Journal: PLOS Biology
Article Title: Resurrection of 2′-5′-oligoadenylate synthetase 1 (OAS1) from the ancestor of modern horseshoe bats blocks SARS-CoV-2 replication
doi: 10.1371/journal.pbio.3002398
Figure Lengend Snippet: (A) Protein alignment of the RhinoCA (ASR), R . ferrumequinum (R. ferr), and P . alecto (P. alec) OAS1 sequences. RhinoCA sites are coloured by each predicted state’s posterior probability. The bars on the bottom row indicate the Shannon’s entropy of each site in the alignment of all 18 Chiroptera OAS1 proteins. Secondary structure alpha helices (zigzag) and beta sheets (arrows) involved in the protein/RNA interface and the active site triad residues D74/D75/D147 are annotated underneath the entropy row (as described for the human OAS1 protein in Donovan and colleagues ). The CAAX box signal at the C-terminal end of the sequence is highlighted in yellow. (B) Maximum likelihood phylogeny of the Chiroptera OAS1 proteins informed by their species tree topology. The ancestrally reconstructed (RhinoCA) node, the branch where the prenylation signal was deleted and the clades of each superfamily are annotated on the tree. The variable indel region sequence of OAS1 is shown on the right of each tip. Residues are coloured according to potential homology between the proteins. ASR, ancestral sequence reconstruction; OAS1, 2′-5′-oligoadenylate synthetase 1.
Article Snippet: The entropy value for each site in the Chiroptera OAS1 protein alignment shown in was calculated using Shannon’s entropy formula with a natural log as implemented in Bioedit [ ] (H(l) = -Sf(a,l)ln(f(a,l)); f(a,l) being the frequency of amino acid a at position l).
Techniques: Sequencing
