Virion structure and genome delivery mechanism of sacbrood honeybee virus

Procházková, Michaela; Füzik, T.; Škubník, Karel; Moravcová, Jana; Ubiparip, Zorica; Přidal, Antonín; Plevka, Pavel

doi:10.1073/pnas.1722018115

Cited by 29 publications

(45 citation statements)

References 40 publications

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“…1F. Protruding CD-loops of various sizes in VP1 are a common feature among the invertebrate picornavirads (26,27,33,50,54) (Fig. 5).…”

Section: Resultsmentioning

confidence: 98%

“…Each major CP has one jelly-roll domain (31). Some species included in the families Picornaviridae, Dicistroviridae, Iflaviridae, and Marnaviridae encode an additional minor VP4 protein located underneath the five-fold axes (26,32,33). Some members of the family Secoviridae are composed of three CPs, equivalent to other families of the Picornavirales order, whereas others have either one (folded in three jelly-rolls) or two CPs (one large CP with two jelly-rolls and one small CP with one jelly-roll) (34).…”

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confidence: 99%

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Capsid Structure of a Marine Algal Virus of the Order Picornavirales

Munke

Kimura

Tomaru

et al. 2020

J Virol

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The order Picornavirales includes viruses that infect different kinds of eukaryotes and that share similar properties. The capsid proteins (CPs) of viruses in the order that infect unicellular organisms, such as algae, presumably possess certain characteristics that have changed little over the course of evolution, and thus these viruses may resemble the Picornavirales ancestor in some respects. Herein, we present the capsid structure of Chaetoceros tenuissimus RNA virus type II (CtenRNAV-II) determined using cryo-electron microscopy at a resolution of 3.1 Å, the first alga virus belonging to the family Marnaviridae of the order Picornavirales. A structural comparison to related invertebrate and vertebrate viruses revealed a unique surface loop of the major CP VP1 that had not been observed previously, and further, revealed that another VP1 loop obscures the so-called canyon, which is a host-receptor binding site for many of the mammalian Picornavirales viruses. VP2 has an N-terminal tail, which has previously been reported as a primordial feature of Picornavirales viruses. The above-mentioned and other critical structural features provide new insights on three long-standing theories about Picornavirales: (i) the canyon hypothesis, (ii) the primordial VP2 domain swap, and (iii) the hypothesis that alga Picornavirales viruses could share characteristics with the Picornavirales ancestor. IMPORTANCE Identifying the acquired structural traits in virus capsids is important for elucidating what functions are essential among viruses that infect different hosts. The Picornavirales viruses infect a broad spectrum of hosts, ranging from unicellular algae to insects and mammals and include many human pathogens. Those viruses that infect unicellular protists, such as algae, are likely to have undergone fewer structural changes during the course of evolution compared to those viruses that infect multicellular eukaryotes and thus still share some characteristics with the Picornavirales ancestor. This article describes the first atomic capsid structure of an alga Marnavirus, CtenRNAV-II. A comparison to capsid structures of the related invertebrate and vertebrate viruses identified a number of structural traits that have been functionally acquired or lost during the course of evolution. These observations provide new insights on past theories on the viability and evolution of Picornavirales viruses.

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“…1F. Protruding CD-loops of various sizes in VP1 are a common feature among the invertebrate picornavirads (26,27,33,50,54) (Fig. 5).…”

Section: Resultsmentioning

confidence: 98%

mentioning

confidence: 99%

Capsid Structure of a Marine Algal Virus of the Order Picornavirales

Munke

Kimura

Tomaru

et al. 2020

J Virol

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“…Sacbrood virus (SBV) is a common virus belonging to the genus Iflavirus and causes failure to pupate and subsequent death in Apis mellifera [1][2][3]. It was the first identified iflavirus in European honey bees and a strain has evolved that also infects Asian honey bees, Apis cerana [4,5].…”

Section: Introductionmentioning

confidence: 99%

Visualizing Sacbrood Virus of Honey Bees via Transformation and Coupling with Enhanced Green Fluorescent Protein

