| Autor: |
Kejzar, Nejc, Laanto, Elina, Rissanen, Ilona, Abrishami, Vahid, Selvaraj, Muniyandi, Moineau, Sylvain, Ravantti, Janne, Sundberg, Lotta-Riina, Huiskonen, Juha T. |
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| Zdroj: |
Nature Communications; 12/3/2022, Vol. 13 Issue 1, p1-13, 13p |
| Abstrakt: |
The origin of viruses remains an open question. While lack of detectable sequence similarity hampers the analysis of distantly related viruses, structural biology investigations of conserved capsid protein structures facilitate the study of distant evolutionary relationships. Here we characterize the lipid-containing ssDNA temperate bacteriophage ΦCjT23, which infects Flavobacterium sp. (Bacteroidetes). We report ΦCjT23-like sequences in the genome of strains belonging to several Flavobacterium species. The virion structure determined by cryogenic electron microscopy reveals similarities to members of the viral kingdom Bamfordvirae that currently consists solely of dsDNA viruses with a major capsid protein composed of two upright β-sandwiches. The minimalistic structure of ΦCjT23 suggests that this phage serves as a model for the last common ancestor between ssDNA and dsDNA viruses in the Bamfordvirae. Both ΦCjT23 and the related phage FLiP infect Flavobacterium species found in several environments, suggesting that these types of viruses have a global distribution and a shared evolutionary origin. Detailed comparisons to related, more complex viruses not only expand our knowledge about this group of viruses but also provide a rare glimpse into early virus evolution. Structural biology investigation of conserved capsid proteins facilitates the study of virus evolution. Here, characterization of the lipid-containing ssDNA bacteriophage ΦCjT23 suggests that this phage may serve as a model for the last common ancestor between ssDNA and dsDNA viruses in the Bamfordvirae. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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