Studies on the in vitro uncoating of poliovirus III. Roles of membrane-modifying and -stabilizing factors in the generation of subviral particles

Sena, John De; Torian, Bruce E.

doi:10.1016/0042-6822(80)90373-6

Cited by 24 publications

(5 citation statements)

References 23 publications

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“…This conversion of the virion particle is considered to result in virus uncoating, that is, the formation of an 80S particle which has lost the RNA genome in addition to the VP4. A similar alteration of poliovirus particles is seen when susceptible cell extracts are mixed with poliovirus (9)(10)(11)15). Conversion of poliovirus is also observed when the virus is mixed with nonsusceptible insect cells infected with a recombinant baculovirus carrying a cDNA encoding hPVR (20).…”

mentioning

confidence: 68%

Interaction of Poliovirus with Its Purified Receptor and Conformational Alteration in the Virion

Arita

Koike

Aoki

et al. 1998

J Virol

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Polypeptides of amino acids 1 to 241 (PVR241) and 1 to 330 (PVR330) of the human poliovirus receptor (hPVR) were produced in a baculovirus expression system. PVR241 contained extracellular domains 1 and 2 of hPVR, and PVR330 contained extracellular domains 1, 2, and 3. These peptides were purified by immunoaffinity column chromatography with an anti-hPVR monoclonal antibody (MAb). After the purification, PVR241 and PVR330 appeared to retain their native conformation as judged by reactivity with an anti-PVR MAb that recognized domain 1 of hPVR in a conformation-dependent manner. The virulent Mahoney strain of poliovirus type 1 was mixed with the purified PVRs in various concentrations. An average of at least 43 PVR330 molecules were able to bind to one virion particle under the conditions used. The equilibrium dissociation constant between the PVR330 molecule and the PVR binding site (canyon) on the virion was determined to be 4.50 ± (0.86) × 10−8 M at 4°C. Higher rates of conformational change of the virus (160S) to 135S and 80S particles were observed as the concentration of PVR330 was increased. In this in vitro system, the ratio of the amount of the 135S particle to that of the 80S particle seemed to be always constant. After the disappearance of the 160S particle, the amount of the 80S particle was not increased by further incubation at 37°C. These results suggested that the 80S particle was not derived from the 135S particle under the conditions used in this study.

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confidence: 68%

Interaction of Poliovirus with Its Purified Receptor and Conformational Alteration in the Virion

Arita

Koike

Aoki

et al. 1998

J Virol

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“…Recently, a membrane fraction prepared with the aid of nonionic detergents was shown to modify poliovirions to a form similar if not identical to A particles. Further incubation of the modified particles with membranes or treatment with chymotrypsin caused additional modification (i.e., loss of VP2 and sensitivity to RNase) (58). These data suggest a multistep uncoating process.…”

Section: Fine Structure Of Picornavirionsmentioning

confidence: 80%

Picornaviral structure and assembly.

Putnak¹,

Phillips²

1981

Microbiological Reviews

117

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“…Altered particles, sedimenting at a lower rate than intact virions, are usually found in the infected cells early after adsorption (21). Such particles could also be generated in vitro by heating the virions (22) or by incubating them with HeLa cell membranes or membrane extracts (9,14). Both the altered particles found in vivo and those generated in vitro are devoid of capsid protein VP4.…”

Section: Discussionmentioning

confidence: 99%

Lack of myristoylation of poliovirus capsid polypeptide VP0 prevents the formation of virions or results in the assembly of noninfectious virus particles

Marc

Masson

Girard

et al. 1990

J Virol

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We previously described the generation of a set of mutations into a cDNA of poliovirus type 1 in the myristoylation signal of the capsid polypeptide VP4 (D. Marc, G. Drugeon, A.-L. Haenni, M. Girard, and S. van der Werf, EMBO J. 8:2661, 1989). Genomic transcripts synthesized in vitro from the mutated cDNAs were found to be noninfectious upon transfection of permissive cells, and this property correlated with the lack of VPO myristoylation in vivo. In the study presented here, we analyzed the assembly intermediates that could be recovered from cells transfected with the mutated transcripts. We found that 14S pentamers could still assemble to a certain extent with an unmyristoylated VPO. Furthermore, viral particles sedimenting at 150S and containing capsid polypeptides VP1 to VP4 and virus-specific RNA were detected in the transfected cells. However, these mature virions were less abundant than those recovered after transfection with an infectious transcript, and they were devoid of infectivity. The results suggest that VPO myristoylation plays a role in the late steps of poliovirus assembly and that the myristate moiety of VP4 may be required in the early steps of poliovirus infection.

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Studies on the in vitro uncoating of poliovirus III. Roles of membrane-modifying and -stabilizing factors in the generation of subviral particles

Cited by 24 publications

References 23 publications

Interaction of Poliovirus with Its Purified Receptor and Conformational Alteration in the Virion

Interaction of Poliovirus with Its Purified Receptor and Conformational Alteration in the Virion

Picornaviral structure and assembly.

Lack of myristoylation of poliovirus capsid polypeptide VP0 prevents the formation of virions or results in the assembly of noninfectious virus particles

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