Characterization of a small (25-kilodalton) derivative of the Rous sarcoma virus Gag protein competent for particle release

Weldon, Robert; Wills, John W.

doi:10.1128/jvi.67.9.5550-5561.1993

Cited by 84 publications

(122 citation statements)

References 34 publications

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“…For the present study we established a chimeric VLP assembly process to analyze SARS-CoV N self-interaction capacity. Our evidence-that chimeras containing the SARS-CoV N protein coding sequence as a substitute for HIV-1 NC are capable of producing substantial amounts of VLPs-supports the idea that retroviral gag is capable of tolerating major mutations [48,49,54]. The inability of the PC(CoN) chimera to produce VLPs cannot be explained solely by an assembly limitation of extra-large proteins-as is the case with DNC(CoN), which contains the same full-length N yet still produces significant amounts of VLPs.…”

Section: Discussionsupporting

confidence: 71%

Severe acute respiratory syndrome coronavirus nucleocapsid protein confers ability to efficiently produce virus-like particles when substituted for the human immunodeficiency virus nucleocapsid domain

Wang

Chang²,

Chen³

et al. 2008

J Biomed Sci

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We replaced the HIV-1 nucleocapsid (NC) domain with different N-coding sequences to test SARS-CoV nucleocapsid (N) self-interaction capacity, and determined the capabilities of each chimera to direct virus-like particle (VLP) assembly. Analysis results indicate that the replacement of NC with the carboxyl-terminal half of the SARS-CoV N resulted in the production of wild type (wt)-level virus-like particles (VLPs) with the density of a wt HIV-1 particle. When co-expressed with SARS-CoV N, chimeras containing the N carboxyl-terminal half sequence efficiently packaged N. However, the same was not true for the chimera bearing the N amino-terminal half sequence, despite its production of substantial amounts of VLPs. According to further analysis, HIV-1 NC replacement with N residues 2-213, 215-421, or 234-421 resulted in efficient VLP production at levels comparable to that of wt HIV-1, but replacement with residues 215-359, 302-421, 2-168, or 2-86 failed to restore VLP production to wild-type levels. The results suggest that the domain conferring the ability to direct VLP assembly and release in SARS-CoV N is largely contained between residues 168 and 421.

show abstract

Section: Discussionsupporting

confidence: 71%

Severe acute respiratory syndrome coronavirus nucleocapsid protein confers ability to efficiently produce virus-like particles when substituted for the human immunodeficiency virus nucleocapsid domain

Wang

Chang²,

Chen³

et al. 2008

J Biomed Sci

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show abstract

“…The M domain is located at the amino terminus of Gag and provides the membrane-binding and -targeting functions (reference 55 and this work). Interactions between Gag molecules take place via the I domain, of which there are two copies within the NC sequence (2,50). Completion of the final steps of budding (occurring after Gag proteins have bound to the plasma membrane and established interactions) requires the late domain, L, which maps to the small proline-rich sequence of p2b (26,52).…”

mentioning

confidence: 99%

A large region within the Rous sarcoma virus matrix protein is dispensable for budding and infectivity

Nelle

Wills

1996

J Virol

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All retroviruses have a layer of matrix protein (MA) situated directly beneath the lipid of their envelope. This protein is initially expressed as the amino-terminal sequence of the Gag polyprotein, where it plays an important role in binding Gag to the plasma membrane during the early steps of the budding process. Others have suggested that MA may provide additional functions during virion assembly, including the selective incorporation of viral glycoproteins and the RNA genome into the emerging virion. To further study the role of the Rous sarcoma virus MA sequence in the viral replication cycle, we have pursued an extensive deletion analysis. Surprisingly, the entire second half of MA (residues 87 to 155) and part of the neighboring p2 sequence were found to be dispensable not only for budding but also for infectivity in avian cells. Thus, all of the functions associated with the Rous sarcoma virus MA sequence must be contained within its first half.

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“…Gag Gag [37,38] L-domain [39,40] a These viruses appear to lack a discrete matrix protein, but the matrix function may be carried out by glycoprotein transmembrane and cytoplasmic tail regions. b Borna disease virus M protein contains a YXXL motif that has not yet been demonstrated to function as an L-domain.…”

Section: Retroviridaementioning

confidence: 99%

Arenavirus budding resulting from viral-protein-associated cell membrane curvature

Schley

Whittaker

Neuman

2013

J. R. Soc. Interface.

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Viral replication occurs within cells, with release (and onward infection) primarily achieved through two alternative mechanisms: lysis, in which virions emerge as the infected cell dies and bursts open; or budding, in which virions emerge gradually from a still living cell by appropriating a small part of the cell membrane. Virus budding is a poorly understood process that challenges current models of vesicle formation. Here, a plausible mechanism for arenavirus budding is presented, building on recent evidence that viral proteins embed in the inner lipid layer of the cell membrane. Experimental results confirm that viral protein is associated with increased membrane curvature, whereas a mathematical model is used to show that localized increases in curvature alone are sufficient to generate viral buds. The magnitude of the protein-induced curvature is calculated from the size of the amphipathic region hypothetically removed from the inner membrane as a result of translation, with a change in membrane stiffness estimated from observed differences in virion deformation as a result of protein depletion. Numerical results are based on experimental data and estimates for three arenaviruses, but the mechanisms described are more broadly applicable. The hypothesized mechanism is shown to be sufficient to generate spontaneous budding that matches well both qualitatively and quantitatively with experimental observations.

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Characterization of a small (25-kilodalton) derivative of the Rous sarcoma virus Gag protein competent for particle release

Cited by 84 publications

References 34 publications

Severe acute respiratory syndrome coronavirus nucleocapsid protein confers ability to efficiently produce virus-like particles when substituted for the human immunodeficiency virus nucleocapsid domain

Severe acute respiratory syndrome coronavirus nucleocapsid protein confers ability to efficiently produce virus-like particles when substituted for the human immunodeficiency virus nucleocapsid domain

A large region within the Rous sarcoma virus matrix protein is dispensable for budding and infectivity

Arenavirus budding resulting from viral-protein-associated cell membrane curvature

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