The Unique, the Known, and the Unknown of Spumaretrovirus Assembly

Lindemann, Dirk; Hütter, Sylvia; Wei, Guochao; Löchelt, Martin

doi:10.3390/v13010105

Cited by 8 publications

(9 citation statements)

References 121 publications

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“…S4). This finding expends the repertoire of unique FV features (assembly, particle release 36 , replication 37 ) that are not shared with Orthoretroviruses, and is consistent with the lack of Env sequence conservation between Orthoretroviruses and FVs.…”

Section: Discussionsupporting

confidence: 76%

The crystal structure of a simian Foamy Virus receptor binding domain provides clues about entry into host cells

Fernández

Dynesen

Coquin

et al. 2022

Preprint

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The surface envelope glycoprotein (Env) of all retroviruses mediates virus binding to cells and fusion of the viral and cellular membranes. A structure-function relationship for the HIV Env, which belongs to the Orthoretrovirus subfamily, has been well established. Structural information is however largely missing for the Env of Foamy viruses (FVs), the second retroviral subfamily. FV Envs lack sequence similarity with their HIV counterpart. We present the X-ray structure of the receptor binding domain (RBD) of a simian FV Env at 2.6 Å resolution, revealing two subdomains and an unprecedented fold. We have generated a model for the organization of the RBDs within the trimeric Env which indicates that the upper subdomain is important for stabilization of the full-length Env, and have demonstrated that residues K342, R343, R359 and R369 in the lower subdomain play key roles in the interaction of the RBD and viral particles with heparan sulfate.

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Section: Discussionsupporting

confidence: 76%

The crystal structure of a simian Foamy Virus receptor binding domain provides clues about entry into host cells

Fernández

Dynesen

Coquin

et al. 2022

Preprint

View full text Add to dashboard Cite

show abstract

“…S 4 ). This finding expands the repertoire of unique FV features (assembly, particle release 36 , replication 37 ) that are not shared with Orthoretroviruses, and is not surprising considering the lack of Env sequence conservation between the Orthoretrovirinae and Spumaretrovirinae subfamilies.…”

Section: Discussionmentioning

confidence: 59%

The crystal structure of a simian Foamy Virus receptor binding domain provides clues about entry into host cells

et al. 2023

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The surface envelope glycoprotein (Env) of all retroviruses mediates virus binding to cells and fusion of the viral and cellular membranes. A structure-function relationship for the HIV Env that belongs to the Orthoretrovirus subfamily has been well established. Structural information is however largely missing for the Env of Foamy viruses (FVs), the second retroviral subfamily. In this work we present the X-ray structure of the receptor binding domain (RBD) of a simian FV Env at 2.57 Å resolution, revealing two subdomains and an unprecedented fold. We have generated a model for the organization of the RBDs within the trimeric Env, which indicates that the upper subdomains form a cage-like structure at the apex of the Env, and identified residues K342, R343, R359 and R369 in the lower subdomain as key players for the interaction of the RBD and viral particles with heparan sulfate.

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“…Foamy viruses encode the canonical gag, pol and env genes flanked by the long terminal repeats (LTRs) and additional accessory genes designated as tas (formerly designated as bel 1) and bel2 open reading frames (ORF). The accessory gene Bet is transcribed by a spliced product of the N-terminal tas and the complete bel2 ORF ( Lindemann et al., 2021 ).…”

Section: Simian Foamy Viruses (Sfvs )mentioning

confidence: 99%

Transmission of infectious viruses in the natural setting at human-animal interface

Nandi

Rathore²,

Mathur³

2021

Current Research in Virological Science

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Most viral pathogens causing epidemics and pandemics are zoonotic, emerging from wildlife reservoirs like SARS CoV2 causing the global Covid-19 pandemic, although animal origin of this virus remains a mystery. Cross-species transmission of pathogens from animals to humans is known as zoonosis. However, pathogens are also transmitted from humans to animals in regions where there is a close interaction between animals and humans by ‘reverse transmission’ (anthroponosis). Molecular evidence for the transmission of two zoonotic RNA viruses at the human-monkey interface in Rajasthan forests is presented here: a) the apathogenic Simian Foamy Viruses (SFV), and b): Influenza A viruses (IAV)-like virus, etiologic agent for human flu infecting wild Indian rhesus monkeys inhabiting Rajasthan forests. The data provide critical information on ecology and evolution of viruses of Public Health relevance. During replication, viral genomes mutate along the transmission route to adapt to the new hosts, generating new variants that are likely to have properties different from the founder viruses. Wild Indian monkeys are under-sampled for monitoring infectious diseases mainly because of the difficulties with sample collection. Monkeys are perceived as religious icons by the Hindus in India. It is extremely difficult to obtain permission from the Forest and Wildlife Department government authorities to collect wild simian blood samples for surveillance of infectious diseases caused by viral pathogens. Reducing animal-human contact and affordable vaccination are two relevant anti-viral strategies to counteract the spread of infectious zoonotic pathogens. Genbank Accession numbers : Indian SFVmac: ADN94420, IAV like virus: MZ298601.

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The Unique, the Known, and the Unknown of Spumaretrovirus Assembly

Cited by 8 publications

References 121 publications

The crystal structure of a simian Foamy Virus receptor binding domain provides clues about entry into host cells

The crystal structure of a simian Foamy Virus receptor binding domain provides clues about entry into host cells

The crystal structure of a simian Foamy Virus receptor binding domain provides clues about entry into host cells

Transmission of infectious viruses in the natural setting at human-animal interface

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