Identification and comparative analysis of subolesin/akirin ortholog from Ornithodoros turicata ticks
Autor: | Daniel E. Sonenshine, Unnati Patel, Hameeda Sultana, Girish Neelakanta |
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Jazyk: | angličtina |
Předmět: |
Male
Veterinary medicine Sequence analysis Relapsing fever Sequence alignment Salivary Glands Evolution Molecular Phylogenetics Gene expression Animals Humans Ornithodoros turicata Amino Acid Sequence RNA Messenger Subolesin Ornithodoros Gene Phylogeny Genetics Phylogenetic analysis biology Base Sequence Research Midgut Sequence Analysis DNA biology.organism_classification Reverse transcription polymerase chain reaction Infectious Diseases Anti-vector vaccine Nucleotide and amino acid sequence alignment Female Parasitology Sequence Alignment Post-translational modifications |
Zdroj: | Parasites & Vectors |
ISSN: | 1756-3305 |
DOI: | 10.1186/s13071-015-0749-x |
Popis: | Background Subolesin is an evolutionary conserved molecule in diverse arthropod species that play an important role in the regulation of genes involved in immune responses, blood digestion, reproduction and development. In this study, we have identified a subolesin ortholog from soft ticks Ornithodoros turicata, the vector of the relapsing fever spirochete in the United States. Methods Uninfected fed or unfed O. turicata ticks were used throughout this study. The subolesin mRNA was amplified by reverse transcription polymerase chain reaction (RT-PCR) and sequenced. Quantitative-real time PCR (QRT-PCR) was performed to evaluate subolesin mRNA levels at different O. turicata developmental stages and from salivary glands and gut tissues. Bioinformatics and comparative analysis was performed to predict potential post-translational modifications in O. turicata subolesin amino-acid sequences. Results Our study reveals that O. turicata subolesin gene expression is developmentally regulated, where; adult ticks expressed significantly higher levels in comparison to the larvae or nymphal ticks. Expression of subolesin was evident in both unfed and fed ticks and in the salivary glands and midgut tissues. The expression of subolesin transcripts varied in fed ticks with peak levels at day 14 post-feeding. Phylogenetic analysis revealed that O. turicata subolesin showed a high degree of sequence conservation with subolesin’s from other soft and hard ticks. Bioinformatics and comparative analysis predicted that O. turicata subolesin carry three Protein kinase C and one Casein kinase II phosphorylation sites. However, no myristoylation or glycosylation sites were evident in the O. turicata subolesin sequence. Conclusion Our study provides important insights in recognizing subolesin as a conserved potential candidate for the development of a broad-spectrum anti-vector vaccine to control not only ticks but also several other arthropods that transmit diseases to humans and animals. Electronic supplementary material The online version of this article (doi:10.1186/s13071-015-0749-x) contains supplementary material, which is available to authorized users. |
Databáze: | OpenAIRE |
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