Molecular and Immunogenic Properties of Apyrase SP01B and D7-Related SP04 Recombinant Salivary Proteins of Phlebotomus perniciosus from Madrid, Spain
Figure 1
Multiple sequence alignment of apyrases from sand flies and other related sequences: L. longipalpis (Lon), Lutzomyia intermedia (Int), Lutzomyia ayacuchensis (Aya), Phlebotomus arabicus (Ara), Phlebotomus ariasi (Ari), P. perniciosus Italian strain (PerIta), P. perniciosus Spanish strain (PerSpa), Phlebotomus tobbi (Tob), Phlebotomus argentipes (Arg), P. duboscqi (Dub), P. papatasi (Pap), Phlebotomus sergenti (Ser), Homo sapiens (Hum), Drosophila melanogaster (Dro), and Cimex lectularius (Cim). Accession numbers are indicated in the sequence name. Sequences without a signal peptide were aligned with ClustalW and refined using Boxshade server, and the percentage of the identities or similarities that must agree for shading was set at 80%. Black background shading represents identical amino acids, and grey shading designates similar amino acids while white shading indicates no similarity. (*) and (Ø) indicate changes in the prediction of the antigenic index and secondary structure, respectively, between P. perniciosus Spanish and Italian strains as performed by Protean (DNASTAR, Lasergene). () signs above amino acids indicate changes in phosphorylation sites as predicted by NetPhos 2.0 Server, and the amino acid affected by the prediction on the phosphorylation site is encircled. Binding sites of nucleotides and Ca2+ are represented by and (+), respectively, as predicted for the human apyrase [52].
