Revisiting an old friend: new findings in alphavirus structure and assembly

Button, Julie M.; Qazi, Shefah; Wang, Joseph Che Yen; Mukhopadhyay, Suchetana

doi:10.1016/j.coviro.2020.06.005

Cited by 24 publications

(17 citation statements)

References 68 publications

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“…Two recoding signals have been reported for alphaviruses: termination codon region (TCR) located at opal (UGA) termination codon at the boundary between nsP3 and nsP4 genes, and the -1 PRF signal located near the 3' end of 6K gene which leads to the production of trans -frame product that functions as an ion channel and is known to be important for neuropathogenesis in SINV. 181 , 186 , 187 NS1' protein of flaviviruses (JEV and WNV), a larger-NS1 related protein involved in viral replication and regulation of innate immune response, is also a product of -1 PRF event that occurs near the start point of NS2A gene and is playing a role in viral neuroinvasiveness. 188 ORF1a and ORF1b of coronaviruses including SARS-CoV-2 are slightly overlapping, and since ORF1b lacks translation initiation site, proteins encoded by ORF1b are translated by -1 PRF mechanism leading to the production of fusion polypeptide proteolytically cleaved by viral proteases.…”

Section: Host Pathways Exploited By +Ssrna Virusesmentioning

confidence: 99%

Antiviral strategies targeting host factors and mechanisms obliging +ssRNA viral pathogens

Mahajan

Choudhary

Kumar

2021

Bioorganic & Medicinal Chemistry

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Section: Host Pathways Exploited By +Ssrna Virusesmentioning

confidence: 99%

Antiviral strategies targeting host factors and mechanisms obliging +ssRNA viral pathogens

Mahajan

Choudhary

Kumar

2021

Bioorganic & Medicinal Chemistry

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“…TF antagonizes interferon production during early infection, while 6K forms ion channels and functions as a viroporin [ 86 , 87 , 88 ]. E3, 6K, and TF do not need to be present in a viral particle for it to be infectious [ 89 ].…”

Section: Overview Of the Alphavirus Lifecyclementioning

confidence: 99%

Alphavirus-Induced Membrane Rearrangements during Replication, Assembly, and Budding

2021

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Alphaviruses are arthropod-borne viruses mainly transmitted by hematophagous insects that cause moderate to fatal disease in humans and other animals. Currently, there are no approved vaccines or antivirals to mitigate alphavirus infections. In this review, we summarize the current knowledge of alphavirus-induced structures and their functions in infected cells. Throughout their lifecycle, alphaviruses induce several structural modifications, including replication spherules, type I and type II cytopathic vacuoles, and filopodial extensions. Type I cytopathic vacuoles are replication-induced structures containing replication spherules that are sites of RNA replication on the endosomal and lysosomal limiting membrane. Type II cytopathic vacuoles are assembly induced structures that originate from the Golgi apparatus. Filopodial extensions are induced at the plasma membrane and are involved in budding and cell-to-cell transport of virions. This review provides an overview of the viral and host factors involved in the biogenesis and function of these virus-induced structures. Understanding virus–host interactions in infected cells will lead to the identification of new targets for antiviral discovery.

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“…The nucleocapsid then binds to the cytoplasmic tail of E2 to form viral particles and initiate the budding of enveloped virions to the extracellular medium. For most alphaviruses, the 6K protein is suggested to act as an ion channel, and the E3 protein is not incorporated into virions [23,24,76,77]. Though the exact details have yet to be discovered, palmitoylated TF has been demonstrated to be crucial for virus assembly [78].…”

Section: Lifecycle Of Alphavirusmentioning

confidence: 99%

The Putative Roles and Functions of Indel, Repetition and Duplication Events in Alphavirus Non-Structural Protein 3 Hypervariable Domain (nsP3 HVD) in Evolution, Viability and Re-Emergence

Abdullah

Ahemad

Aliazis

et al. 2021

Viruses

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Alphavirus non-structural proteins 1–4 (nsP1, nsP2, nsP3, and nsP4) are known to be crucial for alphavirus RNA replication and translation. To date, nsP3 has been demonstrated to mediate many virus–host protein–protein interactions in several fundamental alphavirus mechanisms, particularly during the early stages of replication. However, the molecular pathways and proteins networks underlying these mechanisms remain poorly described. This is due to the low genetic sequence homology of the nsP3 protein among the alphavirus species, especially at its 3′ C-terminal domain, the hypervariable domain (HVD). Moreover, the nsP3 HVD is almost or completely intrinsically disordered and has a poor ability to form secondary structures. Evolution in the nsP3 HVD region allows the alphavirus to adapt to vertebrate and insect hosts. This review focuses on the putative roles and functions of indel, repetition, and duplication events that have occurred in the alphavirus nsP3 HVD, including characterization of the differences and their implications for specificity in the context of virus–host interactions in fundamental alphavirus mechanisms, which have thus directly facilitated the evolution, adaptation, viability, and re-emergence of these viruses.

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Revisiting an old friend: new findings in alphavirus structure and assembly

Cited by 24 publications

References 68 publications

Antiviral strategies targeting host factors and mechanisms obliging +ssRNA viral pathogens

Antiviral strategies targeting host factors and mechanisms obliging +ssRNA viral pathogens

Alphavirus-Induced Membrane Rearrangements during Replication, Assembly, and Budding

The Putative Roles and Functions of Indel, Repetition and Duplication Events in Alphavirus Non-Structural Protein 3 Hypervariable Domain (nsP3 HVD) in Evolution, Viability and Re-Emergence

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