comprehensive phylogenetic, similarity and allergenicity analysis of boophilus genus tick tropomyosin protein

نویسندگان

mohammad mahdi ranjbar department of immunology, university of tehran, tehran

sedigheh nabian department of parasitology and tick and tick born diseases center, faculty of veterinary medicine university of tehran, tehran

seyed dawood mousavi nasab department of virology, faculty of medical sciences, tarbiat modares university, tehran

mohammad taheri rastegar central laboratory, faculty of veterinary medicine, university of tehran, tehran

چکیده

boophilus genus ticks are responsible for transferring some pathogens and reducing production factors in cattle. tropomysin (tpm) protein has actin regulator activity and playing important role in immune and allergic reactions. the main goal is to determine different aspects of phylogenetic, similarity, homology, structure and allergenicity of tpm protein. in prior study, we identified tpm by using mass-spectrometry in boophilus anulatus larva proteins extraction. analysis by ncbi and mascot software showed complete similarity of this protein with boophilus microplus . tpm blasting, invertebrates tpm sequences retrieval, aligning and analyzing of conserved and variable regions along sequences were next steps. also, construction the phylogenetic tree, overall mean distances estimation, homology protein secondary structure, allergencity analysis was achieved. the most similar sequences to boophilus genus tpm are haemaphysalis sp., scolopendra sp. and etc., respectively. the multiple sequence alignment showed that conserved and variable regions stretched in different part of tpm. the close relationships in phylogenetic tree between ticks and mites were seen, although the tpm sequences in ticks are more similar to each other than to mites and assume as the nearest relatives. insects tpm like worms, located in two separated clades, and trichinella spiralis in worm clades are more related taxa to members of ticks and mites groups. furthermore, overall mean distances over sequence pairs reflects tpm conservation during speciation. tpm has high homology in different species and has two domain of α-helix that cannot form disulfide bonds. finally, allergenicity analysis by separated and hybrid approach showed it undoubted is allergen and candidates some peptides as responsible for allergenicity of tpm. the comprehensive analysis of tpm has never been easy, especially when we attempt to make statements from different aspects about this protein.  our study revealed the some unique and valuable aspects of tpm protein of boophilus genus, and will help to further studies on mentioned protein.

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عنوان ژورنال:
journal of paramedical sciences

جلد ۴، شماره ۴، صفحات ۰-۰

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