The complete nucleotide sequence of a variant of coxsackievirus A24, an agent causing acute hemorrhagic conjunctivitis

Supanaranond, Kasama; Takeda, Naokazu; Yamazaki, Shudo

doi:10.1007/bf01703064

Cited by 51 publications

(24 citation statements)

References 29 publications

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“…There is no experimental evidence that recombinants between PV and NPEV are viable. However, there are findings suggesting that such recombinants circulate in nature, as the remarkable similarity to PV of the 3Ј end of the CA21 or the CA24 reference strains shows (15,36). Thus, it is clear that OPV-derived PVs can acquire highly modified genomes not only by mutation but also by genetic exchanges with vaccine or wild PV, or even with NPEV.…”

Section: Discussionmentioning

confidence: 99%

Natural Genetic Exchanges between Vaccine and Wild Poliovirus Strains in Humans

Guillot

Caro

Cuervo

et al. 2000

J Virol

182

165

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In a previous study of poliovirus vaccine-derived strains isolated from patients with vaccine-associated paralytic poliomyelitis (VAPP) (9, 11), we reported that a high proportion (over 50%) of viruses had a recombinant genome. Most were intertypic vaccine/vaccine recombinants. However, some had restriction fragment length polymorphism (RFLP) profiles different from those of poliovirus vaccine strains. We demonstrate here that five such recombinants, of 88 VAPP strains examined, carried sequences of wild (nonvaccine) origin. To identify the parental wild donor of these sequences, we used RFLP profiles and nucleotide sequencing to look for similarity in the 3D polymerase-coding region of 61 wild, cocirculating poliovirus isolates (43 type 1, 16 type 2, and 2 type 3 isolates). In only one case was the donor identified, and it was a wild type 1 poliovirus. For the other four vaccine/wild recombinants, the wild parent could not be identified. The possibility that the wild sequences were of a non-poliovirus-enterovirus origin could not be excluded. Another vaccine/wild recombinant, isolated in Belarus from a VAPP case, indicated that the poliovirus vaccine/wild recombination is not an isolated phenomenon. We also found wild polioviruses (2 of 15) carrying vaccine-derived sequences in the 3 moiety of their genome. All these results suggest that genetic exchanges with wild poliovirus and perhaps with nonpoliovirus enteroviruses, are also a natural means of evolution for poliovirus vaccine strains.

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Section: Discussionmentioning

confidence: 99%

Natural Genetic Exchanges between Vaccine and Wild Poliovirus Strains in Humans

Guillot

Caro

Cuervo

et al. 2000

J Virol

182

165

View full text Add to dashboard Cite

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“…Biotinylated nested-PCR products were sequenced using a direct solid-phase T7-polymerase-mediated nucleotide sequencing strategy, using either a fluorescein-labelled sequencing primer for analysis with an ALF automated DNA sequencer (Pharmacia) as described previously by Nicholson et al (1995), or an unlabelled sequencing primer and Dyedeoxy terminators (Applied Biosystems) for analysis with a 373 automated DNA sequencer (Applied Biosystems). Sequences thus derived were compared with published enterovirus sequences (Chang et al, 1989;Drebot et al, 1994;Hughes et al, 1989;Dahllund e~ al., 1995;Iizuka et al, 1987;Jenkins et al, 1987;Klump et al, 1990;Kraus et al, 1995;Lindberg et al, 1987;Pulli et al, 1995;P6yry et al, 1994;Romero & Rotbart, 1995;Ryan et al, 1990;Supanaranond et al, 1992;Toyoda et al, 1984;Zhang et at., 1993;Zheng et al, 1995), using DNASIS to estabish the likely serotypic identity of viruses detected by PCR.…”

Section: Methodsmentioning

confidence: 99%

Enterovirus infection of the central nervous system of humans: lack of association with chronic neurological disease

