS eukaryotic expression vector, which has also been used in other paramyxovirus VLP assays (31,99,116,121,123).…”

Section: Mva Expression Of Nivmentioning

confidence: 99%

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The Central Role of the Matrix Protein in Nipah Virus Assembly and Morphogenesis

Patch¹

2007

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The author hereby certifies that the use of any copyrighted material in the thesis manuscript entitled:"The Central Role of the Matrix Protein in Nipah Virus Assembly and Morphogenesis" is appropriately acknowledged and, beyond brief excerpts, is with the permission of the copyright owner. Additionally, NiV M contains a sequence that is important for budding and appears to serve as an L-domain. These findings further our understanding of paramyxovirus particle assembly in general and could help facilitate the development of a novel vaccine approach for henipaviruses.ii

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Section: Mva Expression Of Nivsupporting

confidence: 79%

Section: Fig 6amentioning

confidence: 89%

Section: Henipaviru5 Genomementioning

confidence: 99%

Section: Paramyxovirus Assemblymentioning

confidence: 99%

Section: Mva Expression Of Nivmentioning

confidence: 99%

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The Central Role of the Matrix Protein in Nipah Virus Assembly and Morphogenesis

Patch¹

2007

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Nipah virus matrix protein: expert hacker of cellular machines

Watkinson

Lee

2016

FEBS Letters

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Nipah virus (NiV, Henipavirus) is a highly lethal emergent zoonotic paramyxovirus responsible for repeated human outbreaks of encephalitis in South East Asia. There are no approved vaccines or treatments, thus improved understanding of NiV biology is imperative. NiV matrix protein recruits a plethora of cellular machinery to scaffold and coordinate virion budding. Intriguingly, matrix also hijacks cellular trafficking and ubiquitination pathways to facilitate transient nuclear localization. While the biological significance of matrix nuclear localization for an otherwise cytoplasmic virus remains enigmatic, the molecular details have begun to be characterized, and are conserved among matrix proteins from divergent paramyxoviruses. Matrix protein appropriation of cellular machinery will be discussed in terms of its early nuclear targeting and later role in virion assembly.

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Respiroviruses: Parainfluenza Virus

Peluso¹,

Moscona²

2010

Topley &Amp; Wilson's Microbiology and Microbial Infections

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Role of Matrix and Fusion Proteins in Budding of Sendai Virus

Cited by 108 publications

References 43 publications

The Central Role of the Matrix Protein in Nipah Virus Assembly and Morphogenesis

The Central Role of the Matrix Protein in Nipah Virus Assembly and Morphogenesis

Nipah virus matrix protein: expert hacker of cellular machines

Respiroviruses: Parainfluenza Virus

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