Identification of Ixodid Tick-Specific Aquaporin-1 Potential Anti-tick Vaccine Epitopes: An in-silico Analysis
Ticks are arthropod vectors of pathogens of both Veterinary and Public health importance. Acaricide application, which is currently the mainstay of tick control, is hampered by high cost, the need for regular application and a selection of multi-acaricide resistant tick populations. In light of this...
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Frontiers Media S.A.
2019-09-01
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Series: | Frontiers in Bioengineering and Biotechnology |
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Online Access: | https://www.frontiersin.org/article/10.3389/fbioe.2019.00236/full |
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Article |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Christian Ndekezi Joseph Nkamwesiga Sylvester Ochwo Magambo Phillip Kimuda Magambo Phillip Kimuda Frank Norbert Mwiine Robert Tweyongyere Wilson Amanyire Dennis Muhanguzi Dennis Muhanguzi |
spellingShingle |
Christian Ndekezi Joseph Nkamwesiga Sylvester Ochwo Magambo Phillip Kimuda Magambo Phillip Kimuda Frank Norbert Mwiine Robert Tweyongyere Wilson Amanyire Dennis Muhanguzi Dennis Muhanguzi Identification of Ixodid Tick-Specific Aquaporin-1 Potential Anti-tick Vaccine Epitopes: An in-silico Analysis Frontiers in Bioengineering and Biotechnology antigenicity aquaporin-1 protein tick control peptide motifs cattle |
author_facet |
Christian Ndekezi Joseph Nkamwesiga Sylvester Ochwo Magambo Phillip Kimuda Magambo Phillip Kimuda Frank Norbert Mwiine Robert Tweyongyere Wilson Amanyire Dennis Muhanguzi Dennis Muhanguzi |
author_sort |
Christian Ndekezi |
title |
Identification of Ixodid Tick-Specific Aquaporin-1 Potential Anti-tick Vaccine Epitopes: An in-silico Analysis |
title_short |
Identification of Ixodid Tick-Specific Aquaporin-1 Potential Anti-tick Vaccine Epitopes: An in-silico Analysis |
title_full |
Identification of Ixodid Tick-Specific Aquaporin-1 Potential Anti-tick Vaccine Epitopes: An in-silico Analysis |
title_fullStr |
Identification of Ixodid Tick-Specific Aquaporin-1 Potential Anti-tick Vaccine Epitopes: An in-silico Analysis |
title_full_unstemmed |
Identification of Ixodid Tick-Specific Aquaporin-1 Potential Anti-tick Vaccine Epitopes: An in-silico Analysis |
title_sort |
identification of ixodid tick-specific aquaporin-1 potential anti-tick vaccine epitopes: an in-silico analysis |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Bioengineering and Biotechnology |
issn |
2296-4185 |
publishDate |
2019-09-01 |
description |
Ticks are arthropod vectors of pathogens of both Veterinary and Public health importance. Acaricide application, which is currently the mainstay of tick control, is hampered by high cost, the need for regular application and a selection of multi-acaricide resistant tick populations. In light of this, future tick control approaches are poised to rely on the integration of rational acaricide application and other methods, such as vaccination. To contribute to systematic research-guided efforts to produce anti-tick vaccines, we carried out an in-silico analysis of tick aquaporin-1 (AQP1) protein in order to identify tick-specific AQP1 peptide motifs that can be used in future peptide anti-tick vaccine development. We carried out multiple sequence alignment (MSA), motif analysis, homology modeling, and structural analysis to identify tick-specific AQP1 peptide motifs. BepiPred, Chou and Fasman-Turn, Karplus and Schulz Flexibility, and Parker-Hydrophilicity prediction models were used to predict these motifs' potential to induce B cell mediated immune responses. The tick AQP1 (GenBankID: QDO67142.1) protein was largely similar to the bovine AQP1 (PDB:1J4N) (23 % sequence similarity; Structural superimposition of the homology model and 14JN homotetramers gave an RMSD = 3.269 while superimposition of a single chain gave an RMSD = 1.475). Tick and bovine AQP1 transmembrane domains were largely similar while their extracellular and cytoplasmic domain loops showed variation. Two tick-specific AQP1 peptide motifs; M7 (residues 106–125, p = 5.4e-25), and M8 (residues 85–104, p = 3.3e-24) were identified. These two motifs are located on the extra-cellular AQP1 domain. Motifs; M7 and M8 showed the highest Parker-Hydrophilicity prediction immunogenicity scores of 1.784 and 1.536, respectively. These two motifs can be a good starting point for the development of potential tick AQP1 peptide-based anti-tick vaccines. Further analyses such as molecular dynamics, in vitro assays, and in vivo immunization assays are required to validate these findings. |