Muir

Nicholson

Spencer

et al. 1996

Journal of General Virology

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“…replacing the conventional error function (Rumelhart et al, 1986) (Ryan et al, 1990) ok (Supanaranond et al, 1992) ok (Chang et al, 1989) ok (Iizuka et al, 1987 (Robertson et al, 1985) aThe cleavage type and corrected cleavage sequence and entry name are shown, as well as position of erroneous site (Old) and corrected (New). The status of the corresponding GenBank entry is also indicated if available (plus accession number).…”

Section: The Neural Network Algorithmmentioning

confidence: 99%

Cleavage site analysis in picornaviral polyproteins: Discovering cellular targets by neural networks

et al. 1996

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Picornaviral proteinases are responsible for maturation cleavages of the viral polyprotein, but also catalyze the degradation of cellular targets. Using graphical visualization techniques and neural network algorithms, we have investigated the sequence specificity of the two proteinases 2AP" and 3CPm. The cleavage of VPO (giving rise to VP2 and VP4). which is carried out by a so-far unknown proteinase, was also examined. In combination with a novel surface exposure prediction algorithm, our neural network approach successfully distinguishes known cleavage sites from noncleavage sites and yields a more consistent definition of features common to these sites. The method is able to predict experimentally determined cleavage sites in cellular proteins. We present a list of mammalian and other proteins that are predicted to be possible targets for the viral proteinases. Whether these proteins are indeed cleaved awaits experimental verification. Additionally, we report several errors detected in the protein databases.A computer server for prediction of cleavage sites by picornaviral proteinases is publicly available at the e-mail address NetPicoRNA@cbs.dtu.dk or via WWW at http://www.cbs.dtu.dkfservices/NetPicoRNA.Keywords: cleavage site prediction; neural networks; picornavirus; proteinase; surface exposureMembers of the picornavirus family express their genomic RNA as a single polyprotein that is proteolytically processed to the mature polypeptides. At least three proteinases are required for the individual protein components to be released (reviewed in Krausslich Hellen et al., 1989;Lawson & Semler, 1990). The primary cleavage, which severs the capsid precursor PI from the nonstructural region P2-P3, is performed cotranslationally by the viral proteinase 2APm in enteroviruses and human rhinoviruses (HRVs; see Fig. I). Most of the remaining cleavages are catalyzed by the viral proteinase, 3CP". In cardio-, hepato-, and aphthoviruses, which also belong to the picornavirus family, the L-proteinase performs functions similar to those of 2APm, resulting in a somewhat different cleavage scheme (see Fig. I). Concomitantly with RNA encapsidation, VPO is cleaved to VP4 and VP2; it is believed that the RNA itself exerts a catalytic function in this event (Arnold et a!., 1987;Harber et al., 1991;Bishop &Anderson, 1993;Basavappa et al., 1994).In addition to processing of the viral polyprotein, the proteinases also cleave cellular targets. When infected with poliovirus, at least nine acidic and five basic cellular proteins were shown to be degraded in two-dimensional gel electrophoresis (Urzanqui & Carrasco, 1989). The degradation of cellular proteins seems to be part of the viral attack mechanism, leading to host cell shur-ofJ-a decrease in cellular transcription and translation that has no influence on viral replication. The best-studied event is the cleavage of the eukaryotic initiation factor 4G (eIF-4G). which is required for cap-dependent translation of cellular mRNA. This protein is degraded by 2APm in entero-and...

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The complete nucleotide sequence of a variant of coxsackievirus A24, an agent causing acute hemorrhagic conjunctivitis

Cited by 51 publications

References 29 publications

Natural Genetic Exchanges between Vaccine and Wild Poliovirus Strains in Humans

Natural Genetic Exchanges between Vaccine and Wild Poliovirus Strains in Humans

Enterovirus infection of the central nervous system of humans: lack of association with chronic neurological disease

Cleavage site analysis in picornaviral polyproteins: Discovering cellular targets by neural networks

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