Early interactions between poliovirus and ERK cells: Some observations on the nature and significance of the rejected particles

Fenwick, M. L.; Cooper, Penny

doi:10.1016/0042-6822(62)90007-7

Cited by 129 publications

(74 citation statements)

References 16 publications

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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.

303

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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Section: Receptor Binding and Cell Entrymentioning

confidence: 99%

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

Hogle

2002

Annu. Rev. Microbiol.

303

305

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“…Binding of these viruses to soluble monomeric receptor protein in vitro triggers an irreversible conformational change in the virus particle that manifests as a change in the sedimentation characteristics of the virus (from the 160 S mature virion to the 135 S A-particle) (8). Similar changes in sedimentation coefficient are seen when the virus interacts with the receptor at the cell surface, and such transformations are thought to be essential for successful entry and infection (9,10). The structural rearrangements that lead to this change in sedimentation include loss of VP4 and externalization of the N terminus of VP1, which is normally located at the inner surface of the capsid surrounding the pentameric apices in the mature virion.…”

mentioning

confidence: 90%

The Structure of Echovirus Type 12 Bound to a Two-domain Fragment of Its Cellular Attachment Protein Decay-accelerating Factor (CD 55)

Bhella

Goodfellow

Roversi

et al. 2004

Journal of Biological Chemistry

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Echovirus type 12 (EV12), an Enterovirus of the Picornaviridae family, uses the complement regulator decayaccelerating factor (DAF, CD55) as a cellular receptor. We have calculated a three-dimensional reconstruction of EV12 bound to a fragment of DAF consisting of short consensus repeat domains 3 and 4 from cryo-negative stain electron microscopy data (EMD code 1057). This shows that, as for an earlier reconstruction of the related echovirus type 7 bound to DAF, attachment is not within the viral canyon but occurs close to the 2-fold symmetry axes. Despite this general similarity our reconstruction reveals a receptor interaction that is quite different from that observed for EV7. Fitting of the crystallographic co-ordinates for DAF 34 and EV11 into the reconstruction shows a close agreement between the crystal structure of the receptor fragment and the density for the virus-bound receptor, allowing unambiguous positioning of the receptor with respect to the virion (PDB code 1UPN). Our finding that the mode of virusreceptor interaction in EV12 is distinct from that seen for EV7 raises interesting questions regarding the evolution and biological significance of the DAF binding phenotype in these viruses.

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“…Of several stages detected during the penetration of poliovirus, the transition to non-recoverability of infectivity with pH 2.5 buffer ('acid-irreversible eclipse') appears to be the last (Fenwick & Cooper, 1962). The rate of acid-irreversible eclipse in the system used (Fig.…”

Section: Resultsmentioning

confidence: 98%

Synchrony and the Elimination of Chance Delays in the Growth of Poliovirus

Cooper

1964

Journal of General Microbiology

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SUMMARYThe effect of multiplicity of infection on the growth kinetics of poliovirus suggests that the eclipse period usual for singly infected cells (3.6-3-8 hr) includes variable delays averaging about 1 hr. These delays are overcome at multiplicities above 3, and are sometimes spontaneously absent. They are ascribed largely to chance effects, and lead to markedly asynchronous maturation of virus ; in their absence, maturation is almost synchronous.The kinetics of acid-irreversible eclipse and of the development of antiserum resistance show that about half of the delays must occur during viral penetration; in support of this, virus growth initiated with infective RNA is 0.5 hr less delayed than that of intact virus, although otherwise similar. However, infective RNA synthesis was not detected earlier than 2 hr after infection, even in the absence of chance delays.

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Early interactions between poliovirus and ERK cells: Some observations on the nature and significance of the rejected particles

Cited by 129 publications

References 16 publications

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

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

The Structure of Echovirus Type 12 Bound to a Two-domain Fragment of Its Cellular Attachment Protein Decay-accelerating Factor (CD 55)

Synchrony and the Elimination of Chance Delays in the Growth of Poliovirus

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