Maturation of the matrix and viral membrane of HIV-1

Qu, Kun; Ke, Zunlong; Žíla, Vojtěch; Anders-Ößwein, Maria; Glass, Bärbel; Mücksch, Frauke; Müller, Rainer; Schultz, Carsten; Müller, Bárbara; Kräusslich, Hans Georg; Briggs, John

doi:10.1126/science.abe6821

Cited by 83 publications

(88 citation statements)

References 67 publications

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“…In both cases, proteolytic processing would result in a change of the environment of the fluorophore from its packed arrangement within the immature shell. Since mature MA remains associated with the viral membrane and was recently observed to retain a modified lattice arrangement [26], the change in the local microenvironment of eCFP is expected to be less pronounced for HIV eCFP compared to HIV ieCFP , where the released fluorophore would be able to distribute within the particle volume (Figure 1A). To maintain wild-type assembly properties, eCFPtagged HIV-1 plasmids were co-transfected with their untagged counterpart (pCHIV) in an equimolar ratio [27].…”

Section: Resultsmentioning

confidence: 99%

Dynamics of HIV-1 Gag Processing as Revealed by Fluorescence Lifetime Imaging Microscopy and Single Virus Tracking

Qian

Flemming

Müller

et al. 2022

Viruses

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The viral polyprotein Gag plays a central role for HIV-1 assembly, release and maturation. Proteolytic processing of Gag by the viral protease is essential for the structural rearrangements that mark the transition from immature to mature, infectious viruses. The timing and kinetics of Gag processing are not fully understood. Here, fluorescence lifetime imaging microscopy and single virus tracking are used to follow Gag processing in nascent HIV-1 particles in situ. Using a Gag polyprotein labelled internally with eCFP, we show that proteolytic release of the fluorophore from Gag is accompanied by an increase in its fluorescence lifetime. By tracking nascent virus particles in situ and analyzing the intensity and fluorescence lifetime of individual traces, we detect proteolytic cleavage of eCFP from Gag in a subset (6.5%) of viral particles. This suggests that for the majority of VLPs, Gag processing occurs with a delay after particle assembly.

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Section: Resultsmentioning

confidence: 99%

Dynamics of HIV-1 Gag Processing as Revealed by Fluorescence Lifetime Imaging Microscopy and Single Virus Tracking

Qian

Flemming

Müller

et al. 2022

Viruses

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“…Oppositely, depletion of PI(4,5)P2 from the membrane inhibits the release of HIV-1 virions [31]. Finally, a direct interaction of HIV-1 MA with PI(4,5)P2 after the maturation of the viral particle has been documented [26].…”

Section: Fiv Mamentioning

confidence: 99%

“…For HIV-1, it has been suggested that MA/MA interactions mediated by the oligomerization of the Gag polyprotein induce conformational changes that expose this myristoyl group outside the hydrophobic cavity, making it available to interact with the plasma membrane together with the basic patch of helix h1 [11]. Moreover, the reorganization of the MA lattice after the cleavage of HIV-1 Gag also retains the exposure of the myristoyl group and its interaction with the plasma membrane of the infectious particle [26].…”

Section: Fiv Mamentioning

confidence: 99%

Review and Perspectives on the Structure–Function Relationships of the Gag Subunits of Feline Immunodeficiency Virus

2021

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The Gag polyprotein is implied in the budding as well as the establishment of the supramolecular architecture of infectious retroviral particles. It is also involved in the early phases of the replication of retroviruses by protecting and transporting the viral genome towards the nucleus of the infected cell until its integration in the host genome. Therefore, understanding the structure–function relationships of the Gag subunits is crucial as each of them can represent a therapeutic target. Though the field has been explored for some time in the area of Human Immunodeficiency Virus (HIV), it is only in the last decade that structural data on Feline Immunodeficiency Virus (FIV) Gag subunits have emerged. As FIV is an important veterinary issue, both in domestic cats and endangered feline species, such data are of prime importance for the development of anti-FIV molecules targeting Gag. This review will focus on the recent advances and perspectives on the structure–function relationships of each subunit of the FIV Gag polyprotein.

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“…MA crystallizes on membrane monolayers into a hexameric lattice of trimers [ 84 , 85 ]. Recent work from the Briggs group allowed modeling of the structure of MA within immature and mature HIV-1 particles using MA lattice data derived by cryo-ET ( Figure 3 F) [ 43 ]. This work confirmed the presence of a hexameric lattice of MA in the immature virions and of large holes in the lattice at the six-fold axis, although the lattice was poorly ordered.…”

Section: Ma: Regulator Of Gag-membrane Interactions and Env Incorpora...mentioning

confidence: 99%

Advances in HIV-1 Assembly

Lerner

Weaver

Anokhin

et al. 2022

Viruses

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The assembly of HIV-1 particles is a concerted and dynamic process that takes place on the plasma membrane of infected cells. An abundance of recent discoveries has advanced our understanding of the complex sequence of events leading to HIV-1 particle assembly, budding, and release. Structural studies have illuminated key features of assembly and maturation, including the dramatic structural transition that occurs between the immature Gag lattice and the formation of the mature viral capsid core. The critical role of inositol hexakisphosphate (IP6) in the assembly of both the immature and mature Gag lattice has been elucidated. The structural basis for selective packaging of genomic RNA into virions has been revealed. This review will provide an overview of the HIV-1 assembly process, with a focus on recent advances in the field, and will point out areas where questions remain that can benefit from future investigation.

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Maturation of the matrix and viral membrane of HIV-1

Cited by 83 publications

References 67 publications

Dynamics of HIV-1 Gag Processing as Revealed by Fluorescence Lifetime Imaging Microscopy and Single Virus Tracking

Dynamics of HIV-1 Gag Processing as Revealed by Fluorescence Lifetime Imaging Microscopy and Single Virus Tracking

Review and Perspectives on the Structure–Function Relationships of the Gag Subunits of Feline Immunodeficiency Virus

Advances in HIV-1 Assembly

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