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Major alteration in coxsackievirus B3 genomic RNA structure distinguishes a virulent strain from an avirulent strain.

Prusa J, Missak J, Kittrell J, Evans JJ, Tapprich WE - Nucleic Acids Res. (2014)

Bottom Line: Comparative sequence analysis of 170 closely related enteroviruses revealed that the SLII region lacks conservation.Neither the parent SLII nor the remaining domains of the background 5'UTR were structurally altered by the exchange, supporting an independent mechanism of folding and function.We show that the attenuated 5'UTR lacks structure in the SLII cardiovirulence determinant.

View Article: PubMed Central - PubMed

Affiliation: Biology Department, University of Nebraska at Omaha, Omaha, NE 68182, USA.

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Related in: MedlinePlus

Models for structurally distinct domain II folding in CV-B3/GA and CV-B3/28. (A) CV-B3/GA. (B) CV-B3/28. The enlarged nucleotide positions are substituted or inserted in CV-B3/GA.
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Figure 6: Models for structurally distinct domain II folding in CV-B3/GA and CV-B3/28. (A) CV-B3/GA. (B) CV-B3/28. The enlarged nucleotide positions are substituted or inserted in CV-B3/GA.

Mentions: Comparison of the full length naturally folded 5′UTRs of CV-B3/GA and CV-B3/28 revealed that a drastic structural alteration occurs in the SLII region. CV-B3/28 SLII includes pairing between positions 128–132 with 162–166 forming a lower stem that does not form in CV-B3/GA (Figure 6). These results may serve as a starting place to understanding the SLII structure required for enterovirus cardiovirulence.


Major alteration in coxsackievirus B3 genomic RNA structure distinguishes a virulent strain from an avirulent strain.

Prusa J, Missak J, Kittrell J, Evans JJ, Tapprich WE - Nucleic Acids Res. (2014)

Models for structurally distinct domain II folding in CV-B3/GA and CV-B3/28. (A) CV-B3/GA. (B) CV-B3/28. The enlarged nucleotide positions are substituted or inserted in CV-B3/GA.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4150801&req=5

Figure 6: Models for structurally distinct domain II folding in CV-B3/GA and CV-B3/28. (A) CV-B3/GA. (B) CV-B3/28. The enlarged nucleotide positions are substituted or inserted in CV-B3/GA.
Mentions: Comparison of the full length naturally folded 5′UTRs of CV-B3/GA and CV-B3/28 revealed that a drastic structural alteration occurs in the SLII region. CV-B3/28 SLII includes pairing between positions 128–132 with 162–166 forming a lower stem that does not form in CV-B3/GA (Figure 6). These results may serve as a starting place to understanding the SLII structure required for enterovirus cardiovirulence.

Bottom Line: Comparative sequence analysis of 170 closely related enteroviruses revealed that the SLII region lacks conservation.Neither the parent SLII nor the remaining domains of the background 5'UTR were structurally altered by the exchange, supporting an independent mechanism of folding and function.We show that the attenuated 5'UTR lacks structure in the SLII cardiovirulence determinant.

View Article: PubMed Central - PubMed

Affiliation: Biology Department, University of Nebraska at Omaha, Omaha, NE 68182, USA.

Show MeSH
Related in: MedlinePlus