Insights into Minor Group Rhinovirus Uncoating: The X-ray Structure of the HRV2 Empty Capsid

Garriga, Damià; Pickl‐Herk, Angela; Luque, Daniel; Wruss, Jürgen; Castón, José R.; Blaas, Dieter; Verdaguer, N.

doi:10.1371/journal.ppat.1002473

Cited by 101 publications

(164 citation statements)

References 73 publications

(95 reference statements)

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“…1C). Thus, the stability of SBPV virions is similar to that of previously studied vertebrate picornaviruses (19,22,34).…”

Section: Resultssupporting

confidence: 76%

“…In addition, the subunits VP1, VP2, and VP3 rotate 3.1°, 1.7°, and 1.9°, respectively. These shifts and rotations are approximately one-half of those previously reported for the conversion of enteroviruses to A particles (19,20). The rotations together with small conformational changes to residues located at the periphery of the pentamers allow the capsid proteins to remain in contact after the expansion of the capsid.…”

Section: Genome Release Is Associated With Formation Of Pores At Thresupporting

confidence: 51%

“…1073/pnas.1616562114/-/DCSupplemental. particle surface, and released VP4 subunits (19)(20)(21)(22)(23)(24). Amphipathic sequences from the N termini of VP1 and myristoylated VP4 subunits interact with endosome membranes and enable the delivery of enterovirus genomes into the cell cytoplasm (25)(26)(27).…”

mentioning

confidence: 99%

“…Amphipathic sequences from the N termini of VP1 and myristoylated VP4 subunits interact with endosome membranes and enable the delivery of enterovirus genomes into the cell cytoplasm (25)(26)(27). It has been previously proposed that the enterovirus genome leaves the capsid via a pore located at a twofold icosahedral axis (19)(20)(21). The resulting empty capsids are conventionally referred to as B particles (19).…”

mentioning

confidence: 99%

“…It has been previously proposed that the enterovirus genome leaves the capsid via a pore located at a twofold icosahedral axis (19)(20)(21). The resulting empty capsids are conventionally referred to as B particles (19). Acidic pH in the endosomes also induces the genome release of the aphthoviruses foot and mouth disease virus (FMDV) and equine rhinitis A virus (ERAV) (28)(29)(30).…”

mentioning

confidence: 99%

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Cryo-EM study of slow bee paralysis virus at low pH reveals iflavirus genome release mechanism

Kalynych

Füzik

Přidal

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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Viruses from the family Iflaviridae are insect pathogens. Many of them, including slow bee paralysis virus (SBPV), cause lethal diseases in honeybees and bumblebees, resulting in agricultural losses. Iflaviruses have nonenveloped icosahedral virions containing single-stranded RNA genomes. However, their genome release mechanism is unknown. Here, we show that low pH promotes SBPV genome release, indicating that the virus may use endosomes to enter host cells. We used cryo-EM to study a heterogeneous population of SBPV virions at pH 5.5. We determined the structures of SBPV particles before and after genome release to resolutions of 3.3 and 3.4 Å, respectively. The capsids of SBPV virions in low pH are not expanded. Thus, SBPV does not appear to form "altered" particles with pores in their capsids before genome release, as is the case in many related picornaviruses. The egress of the genome from SBPV virions is associated with a loss of interpentamer contacts mediated by N-terminal arms of VP2 capsid proteins, which result in the expansion of the capsid. Pores that are 7 Å in diameter form around icosahedral threefold symmetry axes. We speculate that they serve as channels for the genome release. Our findings provide an atomic-level characterization of the genome release mechanism of iflaviruses.electron microscopy | uncoating | honeybee | structure | virus

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“…1C). Thus, the stability of SBPV virions is similar to that of previously studied vertebrate picornaviruses (19,22,34).…”

Section: Resultssupporting

confidence: 76%

Section: Genome Release Is Associated With Formation Of Pores At Thresupporting

confidence: 51%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Cryo-EM study of slow bee paralysis virus at low pH reveals iflavirus genome release mechanism

Kalynych

Füzik

Přidal

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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Interacting motif networks located in hotspots associated with RNA release are conserved in Enterovirus capsids

2017

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Enteroviruses are responsible for a multitude of human diseases. Expansion of the virus capsid is associated with a cascade of conformational changes that allow the subsequent release of RNA. For the first time, this study presents a comprehensive bioinformatic screen for the prediction of interacting motifs within intraprotomer interfaces and across respective interfaces surrounding the fivefold and twofold axes. The results identify a network of conserved motif residues involved in interactions in enteroviruses that may be critical to capsid stabilisation, providing guidelines towards developing antivirals that interfere with viral expansion during RNA release.

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Characterization of rhinovirus subviral A particles via capillary electrophoresis, electron microscopy and gas phase electrophoretic mobility molecular analysis: Part II

et al. 2013

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Human rhinoviruses (HRVs) are valuable tools in the investigation of early viral infection steps due to their far reaching (although still incomplete) characterization. During endocytosis, native virions first loose one of the four capsid proteins (VP4); corresponding particles sediment at 135S and were termed subviral A particles. Subsequently, the viral RNA genome leaves the viral shell giving rise to empty capsids. In continuation of our previous work with HRV serotype 2 (HRV2) intermediate subviral particles, in which we were able to discriminate by CE even between two intermediates (AI and AII) of virus uncoating, we further concentrated on the characterization of AI particles with the electrophoretic mobility of around -17.2 × 10(-9) m(2) /Vs at 20°C. In the course of our present work we related these particles to virions as previously described at the subviral A stage of uncoating (and as such sedimenting at 135S) by determination of their protein and RNA content--in comparison to native virions AI particles did not include VP4, however, still 93% of their initial RNA content. Binding of an mAb specific for subviral particles demonstrated antigenic rearrangements on the capsid surface at the AI stage. Furthermore, we investigated possible factors stabilizing intermediates of virus uncoating. We could exclude the influence of the previously suspected so-called contaminant of virus preparation on HRV2 subviral particle formation. Instead, we regarded other factors being part of the virus preparation system and found a dependence of AI particle formation on the presence of divalent cations.

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Insights into Minor Group Rhinovirus Uncoating: The X-ray Structure of the HRV2 Empty Capsid

Cited by 101 publications

References 73 publications

Cryo-EM study of slow bee paralysis virus at low pH reveals iflavirus genome release mechanism

Cryo-EM study of slow bee paralysis virus at low pH reveals iflavirus genome release mechanism

Interacting motif networks located in hotspots associated with RNA release are conserved in Enterovirus capsids

Characterization of rhinovirus subviral A particles via capillary electrophoresis, electron microscopy and gas phase electrophoretic mobility molecular analysis: Part II

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