Requirements for the Assembly and Release of Newcastle Disease Virus-Like Particles

Pantua, Homer; McGinnes, Lori W.; Peeples, Mark E.; Morrison, Trudy G.

doi:10.1128/jvi.00726-06

Cited by 158 publications

(114 citation statements)

References 52 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: 88%

“…Indeed, in certain other recombinant VLP expression systems, the amounts of transfected plasmids have been adjusted to more accurately reflect or achieve cellular expression levels of the individual viral proteins produced using infectious virus (99,116,121). In an attempt to increase the amount of protein release in our system, we performed similar experimental variations in the amounts of transfected plasmids and estimated envelope glycoprotein expression in authentic NiV infection as one third of M expression and adjusted plasmid ratios accordingly (56,117,140).…”

Section: Mva Expression Of Nivmentioning

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

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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: 88%

Section: Mva Expression Of Nivmentioning

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

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2007

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“…These structures are built of one or two domains that have similar β-sandwich folds, suggesting gene duplication during evolution. The dimers of paramyxovirus M protein (approximately 40 kDa) can form a grid-like array on the inner surface of the viral membrane (15)(16)(17)(18), and probably interact with both the cytoplasmic tails of the HN and F glycoproteins (19,20) as well as the nucleocapsid (21)(22)(23)(24) to initiate virus assembly and budding (20). The NDV M protein has greater than 20% sequence identity with other paramyxovirus M proteins including measles, mumps, and the parainfluenza viruses.…”

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confidence: 99%

Structure and assembly of a paramyxovirus matrix protein

Battisti

Meng

Winkler

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Many pleomorphic, lipid-enveloped viruses encode matrix proteins that direct their assembly and budding, but the mechanism of this process is unclear. We have combined X-ray crystallography and cryoelectron tomography to show that the matrix protein of Newcastle disease virus, a paramyxovirus and relative of measles virus, forms dimers that assemble into pseudotetrameric arrays that generate the membrane curvature necessary for virus budding. We show that the glycoproteins are anchored in the gaps between the matrix proteins and that the helical nucleocapsids are associated in register with the matrix arrays. About 90% of virions lack matrix arrays, suggesting that, in agreement with previous biological observations, the matrix protein needs to dissociate from the viral membrane during maturation, as is required for fusion and release of the nucleocapsid into the host's cytoplasm. Structure and sequence conservation imply that other paramyxovirus matrix proteins function similarly.

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Newcastle Disease Virus‐Like Particles: Preparation, Purification, Quantification, and Incorporation of Foreign Glycoproteins

McGinnes

Morrison

2013

CP Microbiology

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Virus‐like particles (VLPs) are large particles, the size of viruses, composed of repeating structures that mimic those of infectious virus. Since their structures are similar to that of viruses, they have been used to study the mechanisms of virus assembly. They are also in development for delivery of molecules to cells and in studies of the immunogenicity of particle‐associated antigens. However, they have been most widely used for development of vaccines and vaccine candidates. VLPs can form upon the expression of the structural proteins of many different viruses. This chapter describes the generation and purification of VLPs formed with the structural proteins, M, NP, F, and HN proteins, of Newcastle disease virus (NDV). Newcastle disease virus‐like particles (ND VLPs) have also been developed as a platform for assembly into VLPs of glycoproteins from other viruses. This chapter describes the methods for this use of ND VLPs. Curr. Protoc. Microbiol. 30:18.2.1‐18.2.21. © 2013 by John Wiley & Sons, Inc.

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Requirements for the Assembly and Release of Newcastle Disease Virus-Like Particles

Cited by 158 publications

References 52 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

Structure and assembly of a paramyxovirus matrix protein

Newcastle Disease Virus‐Like Particles: Preparation, Purification, Quantification, and Incorporation of Foreign Glycoproteins

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