Journal: Parasites & Vectors

Article Title: Rhipicephalus ( Boophilus ) microplus aquaporin as an effective vaccine antigen to protect against cattle tick infestations

doi: 10.1186/s13071-014-0475-9

Figure Lengend Snippet: Amino acid sequence alignments of RmAQP1-3 with putative aquaporins from other tick species. Alignment was by the ClustalW multiple alignment function of MacVector 12.7.5 using the Gonnet matrix with open gap penalty of 10 and extend gap penalty of 0.05. Determination of amino acid similarity was by chemical properties of amino acid side chains with DE, AGILV, NQ, FWY, RHK, ST, CM, and P comprising the groups considered as conservative substitutions. The accession numbers for the putative tick aquaporins from R. appendiculatus , R. sanguineus , I. scapularis , I. ricinus , and D. variabilis are CD780384, CAR66115, XP_002399794, CAX48964, and ABI53034, respectively. One member each from the human aquaporin families 3 (NP 004916) and 7 (NP 001161) are also included in the alignment. The RmAQP1 was used as the model for comparing other sequences, with identities indicated by colon (:) and similarities by period (.). In the summary line below the 10 aligned sequences, a colon (:) notes amino acid positions where all 10 sequences contain the identical amino acid, a period (.) indicates all 10 sequences contain identical or similar amino acids, and an asterisk (*) indicates 9 of the 10 aligned sequences have identical or similar amino acids. Gaps inserted to optimize alignments are indicated by a dash (−). The shaded portions of the RmAQP1 sequence indicate the six predicted transmembrane helical regions.

Article Snippet: Alignment was by the ClustalW multiple alignment function of MacVector 12.7.5 using the Gonnet matrix with open gap penalty of 10 and extend gap penalty of 0.05.

Techniques: Sequencing