In silico characterization and structural modeling of Dermacentor andersoni p36 immunosuppressive protein
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 i...
| Autores principales: | , , , , , |
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| Formato: | Journal Article |
| Lenguaje: | Inglés |
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Hindawi Limited
2018
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| Materias: | |
| Acceso en línea: | https://hdl.handle.net/10568/98957 |
| _version_ | 1855515289579421696 |
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| author | Oyugi, M.O. Kinyua, J.K. Magiri, E.N. Kigoni, M.W. Costa, E.P. Githaka, Naftaly W. |
| author_browse | Costa, E.P. Githaka, Naftaly W. Kigoni, M.W. Kinyua, J.K. Magiri, E.N. Oyugi, M.O. |
| author_facet | Oyugi, M.O. Kinyua, J.K. Magiri, E.N. Kigoni, M.W. Costa, E.P. Githaka, Naftaly W. |
| author_sort | Oyugi, M.O. |
| collection | Repository of Agricultural Research Outputs (CGSpace) |
| description | 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. |
| format | Journal Article |
| id | CGSpace98957 |
| institution | CGIAR Consortium |
| language | Inglés |
| publishDate | 2018 |
| publishDateRange | 2018 |
| publishDateSort | 2018 |
| publisher | Hindawi Limited |
| publisherStr | Hindawi Limited |
| record_format | dspace |
| spelling | CGSpace989572023-10-02T12:08:00Z In silico characterization and structural modeling of Dermacentor andersoni p36 immunosuppressive protein Oyugi, M.O. Kinyua, J.K. Magiri, E.N. Kigoni, M.W. Costa, E.P. Githaka, Naftaly W. vaccines livestock dermacentor andersoni proteins biomedical engineering 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. 2018-04-08 2019-01-08T09:09:37Z 2019-01-08T09:09:37Z Journal Article https://hdl.handle.net/10568/98957 en Open Access Hindawi Limited Oyugi, M.O., Kinyua, J.K., Magiri, E.N., Kigoni, M.W., Costa, E.P. and Githaka, N.W. 2018. In silico characterization and structural modeling of Dermacentor andersoni p36 immunosuppressive protein. Advances in Bioinformatics 2018: 7963401. |
| spellingShingle | vaccines livestock dermacentor andersoni proteins biomedical engineering Oyugi, M.O. Kinyua, J.K. Magiri, E.N. Kigoni, M.W. Costa, E.P. Githaka, Naftaly W. In silico characterization and structural modeling of Dermacentor andersoni p36 immunosuppressive protein |
| title | In silico characterization and structural modeling of Dermacentor andersoni p36 immunosuppressive protein |
| title_full | In silico characterization and structural modeling of Dermacentor andersoni p36 immunosuppressive protein |
| title_fullStr | In silico characterization and structural modeling of Dermacentor andersoni p36 immunosuppressive protein |
| title_full_unstemmed | In silico characterization and structural modeling of Dermacentor andersoni p36 immunosuppressive protein |
| title_short | In silico characterization and structural modeling of Dermacentor andersoni p36 immunosuppressive protein |
| title_sort | in silico characterization and structural modeling of dermacentor andersoni p36 immunosuppressive protein |
| topic | vaccines livestock dermacentor andersoni proteins biomedical engineering |
| url | https://hdl.handle.net/10568/98957 |
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