Fig. 3
From: Fourteen anti-tick vaccine targets are variably conserved in cattle fever ticks
Location of amino acid replacements (blue) mapped onto predicted 3D structural models of selected proteins: A voltage-dependent anion channel (RmVDAC); B vitellogenin receptor (VgR); C aquaporin-1 (RmAQP1); D serine protease inhibitor-1 (RmS-1); E subolesin (RmSub); F aquaporin-2 (RmAQP2); G chitinase (Chit); H glycoprotein Bm86 (Bm86). Published short-peptide vaccine targets (magenta) are highlighted for RmAQP2, Chit, RmSub, and Bm86; magenta is also used to highlight two lipid-binding domains (LBDs) that were assayed in VgR. Only those replacements identified in our Rhipicephalus (Boophilus) microplus dataset from the Americas and Pakistan are highlighted; additional replacements identified from previously published sequences of R. microplus and other Rhipicephalus species are documented in the amino acid alignments within Additional file 6. All 3D protein models were generated using the Alphafold website; specific URL addresses for each protein are provided