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Proceedings of the National Academy of Sciences of the United States of America 106, 50 (2009) 21155-60
Acidianus filamentous virus 1 coat proteins display a helical fold spanning the filamentous archaeal viruses lineage.
Adeline Goulet, Stéphanie Blangy, Peter Redder, David Prangishvili 1, Catarina Felisberto-Rodrigues, Patrick Forterre 1, 2, Valérie Campanacci 3, Christian Cambillau 3
(15/12/2009)

Acidianus filamentous virus 1 (AFV1), a member of the Lipothrixviridae family, infects the hyperthermophilic, acidophilic crenarchaeaon Acidianus hospitalis. The virion, covered with a lipidic outer shell, is 9,100-A long and contains a 20.8-kb linear dsDNA genome. We have identified the two major coat proteins of the virion (MCPs; 132 and 140 amino acids). They bind DNA and form filaments when incubated with linear dsDNA. A C-terminal domain is identified in their crystal structure with a four-helix-bundle fold. In the topological model of the virion filament core, the genomic dsDNA superhelix wraps around the AFV1-132 basic protein, and the AFV1-140 basic N terminus binds genomic DNA, while its lipophilic C-terminal domain is imbedded in the lipidic outer shell. The four-helix bundle fold of the MCPs from AFV1 is identical to that of the coat protein (CP) of Sulfolobus islandicus rod-shaped virus (SIRV), a member of the Rudiviridae family. Despite low sequence identity between these proteins, their high degree of structural similarity suggests that they could have derived from a common ancestor and could thus define an yet undescribed viral lineage.
1 :  Biologie Moléculaire du Gène chez les Extrêmophiles (BMGE)
Institut Pasteur de Paris
2 :  Institut de génétique et microbiologie (IGM)
CNRS : UMR8621 – Université Paris XI - Paris Sud
3 :  Architecture et fonction des macromolécules biologiques (AFMB)
CNRS : UMR6098 – Université de la Méditerranée - Aix-Marseille II – Université de Provence - Aix-Marseille I
Sciences du Vivant/Biochimie, Biologie Moléculaire

Sciences du Vivant/Microbiologie et Parasitologie