topic |
antigenicity aquaporin-1 protein tick control peptide motifs cattle |
url |
https://www.frontiersin.org/article/10.3389/fbioe.2019.00236/full |
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doaj-aa6277236b1749fb9769f1793d87fbda2020-11-25T01:51:12ZengFrontiers Media S.A.Frontiers in Bioengineering and Biotechnology2296-41852019-09-01710.3389/fbioe.2019.00236478297Identification of Ixodid Tick-Specific Aquaporin-1 Potential Anti-tick Vaccine Epitopes: An in-silico AnalysisChristian Ndekezi0Joseph Nkamwesiga1Sylvester Ochwo2Magambo Phillip Kimuda3Magambo Phillip Kimuda4Frank Norbert Mwiine5Robert Tweyongyere6Wilson Amanyire7Dennis Muhanguzi8Dennis Muhanguzi9School of Biosecurity, Biotechnical and Laboratory Science, College of Veterinary Medicine Animal Resources and Biosecurity, Makerere University, Kampala, UgandaSchool of Biosecurity, Biotechnical and Laboratory Science, College of Veterinary Medicine Animal Resources and Biosecurity, Makerere University, Kampala, UgandaSchool of Biosecurity, Biotechnical and Laboratory Science, College of Veterinary Medicine Animal Resources and Biosecurity, Makerere University, Kampala, UgandaSchool of Biosecurity, Biotechnical and Laboratory Science, College of Veterinary Medicine Animal Resources and Biosecurity, Makerere University, Kampala, UgandaResearch Unit in Bioinformatics, Department of Biochemistry and Microbiology, Rhodes University, Grahamstown, South AfricaSchool of Biosecurity, Biotechnical and Laboratory Science, College of Veterinary Medicine Animal Resources and Biosecurity, Makerere University, Kampala, UgandaSchool of Veterinary Medicine and Animal Resources, College of Veterinary Medicine Animal Resources and Biosecurity, Makerere University, Kampala, UgandaSchool of Biosecurity, Biotechnical and Laboratory Science, College of Veterinary Medicine Animal Resources and Biosecurity, Makerere University, Kampala, UgandaSchool of Biosecurity, Biotechnical and Laboratory Science, College of Veterinary Medicine Animal Resources and Biosecurity, Makerere University, Kampala, UgandaMakerere University/Uganda Virus Research Institute Centre of Excellence in Infection and Immunity Research and Training, Entebbe, UgandaTicks are arthropod vectors of pathogens of both Veterinary and Public health importance. Acaricide application, which is currently the mainstay of tick control, is hampered by high cost, the need for regular application and a selection of multi-acaricide resistant tick populations. In light of this, future tick control approaches are poised to rely on the integration of rational acaricide application and other methods, such as vaccination. To contribute to systematic research-guided efforts to produce anti-tick vaccines, we carried out an in-silico analysis of tick aquaporin-1 (AQP1) protein in order to identify tick-specific AQP1 peptide motifs that can be used in future peptide anti-tick vaccine development. We carried out multiple sequence alignment (MSA), motif analysis, homology modeling, and structural analysis to identify tick-specific AQP1 peptide motifs. BepiPred, Chou and Fasman-Turn, Karplus and Schulz Flexibility, and Parker-Hydrophilicity prediction models were used to predict these motifs' potential to induce B cell mediated immune responses. The tick AQP1 (GenBankID: QDO67142.1) protein was largely similar to the bovine AQP1 (PDB:1J4N) (23 % sequence similarity; Structural superimposition of the homology model and 14JN homotetramers gave an RMSD = 3.269 while superimposition of a single chain gave an RMSD = 1.475). Tick and bovine AQP1 transmembrane domains were largely similar while their extracellular and cytoplasmic domain loops showed variation. Two tick-specific AQP1 peptide motifs; M7 (residues 106–125, p = 5.4e-25), and M8 (residues 85–104, p = 3.3e-24) were identified. These two motifs are located on the extra-cellular AQP1 domain. Motifs; M7 and M8 showed the highest Parker-Hydrophilicity prediction immunogenicity scores of 1.784 and 1.536, respectively. These two motifs can be a good starting point for the development of potential tick AQP1 peptide-based anti-tick vaccines. Further analyses such as molecular dynamics, in vitro assays, and in vivo immunization assays are required to validate these findings.https://www.frontiersin.org/article/10.3389/fbioe.2019.00236/fullantigenicityaquaporin-1 proteintick controlpeptide motifscattle |