Virus Budding

Rheinemann, Lara; Sundquist, Wesley I.

doi:10.1016/b978-0-12-814515-9.00023-0

Cited by 26 publications

(22 citation statements)

References 145 publications

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“…All retroviruses express structural Gag polyproteins that drive the assembly and the release of v irus- l ike p articles (VLPs), even in the absence of other viral components (for reviews, see [ 33 , 34 ]), and all retroviral Gag precursors contain the three structural domains of matrix (MA), capsid (CA), and nucleocapsid (NC), each of them playing an essential role in the retroviral particle assembly and in budding processes. Gag usually also carry additional domains and spacer peptides such as, for example, the HIV-1 p6 domain, as well as SP1 and SP2 linkers (for reviews, see [ 34 , 35 , 36 , 37 ]) ( Figure 3 ).…”

Section: Identification Of L Domains Within Hiv-1 P6 Domain Of Pr55 Gag Precursormentioning

confidence: 99%

Importance of Viral Late Domains in Budding and Release of Enveloped RNA Viruses

Welker

Paillart

Bernacchi

2021

Viruses

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Late assembly (L) domains are conserved sequences that are necessary for the late steps of viral replication, acting like cellular adaptors to engage the ESCRT membrane fission machinery that promote virion release. These short sequences, whose mutation or deletion produce the accumulation of immature virions at the plasma membrane, were firstly identified within retroviral Gag precursors, and in a further step, also in structural proteins of many other enveloped RNA viruses including arenaviruses, filoviruses, rhabdoviruses, reoviruses, and paramyxoviruses. Three classes of L domains have been identified thus far (PT/SAP, YPXnL/LXXLF, and PPxY), even if it has recently been suggested that other motifs could act as L domains. Here, we summarize the current state of knowledge of the different types of L domains and their cellular partners in the budding events of RNA viruses, with a particular focus on retroviruses.

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Section: Identification Of L Domains Within Hiv-1 P6 Domain Of Pr55 Gag Precursormentioning

confidence: 99%

Importance of Viral Late Domains in Budding and Release of Enveloped RNA Viruses

Welker

Paillart

Bernacchi

2021

Viruses

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“…Several pathogens, such as bacteria and enveloped viruses, interplay with the plasma membrane in the course of their replication cycle. Pathogens often enter the cells by endocytosis ( Grove and Marsh, 2011 ; Gruenberg and van der Goot, 2006 ) and exit by membrane vesiculation ( Rheinemann and Sundquist, 2020 ; Welsch et al, 2007 ), which are processes linked to the generation of plasma membrane curvature; either inward or outward. HIV-1 is an enveloped positive-strand RNA virus belonging to the family Retroviridae , and it is known to assemble and bud outward from the host cell plasma membrane ( Coffin et al, 1997 ).…”

Section: Introductionmentioning

confidence: 99%

Full assembly of HIV-1 particles requires assistance of the membrane curvature factor IRSp53

Inamdar

Tsai

Dibsy

et al. 2021

eLife

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During HIV-1 particle formation, the requisite plasma membrane curvature is thought to be solely driven by the retroviral Gag protein. Here, we reveal that the cellular I-BAR protein IRSp53 is required for the progression of HIV-1 membrane curvature to complete particle assembly. SiRNA-mediated knockdown of IRSp53 gene expression induces a decrease in viral particle production and a viral bud arrest at half completion. Single molecule localization microscopy at the cell plasma membrane shows a preferential localization of IRSp53 around HIV-1 Gag assembly sites. In addition, we observe the presence of IRSp53 in purified HIV-1 particles. Finally, HIV-1 Gag protein preferentially localizes to curved membranes induced by IRSp53 I-BAR domain on giant unilamellar vesicles. Overall, our data reveal a strong interplay between IRSp53 I-BAR and Gag at membranes during virus assembly. This highlights IRSp53 as a crucial host factor in HIV-1 membrane curvature and its requirement for full HIV-1 particle assembly.

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“…The selective interaction of AL1 PNF with membranes of virions but not cells suggests that differences in the composition of the viral and cellular lipid bilayer may account for this observation. The retroviral envelope is derived from the cell membrane which resembles a typical lipid bilayer and is negatively charged due to the anionic phospholipid phosphatidylserine 28,29 . However, viral and cellular membranes are not identical.…”

Section: Discussionmentioning

confidence: 99%

“…However, as shown by TEM, Cryo-EM, confocal microscopy and flow cytometry, AL1-PNF fibrils captured lentiviral or retroviral particles lacking viral glycoproteins, which were used in these experiments for safety reasons as they are not infectious. Second, retroviral particles are budding through membrane microdomains which are rich in cholesterol, sphingolipids, as well as GPI-linked and fatty acylated proteins 29,30 . Consequently, the viral membrane is enriched in these fatty acids.…”

Section: Discussionmentioning

confidence: 99%

Negatively charged peptide nanofibrils from immunoglobulin light chain sequester viral particles but lack cell-binding and viral transduction-enhancing properties

Schuetz

Read

Groß

et al. 2020

Preprint

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Positively charged naturally occurring or engineered peptide nanofibrils (PNF) are effective enhancers of lentiviral and retroviral transduction, an often rate limiting step in gene transfer and gene therapy approaches. These polycationic PNF are thought to bridge the electrostatic repulsions between negatively charged membranes of virions and cells, thereby enhancing virion attachment to and infection of target cells. Here, we analyzed PNF which are formed by the peptide AL1, which represents a fragment of an immunoglobulin light chain that causes systemic AL amyloidosis. We found that negatively charged AL1 PNF interact with viral particles to a comparable extent as positively charged PNF. However, AL1 PNF lacked cell binding activity and consequently did not enhance retroviral infection. These findings show that virion capture and cell binding of PNF are mediated by different mechanisms, offering avenues for the design of advanced PNF with selective functions.

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Virus Budding

Cited by 26 publications

References 145 publications

Importance of Viral Late Domains in Budding and Release of Enveloped RNA Viruses

Importance of Viral Late Domains in Budding and Release of Enveloped RNA Viruses

Full assembly of HIV-1 particles requires assistance of the membrane curvature factor IRSp53

Negatively charged peptide nanofibrils from immunoglobulin light chain sequester viral particles but lack cell-binding and viral transduction-enhancing properties

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