Studies on the in vitro uncoating of poliovirus II. Characteristics of the membrane-modified particle

Sena, John De; Mandel, Benjamin

doi:10.1016/0042-6822(77)90130-1

Cited by 125 publications

(99 citation statements)

References 17 publications

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“…Protease treatment of 'A' particles produced another subviral particle, which sedimented at 70S to 80S, referred to as a 'C' particle (DeSena & Mandel, 1977), and continued proteolysis released viral RNA presumably by degradation of the 'C' particle. In the present study, experiments were performed to determine whether these in vitro systems represented reactions which occur during virus uncoating by cells.…”

Section: Discussionmentioning

confidence: 99%

Proteolytic Cleavage of VP1 in 'A' Particles of Coxsackievirus B3 Does Not Appear to Mediate Virus Uncoating by HeLa Cells

McGeady

Crowell

1981

Journal of General Virology

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SUMMARY'A' particles of Coxsackievirus B3 were generated from native virus by heating and purified by sucrose gradient centrifugation. These particles were found to be similar to 'A' particles formed by elution from cellular receptors of HeLa cells. Electrophoretic analysis of [35S]methionine-labelled 'A' particles revealed that treatment of the particles with chymotrypsin resulted in the cleavage of VP 1 and the formation of a cleavage product which migrated between VP2 and VP3. Analysis of the protease-treated material on sucrose gradients revealed a ribonuclease-sensitive particle which sedimented more slowly than an 'A' particle. This particle apparently degraded to release the viral RNA, thereby providing an in vitro model for protease-mediated uncoating of 'A' particles. The subviral particles of Coxsackievirus B3 were found to be immunoprecipitable with heterotypic Coxsackievirus group B antisera, thereby providing a method for the recovery of products produced in the cell early in infection. Infected cells which had been treated to remove unreacted virus were disrupted, and the lysates were reacted with heterotypic antisera. Analysis of the precipitated material revealed that no cleavage products were formed and no polypeptides were lost. Therefore, it appears that proteolysis is not involved in the uncoating of Coxsackievirus B3 in infected cells.

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Section: Discussionmentioning

confidence: 99%

Proteolytic Cleavage of VP1 in 'A' Particles of Coxsackievirus B3 Does Not Appear to Mediate Virus Uncoating by HeLa Cells

McGeady

Crowell

1981

Journal of General Virology

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“…STRUCTURAL ALTERATIONS ASSOCIATED WITH CELL ENTRY For polioviruses, rhinoviruses, and most related enteroviruses, binding cells expressing the receptor at physiological temperatures result in the induction of conformational changes in the virus to produce a particle called the A particle or 135S particle (29,33). In the course of a typical experimental infection, a significant fraction of the A particle subsequently elutes from cells in what is thought to represent an abortive infection.…”

Section: Receptor Binding and Cell Entrymentioning

confidence: 99%

Poliovirus Cell Entry: Common Structural Themes in Viral Cell Entry Pathways

Hogle

2002

Annu. Rev. Microbiol.

313

305

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Structural studies of polio-and closely related viruses have provided a series of snapshots along their cell entry pathways. Based on the structures and related kinetic, biochemical, and genetic studies, we have proposed a model for the cell entry pathway for polio-and closely related viruses. In this model a maturation cleavage of a capsid protein precursor locks the virus in a metastable state, and the receptor acts like a transition-state catalyst to overcome an energy barrier and release the mature virion from the metastable state. This initiates a series of conformational changes that allow the virus to attach to membranes, form a pore, and finally release its RNA genome into the cytoplasm. This model has striking parallels with emerging models for the maturation and cell entry of more complex enveloped viruses such as influenza virus and HIV.

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“…In poliovirus, the A-particle is more susceptible to proteolysis than the intact virion and is characterized by the irreversible externalization of the N terminus of VP1 (38)(39)(40). To assess and compare the proteolytic sensitivities of the full virion and the uncoating intermediate, we performed trypsin digestion experiments.…”

Section: Crystallization Of Two Forms Of Ev71mentioning

confidence: 99%

Human Enterovirus 71 Uncoating Captured at Atomic Resolution

Lyu

Ding

Han

et al. 2014

J Virol

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Human enterovirus 71 (EV71) is the major causative agent of severe hand-foot-and-mouth diseases (HFMD) in young children, and structural characterization of EV71 during its life cycle can aid in the development of therapeutics against HFMD. Here, we present the atomic structures of the full virion and an uncoating intermediate of a clinical EV71 C4 strain to illustrate the structural changes in the full virion that lead to the formation of the uncoating intermediate prepared for RNA release. Although the VP1 N-terminal regions observed to penetrate through the junction channel at the quasi-3-fold axis in the uncoating intermediate of coxsackievirus A16 were not observed in the EV71 uncoating intermediate, drastic conformational changes occur in this region, as has been observed in all capsid proteins. Additionally, the RNA genome interacts with the N-terminal extensions of VP1 and residues 32 to 36 of VP3, both of which are situated at the bottom of the junction. These observations highlight the importance of the junction for genome release. Furthermore, EV71 uncoating is associated with apparent rearrangements and expansion around the 2-and 5-fold axes without obvious changes around the 3-fold axes. Therefore, these structures enabled the identification of hot spots for capsid rearrangements, which led to the hypothesis that the protomer interface near the junction and the 2-fold axis permits the opening of large channels for the exit of polypeptides and viral RNA, which is an uncoating mechanism that is likely conserved in enteroviruses. IMPORTANCE Human enterovirus 71 (EV71) is the major causative agent of severe hand-foot-and-mouth diseases (HFMD Human enterovirus 71 (EV71) is the leading causative agent for severe hand-foot-and-mouth diseases (HFMD) in infants and young children (1), and EV71 infection has caused significant morbidity and mortality in the Asia-Pacific regions. During 2008 to 2012, numerous outbreaks of HFMD occurred in mainland China, with over 2,000 fatal cases reported (www.chinacdc.cn). However, vaccines and effective drugs remain unavailable. EV71 belongs to Enterovirus species A within the Enterovirus genus of the Picornaviridae (2). The EV71 virion contains a singlestranded positive-sense RNA genome of 7.5 kb. The viral capsid, which has a diameter of approximately 300 Å, is composed of 60 copies each of VP1 to VP4 (3, 4) that are organized onto a quasi-Tϭ3 icosahedral lattice. The capsid proteins VP1, VP2, and VP3 each possess a ␤-sandwich jelly roll fold and form the outer surface of the capsid shell, whereas VP4 is situated inside the shell. The capsid surface is characterized by a depression encircling each 5-fold symmetry axis, which is referred to as the "canyon" and often contains the receptor-binding site in picornaviruses (5, 6). The hydrophobic pocket of VP1, which is located at the bottom of the canyon, contains a lipid moiety termed the "pocket factor," which likely stabilizes the mature virion. As observed in poliovirus and certain picornaviruses, receptor bindin...

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Studies on the in vitro uncoating of poliovirus II. Characteristics of the membrane-modified particle

Cited by 125 publications

References 17 publications

Proteolytic Cleavage of VP1 in 'A' Particles of Coxsackievirus B3 Does Not Appear to Mediate Virus Uncoating by HeLa Cells

Proteolytic Cleavage of VP1 in 'A' Particles of Coxsackievirus B3 Does Not Appear to Mediate Virus Uncoating by HeLa Cells

Poliovirus Cell Entry: Common Structural Themes in Viral Cell Entry Pathways

Human Enterovirus 71 Uncoating Captured at Atomic Resolution

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