Structure and Replication of α-Viruses

Kääriäinen, Leevi; Söderlund, Hans

doi:10.1007/978-3-642-46388-4_2

Cited by 105 publications

(52 citation statements)

References 369 publications

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“…This view is supported by ultraviolet inactivation data, which show different target sizes for 26-S and 42-S RNA templates [19]. Previous results cannot, however, discriminate between the 'polymerase jump' and the 'internal initiation' models [3].…”

mentioning

confidence: 84%

“…One is the 42-S RNA ( M , 4.3 x lo6) which also is the viral genome. The genome codes for the non-structural proteins, i. e. the viral enzymes [2,3]. The other, 26-S RNA ( M , 1.6 x lo6) is a subgenomic messenger species which is identical to the 3' third of the genome [4-61. This RNA codes for the structural proteins of the virus [2,3].…”

mentioning

confidence: 99%

“…The genome codes for the non-structural proteins, i. e. the viral enzymes [2,3]. The other, 26-S RNA ( M , 1.6 x lo6) is a subgenomic messenger species which is identical to the 3' third of the genome [4-61. This RNA codes for the structural proteins of the virus [2,3]. Both RNAs are polyadenylated at their 3' ends [7-91 while the 5' end is capped with m7G(5')ppp(5')Ap as shown for Sindbis virus [lo, 111.…”

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confidence: 99%

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The Nucleotide Sequences of the 5′‐Terminal T1 Oligonucleotides of Semliki‐Forest‐Virus 42‐S and 26‐S RNAs are Different

Pettersson¹,

Söderlund²,

Kääriäinen³

1980

European Journal of Biochemistry

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To study the mechanism of the synthesis of Semliki Forest virus (SFV) 26-S RNA, we have isolated the 5'-terminal 'cap'-containing RNase-T1-resistant oligonucleotide (T1 cap) from the genomic 42-S RNA and from the subgenomic 26-S RNA and determined their nucleotide sequences. The T1 caps were purified from 32P-labelled RNAs on two successive two-dimensional fractionation systems : (a) electrophoresis on cellulose acetate paper followed by homochromatography and (b) two-dimensional polyacrylamide gel electrophoresis. The T1 caps derived from the two RNAs had different mobilities in both systems. Their nucleotide sequence was found to be : m7G(5')ppp-(5')ApUpGp-for the 42-S RNA and m7G(5')ppp(5')ApUpUpGp-for the 26-S RNA, respectively. Thus, it appears that the 26-S RNA is not formed by initiation of the RNA polymerase at the 3' end of the negative-strand template followed by 'cleavage and splicing' or as the result of a 'polymerase jump'. Our results, instead, favour the model of internal initiation of the polymerase on the 42-S negative-strand RNA template.

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confidence: 84%

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confidence: 99%

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confidence: 99%

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The Nucleotide Sequences of the 5′‐Terminal T1 Oligonucleotides of Semliki‐Forest‐Virus 42‐S and 26‐S RNAs are Different

Pettersson¹,

Söderlund²,

Kääriäinen³

1980

European Journal of Biochemistry

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“…The 5' end has a cap-structure m 7GpppAUG and the 3' end a poly(A) tract (1)(2)(3). Another positive-strand RNA is synthesized in SFV infected cells: the 26S RNA, which codes for the virion structural proteins is identical to the 3' third of 42S RNA and has a cap m7GpppAUUG (3)(4)(5)(6).…”

Section: Introductionmentioning

confidence: 99%

“…Both 42S and 26S positive strands are synthesized from 42S RNA negative strands (for review see 5,6).…”

Section: Introductionmentioning

confidence: 99%

Structural complexity of defective-interfering RNAs of Semliki Forest virus as revealed by analysis of complementary DNA

et al. 1981

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The 18S defective interfering RNA of Semliki Forest virus has been reverse transcribed to cDNA, which was shown to be heterogeneousby restriction enzyme analysis. After transformation to E.coli, using pBR322 as a vector, two clones, pKTH301 and pKTH309 with inserts of 1. 7 kb and 2 kb, were charac ter.-ized, respectively. The restriction maps of the two clones were different but suggested that both contained repeating units. At the 3' terminus, pKTH301 had preserved 106 nucleotides and pKTH309 102 nucleotides from the 3' end of the viral 42S genome. The conserved 3' terminal sequence was joined to a different sequence in the two clones, and these sequences were not derived from the region coding for the viral structural proteins. The DI RNAs represented by the two clones are generated from the viral 42S RNA by several noncontinuous internal deletions, since the largest colinear regions with 42S RNA are 320 nucleotides in pIKrH301, and 430 and 340 nucleotides in pKTH309. All these fragments had unique RNase Ti oligonucleotide fingerprints, suggesting that they were derived from different regions of 42S RNA.

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A model of the binding, entry, uncoating, and RNA synthesis of Semliki Forest virus in baby hamster kidney (BHK‐21) cells

Dee

Hammer

Shuler

1995

Biotech & Bioengineering

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A quantitative understanding of viral trafficking would be useful in treating viral-mediated diseases, designing protocols for viral gene therapy, and optimizing heterologous protein production. In this article, a model for the trafficking of Semliki Forest virus and its RNA synthesis in baby hamster kidney (BHK-21) cells is presented. This model includes the various steps leading to infection such as attachment, endocytosis, and viral fusion in the endosome. The model estimates a mean fusion time of 4 to 6 min for the wild-type virus, and 38 min for Fus-1, an SFV mutant which requires a lower pH for fusion. These mean fusion times are consistent with the time-scale of endosomal acidification, suggesting viruses fuse almost instantaneously with the endosomal membrane as soon as the pH of the endosome drops below the pH threshold of the virus. Infection is most likely controlled at the level of viral uncoating, as shown by the close agreement between the efficiency of uncoating and the experimentally determined fraction of viruses that is infectious. The viral RNA synthesized per cell is best described by assuming that it depends on the number of uncoated viruses prior to the onset of replication according to a saturation-type expression. A Poisson distribution is used to determine the distribution of uncoated viruses among the cells. Because attachment is the rate-limiting step in the uncoating of the virus, increasing the attachment rate can lead to enhanced RNA synthesis and, hence, new virion production. Such an increase in the attachment rate may be obtained by lowering the medium pH or the addition of a polycation. (c) 1995 John Wiley & Sons, Inc.

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Structure and Replication of α-Viruses

Cited by 105 publications

References 369 publications

The Nucleotide Sequences of the 5′‐Terminal T1 Oligonucleotides of Semliki‐Forest‐Virus 42‐S and 26‐S RNAs are Different

The Nucleotide Sequences of the 5′‐Terminal T1 Oligonucleotides of Semliki‐Forest‐Virus 42‐S and 26‐S RNAs are Different

Structural complexity of defective-interfering RNAs of Semliki Forest virus as revealed by analysis of complementary DNA

A model of the binding, entry, uncoating, and RNA synthesis of Semliki Forest virus in baby hamster kidney (BHK‐21) cells

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