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Advances in Bioinformatics
Volume 2018, Article ID 7963401, 12 pages
https://doi.org/10.1155/2018/7963401
Research Article

In Silico Characterization and Structural Modeling of Dermacentor andersoni p36 Immunosuppressive Protein

1Department of Biochemistry, Jomo Kenyatta University of Agriculture and Technology, P.O. Box 62000, Nairobi 00200, Kenya
2Cooperative University of Kenya, P.O. Box 24814, Nairobi 00502, Kenya
3Department of Biochemistry, Kenyatta University, P.O. Box 43844, Nairobi 00100, Kenya
4Unit of Animal Experimentation, State University of North Fluminense, Centre of Biosciences and Biotechnology, Campos dos Goytacazes, RJ, Brazil
5Animal and Human Health Program, International Livestock Research Institute, P.O. Box 30709, Nairobi 00100, Kenya

Correspondence should be addressed to Martin Omulindi Oyugi; moc.liamg@nitramidnilumo

Received 5 November 2017; Accepted 14 February 2018; Published 8 April 2018

Academic Editor: David A. McClellan

Copyright © 2018 Martin Omulindi Oyugi et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Ticks cause approximately $17–19 billion economic losses to the livestock industry globally. Development of recombinant antitick vaccine is greatly hindered by insufficient knowledge and understanding of proteins expressed by ticks. Ticks secrete immunosuppressant proteins that modulate the host’s immune system during blood feeding; these molecules could be a target for antivector vaccine development. Recombinant p36, a 36 kDa immunosuppressor from the saliva of female Dermacentor andersoni, suppresses T-lymphocytes proliferation in vitro. To identify potential unique structural and dynamic properties responsible for the immunosuppressive function of p36 proteins, this study utilized bioinformatic tool to characterize and model structure of D. andersoni p36 protein. Evaluation of p36 protein family as suitable vaccine antigens predicted a p36 homolog in Rhipicephalus appendiculatus, the tick vector of East Coast fever, with an antigenicity score of 0.7701 that compares well with that of Bm86 (0.7681), the protein antigen that constitute commercial tick vaccine Tickgard™. Ab initio modeling of the D. andersoni p36 protein yielded a 3D structure that predicted conserved antigenic region, which has potential of binding immunomodulating ligands including glycerol and lactose, found located within exposed loop, suggesting a likely role in immunosuppressive function of tick p36 proteins. Laboratory confirmation of these preliminary results is necessary in future studies.