Assembly and Budding of Negative-Strand RNA Viruses

Lyles, Douglas S.

doi:10.1016/b978-0-12-408116-1.00003-3

Cited by 34 publications

(37 citation statements)

References 149 publications

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“…To study viral assembly and budding processes, individual or isolated viral components are expressed in cells to test their release into the culture medium as VLPs corresponding to membranecontaining viral structures (17). Previously, it has been reported that hantavirus VLPs are produced when Gn, Gc, and N proteins are coexpressed (18,19).…”

mentioning

confidence: 99%

Hantavirus Gn and Gc Glycoproteins Self-Assemble into Virus-Like Particles

Acuña

Cifuentes-Muñoz

Márquez

et al. 2014

J Virol

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f How hantaviruses assemble and exit infected cells remains largely unknown. Here, we show that the expression of Andes (ANDV) and Puumala (PUUV) hantavirus Gn and Gc envelope glycoproteins lead to their self-assembly into virus-like particles (VLPs) which were released to cell supernatants. The viral nucleoprotein was not required for particle formation. Further, a Gc endodomain deletion mutant did not abrogate VLP formation. The VLPs were pleomorphic, exposed protrusions and reacted with patient sera.

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mentioning

confidence: 99%

Hantavirus Gn and Gc Glycoproteins Self-Assemble into Virus-Like Particles

Acuña

Cifuentes-Muñoz

Márquez

et al. 2014

J Virol

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“…Recruitment of host machinery via the matrix and Gag proteins of negative-strand RNA viruses and retroviruses is critical in many cases for proper formation and release of virus particles (25)(26)(27)(28), yet for many paramyxoviruses, including the henipaviruses, M protein-host protein interactions remain largely unexplored. In this study, we identified the beta subunit of the AP-3 adapter protein complex, AP3B1, as a binding partner for the Nipah virus and Hendra virus M proteins.…”

mentioning

confidence: 99%

Matrix Proteins of Nipah and Hendra Viruses Interact with Beta Subunits of AP-3 Complexes

Sun

McCrory

Khaw

et al. 2014

J Virol

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Paramyxoviruses and other negative-strand RNA viruses encode matrix proteins that coordinate the virus assembly process. The matrix proteins link the viral glycoproteins and the viral ribonucleoproteins at virus assembly sites and often recruit host machinery that facilitates the budding process. Using a co-affinity purification strategy, we have identified the beta subunit of the AP-3 adapter protein complex, AP3B1, as a binding partner for the M proteins of the zoonotic paramyxoviruses Nipah virus and Hendra virus. Binding function was localized to the serine-rich and acidic Hinge domain of AP3B1, and a 29-amino-acid Hingederived polypeptide was sufficient for M protein binding in coimmunoprecipitation assays. Virus-like particle (VLP) production assays were used to assess the relationship between AP3B1 binding and M protein function. We found that for both Nipah virus and Hendra virus, M protein expression in the absence of any other viral proteins led to the efficient production of VLPs in transfected cells, and this VLP production was potently inhibited upon overexpression of short M-binding polypeptides derived from the Hinge region of AP3B1. Both human and bat (Pteropus alecto) AP3B1-derived polypeptides were highly effective at inhibiting the production of VLPs. VLP production was also impaired through small interfering RNA (siRNA)-mediated depletion of AP3B1 from cells. These findings suggest that AP-3-directed trafficking processes are important for henipavirus particle production and identify a new host protein-virus protein binding interface that could become a useful target in future efforts to develop small molecule inhibitors to combat paramyxoviral infections. IMPORTANCEHenipaviruses cause deadly infections in humans, with a mortality rate of about 40%. Hendra virus outbreaks in Australia, all involving horses and some involving transmission to humans, have been a continuing problem. Nipah virus caused a large outbreak in Malaysia in 1998, killing 109 people, and smaller outbreaks have since occurred in Bangladesh and India. In this study, we have defined, for the first time, host factors that interact with henipavirus M proteins and contribute to viral particle assembly. We have also defined a new host protein-viral protein binding interface that can potentially be targeted for the inhibition of paramyxovirus infections.

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“…The assembly of viral membranes is a sophisticated and specific process that involves coalescence of viral components at discrete sites on cellular membranes and exclusion of the majority of host cell membrane proteins. Recent data support the idea that viral glycoproteins of enveloped RNA viruses are not randomly distributed on the cell surface but instead are clustered within lipid raft membrane microdomains to form the nucleation points for budding [224]. Lipid rafts, which are rich in cholesterol and sphingolipids, are characterized by a rigid, ordered structure with limited flexibility and can thus act as platforms for virus assembly (reviewed in [21,225,226,227,228]).…”

Section: Localization Of Glycoproteins At Membrane Assembly Sites:mentioning

confidence: 93%

Paramyxovirus Glycoprotein Incorporation, Assembly and Budding: A Three Way Dance for Infectious Particle Production

Najjar

Schmitt

Dutch

2014

Viruses

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Paramyxoviruses are a family of negative sense RNA viruses whose members cause serious diseases in humans, such as measles virus, mumps virus and respiratory syncytial virus; and in animals, such as Newcastle disease virus and rinderpest virus. Paramyxovirus particles form by assembly of the viral matrix protein, the ribonucleoprotein complex and the surface glycoproteins at the plasma membrane of infected cells and subsequent viral budding. Two major glycoproteins expressed on the viral envelope, the attachment protein and the fusion protein, promote attachment of the virus to host cells and subsequent virus-cell membrane fusion. Incorporation of the surface glycoproteins into infectious progeny particles requires coordinated interplay between the three viral structural components, driven primarily by the matrix protein. In this review, we discuss recent progress in understanding the contributions of the matrix protein and glycoproteins in driving paramyxovirus assembly and budding while focusing on the viral protein interactions underlying this process and the intracellular trafficking pathways for targeting viral components to assembly sites. Differences in the mechanisms of particle production among the different family members will be highlighted throughout.

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Assembly and Budding of Negative-Strand RNA Viruses

Cited by 34 publications

References 149 publications

Hantavirus Gn and Gc Glycoproteins Self-Assemble into Virus-Like Particles

Hantavirus Gn and Gc Glycoproteins Self-Assemble into Virus-Like Particles

Matrix Proteins of Nipah and Hendra Viruses Interact with Beta Subunits of AP-3 Complexes

Paramyxovirus Glycoprotein Incorporation, Assembly and Budding: A Three Way Dance for Infectious Particle Production

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