The poliovirus 135S particle is infectious

Curry, Stephen; Chow, Marie; Hogle, James M.

doi:10.1128/jvi.70.10.7125-7131.1996

Cited by 125 publications

(64 citation statements)

References 45 publications

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“…However, because both of the viral particles tested in these studies are present during the entry process, it is possible that these channels are important for poliovirus entry into cells. This hypothesis then raises the possibility of infection of cells believed heretofore to be nonpermissive and are consistent with the recent findings that 135S can infect nonsusceptible cells in a receptor-independent manner (3).…”

Section: Discussionsupporting

confidence: 89%

Characterization of the ion channels formed by poliovirus in planar lipid membranes

Tosteson

Chow

1997

J Virol

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The steps in poliovirus infection leading to viral entry and uncoating are not well understood. Current evidence suggests that the virus first binds to a plasma membrane-bound receptor present in viable cells, leading to a conformational rearrangement of the viral proteins such that the virus crosses the membrane and releases the genomic RNA. The studies described in this report were undertaken to determine if poliovirus (160S) as well as one of the subviral particles (135S) could interact with membranes lacking poliovirus receptors in an effort to begin to understand the process of uncoating of the virus. We report that both forms of viral particles, 160S and 135S, interact with lipid membranes and induce the formation of ion-permeable channels in a manner that does not require acid pH. The channels induced by the viral particles 160S have a voltage-dependent conductance which depends on the ionic composition of the medium. Our findings raise the possibility that viral entry into cells may be mediated by direct interaction of viral surface proteins with membrane lipids.Poliovirus is a prototypical member of the Picornaviridae family. The plus-stranded RNA genome of this nonenveloped virus is tightly packed within an icosahedrally symmetric spherical shell which is composed of 60 copies of each of four proteins (VP1 to VP4). The myristoylated VP4 and the aminoterminal sequences of the other three capsid proteins are located on the inner surface of the poliovirus virion (8).Infection of cells by poliovirus starts as the virus particle attaches to the receptor at the cell membrane (2, 6). Receptor binding leads to a conformational transition that results in altered particles which lack VP4 and sediment with a coefficient of 135S (compared to 16 0S for the intact virion) (3a, 6, 9). This alteration in sedimentation behavior is further accompanied by the relocation and exposure of most of the aminoterminal regions of VP1 from the inner to the outer surface of the virion shell. Exposure of the amino-terminal regions of VP1 confers membrane binding properties to the 135S particles, which has been observed by Fricks and Hogle (5), using a liposome flotation method. However, the subsequent stages of penetration and uncoating remain poorly defined.For viral replication to take place, the viral RNA must traverse the plasma membrane and be uncoated and released to the cytosol. Several hypotheses have been put forth to explain viral entry and uncoating, ranging from receptor-mediated endocytosis of the whole virion, to direct penetration of the plasma membrane by the 160S particle (hereafter referred to as simply 160S), to entry of the subviral particle 135S by either of those mechanisms (references 1 and 13 and references therein). Binding and anchoring of the viral particle to a membrane are required steps in any of these hypotheses.In this report, we present evidence that domains of the native virion (160S) and the receptor-altered viral particle (135S) bind and interact with lipid bilayers to form ion-permeable channels...

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Section: Discussionsupporting

confidence: 89%

Characterization of the ion channels formed by poliovirus in planar lipid membranes

Tosteson

Chow

1997

J Virol

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“…Alteration and virus entry can be blocked by antiviral compounds such as arildone and disoxaril, and drug-resistant viral mutants are capable of undergoing alteration in the presence of the inhibitors (6,16,38,56). Altered particles contain full-length RNA (10) and can initiate a productive infection when very high concentrations of particles are used (9). These results have been interpreted to mean that the altered particle is an essential intermediate in virus entry (reviewed in reference 15).…”

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confidence: 99%

Cold-adapted poliovirus mutants bypass a postentry replication block

Dove

Racaniello

1997

J Virol

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In the current model of poliovirus entry, the initial interaction of the native virion with its cellular receptor is followed by a transition to an altered form, which then acts as an intermediate in viral entry. While the native virion sediments at 160S in a sucrose gradient, the altered particle sediments at 135S, has lost the coat protein VP4, and has become more hydrophobic. Altered particles can be found both associated with cells and in the culture medium. It has been hypothesized that the cell-associated 135S particle releases the viral genome into the cell cytoplasm and that nonproductive transitions to the 135S form are responsible for the high particleto-PFU ratio observed for polioviruses. At 25°C, a temperature at which the transition to 135S particles does not occur, the P1/Mahoney strain of poliovirus was unable to replicate, and cold-adapted (ca) mutants were selected from the population. These mutants have not gained the ability to convert to 135S particles at 25°C, and the block to wild-type (wt) infection at low temperatures is not at the level of cellular entry. The particle-to-PFU ratio of poliovirus does not change at 25°C in the absence of alteration. Three independent amino acid changes in the 2C coding region were identified in ca mutants, at positions 218 (Val to Ile), 241 (Arg to Ala), and 309 (Met to Val). Introduction of any of these mutations individually into wt poliovirus by site-directed mutagenesis confers the ca phenotype. All three serotypes of the Sabin vaccine strains and the P3/Leon strain of poliovirus also exhibit the ca phenotype. These results do not support a model of poliovirus entry into cells that includes an obligatory transition to the 135S particle.

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“…Differences between host cell-induced structural transitions of PV1/ Mahoney and PV3/Saukett have been described earlier, the uncoating of PV3 being remarkably slower in GMK cells (Piirainen et al, 1996). The 135S particles produced by an in vitro conversion method have been described previously, and although it is not certain that these particles are identical with those seen at the early steps of infection, there is thus far no evidence to the contrary (Lonberg-Holm et al, 1976;Wetz and Kucinski 1991;Curry et al, 1996;Belnap et al, 2000).…”

Section: Figmentioning

confidence: 82%

Variation in Liposome Binding among Enteroviruses

2001

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Liposome-binding properties of native virions and in vitro generated 135S particles of eight enteroviruses were studied. The temperature required for the structural transition from the native 160S virion to a 135S particle was virus-specific, ranging from +38 degrees C to more than +50 degrees C. While the 135S particles of poliovirus 1/Mahoney (PV1) and coxsackievirus A21 (CAV21) were capable of binding to liposomes, the other viruses showed minimal binding. Both of the viruses that bound to liposomes as 135S particles also bound as native virions. In addition, PV3/Sabin bound to liposomes as native virions but not as 135S particles, and the flotation patterns were different from those of PV1 and CAV21. The nonbinding viruses included coxsackieviruses A7, A9, A16, and B5, and enterovirus 68. The results follow the new classification of enteroviruses, as CAV21 is a member of the human enterovirus C species, which is genetically close to the poliovirus species.

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The poliovirus 135S particle is infectious

Cited by 125 publications

References 45 publications

Characterization of the ion channels formed by poliovirus in planar lipid membranes

Characterization of the ion channels formed by poliovirus in planar lipid membranes

Cold-adapted poliovirus mutants bypass a postentry replication block

Variation in Liposome Binding among Enteroviruses

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