Structure of transmembrane subunits gp47 of the foamy virus envelope glycoproteins

Wang, M; Zhang, H; Qm, Liu; Sun, Yan; Z, Li; Wh, Liu; He, Xin; Song, Jian; Yx, Wang

doi:10.4149/av_2016_02_181

Cited by 5 publications

(3 citation statements)

References 34 publications

(59 reference statements)

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“…The 21 turn-long central helix encompasses the HRA segment, and its N-terminal portion includes the region predicted to be the fusion peptide (FP) (Fig. S1C-D) [31, 32]. The 16 N-terminal turns of the central helix (termed HRA N helix) coil around each other along the trimer axis, while its 5 C-terminal turns (termed HRA C helix) run parallel to HRA C of the other protomers and also pack against helix ⍺ 2 of domain III (Fig.…”

Section: Resultsmentioning

confidence: 99%

Structures of the Foamy virus fusion protein reveal an unexpected link with the F protein of paramyxo- and pneumoviruses

Fernández,

Bontems,

Brun

et al. 2024

Preprint

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Foamy viruses (FVs) constitute a subfamily of retroviruses. Their envelope glycoprotein (Env) drives the merger of viral and cellular membranes during entry into cells. The only available structures of retroviral Envs are those from human and simian immunodeficiency viruses from the subfamily of orthoretroviruses, which are only distantly related to the FVs. We report here the cryo-EM structures of the FV Env ectodomain in the pre- and post-fusion states, which demonstrate structural similarity with the fusion protein (F) of paramyxo- and pneumoviruses, implying an evolutionary link between the two viral fusogens. Based on the structural information on the FV Env in two states, we propose a mechanistic model for its conformational change, highlighting how the interplay of its structural elements could drive the structural rearrangement. The structural knowledge on the FV Env now provides a framework for functional investigations such as the FV cell tropism and molecular features controlling the Env fusogenicity, which can benefit the design of FV Env variants with improved features for use as gene therapy vectors.

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Section: Resultsmentioning

confidence: 99%

Structures of the Foamy virus fusion protein reveal an unexpected link with the F protein of paramyxo- and pneumoviruses

Fernández,

Bontems,

Brun

et al. 2024

Preprint

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“…Since the TMDs of gp48 likely need to dissociate to mediate membrane fusion, this structure suggests a model in which the gp18 TMD helices block the dissociation of the gp48 until the fusion cascade promotes movement of the entire TMD complex. Computational analysis of the TMD subunits of several Foamy virus strains revealed a conserved lysine-proline motif that suggests a break may exist in the gp48 TMD helix [142], but this was not observed in the structural analysis. However, this motif could serve as a flex point during the conformational changes of the fusion process.…”

Section: Other Class I Viral Fusion Proteinsmentioning

confidence: 90%

Viral Membrane Fusion and the Transmembrane Domain

Barrett

Dutch

2020

Viruses

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Initiation of host cell infection by an enveloped virus requires a viral-to-host cell membrane fusion event. This event is mediated by at least one viral transmembrane glycoprotein, termed the fusion protein, which is a key therapeutic target. Viral fusion proteins have been studied for decades, and numerous critical insights into their function have been elucidated. However, the transmembrane region remains one of the most poorly understood facets of these proteins. In the past ten years, the field has made significant advances in understanding the role of the membrane-spanning region of viral fusion proteins. We summarize developments made in the past decade that have contributed to the understanding of the transmembrane region of viral fusion proteins, highlighting not only their critical role in the membrane fusion process, but further demonstrating their involvement in several aspects of the viral lifecycle.

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“…As the most important transcriptional regulatory protein of FVs, Tas played a very important role in governing the transcriptions of the structural proteins, initiating virus replication and regulating the interaction between foamy virus and the host cells [13]. But excepted for evolutionary analysis of FVs based on the sequences of structural proteins Gag, Pol, Env or 5'LTR [14], there were few studies on the construction of evolutionary tree based on the function-conserved regulatory protein Tas.…”

Section: Introductionmentioning

confidence: 99%

Paradox of Nonpathogenicity and Cytopathic Effects：Characterization of Regulator Tas in Foamy Virus Evolution and De-Ubiquitylation of Tas in Virus Duplication

Wei

Zhang

Jing

et al. 2021

Preprint

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Background: Foamy virus, which belong to the Spumaretrovirinae subfamily of Retroviridae, bridge the gap between Orthoretrovirinae and Hepadnaviridae, and display a long co-evolution with their hosts. Like other retroviruses, FVs encode a transactivator, Tas, which governs the levels of viral transcripts initiated through binding to the conserved promoters in 5’ long terminal repeat (LTR) and a unique internal promoter (IP). Unlike the other retrovirus, HIV, foamy viruses induced significant cytopathic effects in vitro, but has no significant disease association at the infection level in vivo. The characterization of regulator Tas in the Paradox of nonpathogenicity and cytopathic effects was still unknown.Results: Foamy virus separated from different hosts could form three groups which paralleled with the worldwide distribution of hosts due to geographical isolation. Although the physicochemical properties of different Tas were mainly in line with each other, the conserved motifs analyses still suggested divergences in protein functions. The proteins identified to interact with Tas of PFV, SFVora and SFVagm displayed that the three kinds of foamy viruses regulated different signal pathways and impacted virus-host immune interaction. Interestingly, predictions of interactional factors based on protein sequence showed USP7, a kind of deubiquitinating enzyme, could binding directly to Tas which led to its ubiquitin-dependent proteasome degradation. And this results also implyed that fomay virus could hijacked cytokine USP7 to stabilize the transcriptional activator Tas by de-ubiquitylation and thereby regulate the viral life cycle.Conclusion: Our experiments help to understand the survival strategy of foamy viruses in their hosts.

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Structure of transmembrane subunits gp47 of the foamy virus envelope glycoproteins

Cited by 5 publications

References 34 publications

Structures of the Foamy virus fusion protein reveal an unexpected link with the F protein of paramyxo- and pneumoviruses

Structures of the Foamy virus fusion protein reveal an unexpected link with the F protein of paramyxo- and pneumoviruses

Viral Membrane Fusion and the Transmembrane Domain

Paradox of Nonpathogenicity and Cytopathic Effects：Characterization of Regulator Tas in Foamy Virus Evolution and De-Ubiquitylation of Tas in Virus Duplication

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