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© Tessa Quax, David Prangishvili, Gerard Pehau-Arnaudet, Jean-Marc Panaud
VAPs (virus-associated pyramids) formed by the Sulfolobus islandicus rod-shaped virus 2 (SIRV2) in cells of its hyperthermophilic archaeal host. Negative contrast electron micrography.
Publication : Biology direct

Evolution of an archaeal virus nucleocapsid protein from the CRISPR-associated Cas4 nuclease

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Biology direct - 29 Oct 2015

Krupovic M, Cvirkaite-Krupovic V, Prangishvili D, Koonin EV

Link to Pubmed [PMID] – 26514828

Biol. Direct 2015;10:65

Many proteins of viruses infecting hyperthermophilic Crenarchaeota have no detectable homologs in current databases, hampering our understanding of viral evolution. We used sensitive database search methods and structural modeling to show that a nucleocapsid protein (TP1) of Thermoproteus tenax virus 1 (TTV1) is a derivative of the Cas4 nuclease, a component of the CRISPR-Cas adaptive immunity system that is encoded also by several archaeal viruses. In TTV1, the Cas4 gene was split into two, with the N-terminal portion becoming TP1, and lost some of the catalytic amino acid residues, apparently resulting in the inactivation of the nuclease. To our knowledge, this is the first described case of exaptation of an enzyme for a virus capsid protein function.

http://www.ncbi.nlm.nih.gov/pubmed/26514828