Jin

Mehmood

Zhang

et al. 2020

Viruses

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Sacbrood virus (SBV) of honey bees is a picornavirus in the genus Iflavirus. Given its relatively small and simple genome structure, single positive-strand RNA with only one ORF, cloning the full genomic sequence is not difficult. However, adding nonsynonymous mutations to the bee iflavirus clone is difficult because of the lack of information about the viral protein processes. Furthermore, the addition of a reporter gene to the clones has never been accomplished. In preliminary trials, we found that the site between 3′ untranslated region (UTR) and poly(A) can retain added sequences. We added enhanced green fluorescent protein (EGFP) expression at this site, creating a SBV clone with an expression tag that does not affect virus genes. An intergenic region internal ribosome entry site (IRES) from Black queen cell virus (BQCV) was inserted to initiate EGFP expression. The SBV-IRES-EGFP clone successfully infected Apis cerana and Apis mellifera, and in A. cerana larvae, it was isolated and passaged using oral inoculation. The inoculated larvae had higher mortality and the dead larvae showed sacbrood symptoms. The added IRES-EGFP remained in the clone through multiple passages and expressed the expected EGFP in all infected bees. We demonstrated the ability to add gene sequences in the site between 3′-UTR and poly(A) in SBV and the potential to do so in other bee iflaviruses; however, further investigations of the mechanisms are needed. A clone with a desired protein expression reporter will be a valuable tool in bee virus studies.

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“… Fernandez de la Mora, 2015 ; Fernandez de la Mora, 2018 ; Lübbert and Peukert, 2019 ; Perez-Lorenzo et al, 2020 ; Procházkováa et al, 2018 ; Ribière et al, 2010 ; Trimpin et al, 2007 ; Uetrecht et al, 2010 ; Weiss et al, 2019 .…”

Section: Uncited Referencesunclassified

Exceeding a resolving power of 50 for virus size determination by differential mobility analysis

Perez-Lorenzo

Mora

2021

Journal of Aerosol Science

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A recently described DMA designed for high resolution viral particle analysis ( Perez-DMA; Perez-Lorenzo et al, 2020) is modified to decrease the relative peak full width at half maximum ( FWHM) below previously achieved ≈3.3%. The electrode radii at the outlet slit ( R 1 = 1.01 cm; R 2 = 2 cm) and the working length are almost unchanged ( L = 114.9 vs. 116 mm). The laminarization trumpet and the radius of the curve merging the trumpet to the working section are both considerably widened to improve gas flow laminarization. DMA evaluation with salt clusters is improved by reducing the flow resistance at the gas outlet, to reach substantially larger sheath gas flow rates Q ˜ 1700 L/min. Tests with tetraheptylammonium bromide clusters with a center rod diverging at 3 o demonstrate FWHM<2.7%, without indications of performance loss due to turbulence even at 1700 L/min. Correcting these high flow rate data for diffusive broadening reveals a maximal DMA FWHM in the limit of non-diffusing particles and zero sample flow, FWHM ∞ = 1.8%. An uncorrected peak width approaching 2% is independently demonstrated at much lower flow rates of sheath gas with two recently described bee virus particle standards having singularly narrow size distributions at mean diameters of 38 and 17 nm. Correcting raw 38 nm particle peak widths for broadening due to diffusion and aerosol to sheath gas flow rate ratio q/Q shows an even more ideal response with FWHM ∞ <1%, where this value includes nonidealities in the DMA as well as possible lack of monodispersity in the viral particles.

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Virion structure and genome delivery mechanism of sacbrood honeybee virus

Cited by 29 publications

References 40 publications

Capsid Structure of a Marine Algal Virus of the Order Picornavirales

Capsid Structure of a Marine Algal Virus of the Order Picornavirales

Visualizing Sacbrood Virus of Honey Bees via Transformation and Coupling with Enhanced Green Fluorescent Protein

Exceeding a resolving power of 50 for virus size determination by differential mobility analysis

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