First Data on <i>Ornithodoros moubata</i> Aquaporins: Structural, Phylogenetic and Immunogenic Characterisation as Vaccine Targets
<i>Ornithodoros moubata</i> transmits African swine fever and human relapsing fever in Africa. The elimination of <i>O. moubata</i> populations from anthropic environments is expected to improve the prevention and control of these diseases. Tick vaccines have emerged as a sus...
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MDPI AG
2022-06-01
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author | Ricardo Pérez-Sánchez Ana Laura Cano-Argüelles María González-Sánchez Ana Oleaga |
author_facet | Ricardo Pérez-Sánchez Ana Laura Cano-Argüelles María González-Sánchez Ana Oleaga |
author_sort | Ricardo Pérez-Sánchez |
collection | DOAJ |
description | <i>Ornithodoros moubata</i> transmits African swine fever and human relapsing fever in Africa. The elimination of <i>O. moubata</i> populations from anthropic environments is expected to improve the prevention and control of these diseases. Tick vaccines have emerged as a sustainable method for tick control, and tick aquaporins (AQPs) are promising targets for tick vaccines due to their vital functions, immunogenicity and ease of access by neutralising host antibodies. This study aimed at the systematic identification of the AQPs expressed by <i>O. moubata</i> (OmAQPs) and their characterisation as vaccine targets. Therefore, AQP coding sequences were recovered from available transcriptomic datasets, followed by PCR amplification, cloning, sequence verification and the analysis of the AQP protein structure and epitope exposure. Seven OmAQPs were identified and characterised: six were aquaglyceroporins, and one was a water-specific aquaporin. All of these were expressed in the salivary glands and midgut and only three in the coxal glands. Epitope exposure analysis identified three extracellular domains in each AQP, which concentrate overlapping B and T cell epitopes, making them interesting vaccine targets. Based on these domain sequences, a set of ten antigenic peptides was designed, which showed adequate properties to be produced and tested in pilot vaccine trials. |
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issn | 2076-0817 |
language | English |
last_indexed | 2024-03-09T22:48:15Z |
publishDate | 2022-06-01 |
publisher | MDPI AG |
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series | Pathogens |
spelling | doaj.art-3a62021f06824f8d9c5dde7dd8fdccb22023-11-23T18:25:25ZengMDPI AGPathogens2076-08172022-06-0111669410.3390/pathogens11060694First Data on <i>Ornithodoros moubata</i> Aquaporins: Structural, Phylogenetic and Immunogenic Characterisation as Vaccine TargetsRicardo Pérez-Sánchez0Ana Laura Cano-Argüelles1María González-Sánchez2Ana Oleaga3Parasitology Laboratory, Institute of Natural Resources and Agrobiology (IRNASA, CSIC), Cordel de Merinas, 40-52, 37008 Salamanca, SpainParasitology Laboratory, Institute of Natural Resources and Agrobiology (IRNASA, CSIC), Cordel de Merinas, 40-52, 37008 Salamanca, SpainParasitology Laboratory, Institute of Natural Resources and Agrobiology (IRNASA, CSIC), Cordel de Merinas, 40-52, 37008 Salamanca, SpainParasitology Laboratory, Institute of Natural Resources and Agrobiology (IRNASA, CSIC), Cordel de Merinas, 40-52, 37008 Salamanca, Spain<i>Ornithodoros moubata</i> transmits African swine fever and human relapsing fever in Africa. The elimination of <i>O. moubata</i> populations from anthropic environments is expected to improve the prevention and control of these diseases. Tick vaccines have emerged as a sustainable method for tick control, and tick aquaporins (AQPs) are promising targets for tick vaccines due to their vital functions, immunogenicity and ease of access by neutralising host antibodies. This study aimed at the systematic identification of the AQPs expressed by <i>O. moubata</i> (OmAQPs) and their characterisation as vaccine targets. Therefore, AQP coding sequences were recovered from available transcriptomic datasets, followed by PCR amplification, cloning, sequence verification and the analysis of the AQP protein structure and epitope exposure. Seven OmAQPs were identified and characterised: six were aquaglyceroporins, and one was a water-specific aquaporin. All of these were expressed in the salivary glands and midgut and only three in the coxal glands. Epitope exposure analysis identified three extracellular domains in each AQP, which concentrate overlapping B and T cell epitopes, making them interesting vaccine targets. Based on these domain sequences, a set of ten antigenic peptides was designed, which showed adequate properties to be produced and tested in pilot vaccine trials.https://www.mdpi.com/2076-0817/11/6/694soft ticks<i>Ornithodoros moubata</i>aquaporinstick vaccinesantigenic peptides |
spellingShingle | Ricardo Pérez-Sánchez Ana Laura Cano-Argüelles María González-Sánchez Ana Oleaga First Data on <i>Ornithodoros moubata</i> Aquaporins: Structural, Phylogenetic and Immunogenic Characterisation as Vaccine Targets Pathogens soft ticks <i>Ornithodoros moubata</i> aquaporins tick vaccines antigenic peptides |
title | First Data on <i>Ornithodoros moubata</i> Aquaporins: Structural, Phylogenetic and Immunogenic Characterisation as Vaccine Targets |
title_full | First Data on <i>Ornithodoros moubata</i> Aquaporins: Structural, Phylogenetic and Immunogenic Characterisation as Vaccine Targets |
title_fullStr | First Data on <i>Ornithodoros moubata</i> Aquaporins: Structural, Phylogenetic and Immunogenic Characterisation as Vaccine Targets |
title_full_unstemmed | First Data on <i>Ornithodoros moubata</i> Aquaporins: Structural, Phylogenetic and Immunogenic Characterisation as Vaccine Targets |
title_short | First Data on <i>Ornithodoros moubata</i> Aquaporins: Structural, Phylogenetic and Immunogenic Characterisation as Vaccine Targets |
title_sort | first data on i ornithodoros moubata i aquaporins structural phylogenetic and immunogenic characterisation as vaccine targets |
topic | soft ticks <i>Ornithodoros moubata</i> aquaporins tick vaccines antigenic peptides |
url | https://www.mdpi.com/2076-0817/11/6/694 |
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