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Viruses with different genome types adopt a similar strategy to pack nucleic acids based on positively charged protein domains

Capsid proteins often present a positively charged arginine-rich sequence at their terminal regions, which has a fundamental role in genome packaging and particle stability for some icosahedral viruses. These sequences show little to no conservation and are structurally dynamic such that they cannot...

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Bibliographic Details
Published in:Scientific reports 2020-03, Vol.10 (1), p.5470, Article 5470
Main Authors: Requião, Rodrigo D, Carneiro, Rodolfo L, Moreira, Mariana Hoyer, Ribeiro-Alves, Marcelo, Rossetto, Silvana, Palhano, Fernando L, Domitrovic, Tatiana
Format: Article
Language:English
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Summary:Capsid proteins often present a positively charged arginine-rich sequence at their terminal regions, which has a fundamental role in genome packaging and particle stability for some icosahedral viruses. These sequences show little to no conservation and are structurally dynamic such that they cannot be easily detected by common sequence or structure comparisons. As a result, the occurrence and distribution of positively charged domains across the viral universe are unknown. Based on the net charge calculation of discrete protein segments, we identified proteins containing amino acid stretches with a notably high net charge (Q > + 17), which are enriched in icosahedral viruses with a distinctive bias towards arginine over lysine. We used viral particle structural data to calculate the total electrostatic charge derived from the most positively charged protein segment of capsid proteins and correlated these values with genome charges arising from the phosphates of each nucleotide. We obtained a positive correlation (r = 0.91, p-value
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-020-62328-w