An alternative vaccine target for bovine Anaplasmosis based on enolase, a moonlighting protein
The discovery of new targets for preventing bovine anaplasmosis has moved away from focusing on proteins that have already been extensively studied in Anaplasma marginale, including the Major Surface Proteins, Outer Membrane Proteins, and Type IV Secretion System proteins. An alternative is moonligh...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2023-09-01
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| Series: | Frontiers in Veterinary Science |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/articles/10.3389/fvets.2023.1225873/full |
| _version_ | 1797676871177994240 |
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| author | Rosa Estela Quiroz-Castañeda Hugo Aguilar-Díaz Itzel Amaro-Estrada |
| author_facet | Rosa Estela Quiroz-Castañeda Hugo Aguilar-Díaz Itzel Amaro-Estrada |
| author_sort | Rosa Estela Quiroz-Castañeda |
| collection | DOAJ |
| description | The discovery of new targets for preventing bovine anaplasmosis has moved away from focusing on proteins that have already been extensively studied in Anaplasma marginale, including the Major Surface Proteins, Outer Membrane Proteins, and Type IV Secretion System proteins. An alternative is moonlighting or multifunctional proteins, capable of performing various biological functions within various cellular compartments. There are several reports on the role of moonlighting proteins as virulence factors in various microorganisms. Moreover, it is known that about 25% of all moonlighting is involved in the virulence of pathogens. In this work, for the first time, we present the identification of three enolase proteins (AmEno01, AmEno15, and AmEno31) in the genome of Mexican strains of A. marginale. Using bioinformatics tools, we predicted the catalytic domains, enolase signature, and amino acids binding magnesium ion of the catalytic domain and performed a phylogenetic reconstruction. In addition, by molecular docking analysis, we found that AmEno01 would bind to erythrocyte proteins spectrin, ankyrin, and stomatin. This adhesion function has been reported for enolases from other pathogens. It is considered a promising target since blocking this function would impede the fundamental adhesion process that facilitates the infection of erythrocytes. Additionally, molecular docking predicts that AmEno01 could bind to extracellular matrix protein fibronectin, which would be significant if we consider that some proteins with fibronectin domains are localized in tick gut cells and used as an adhesion strategy to gather bacteria before traveling to salivary glands. Derived from the molecular docking analysis of AmEno01, we hypothesized that enolases could be proteins driven by the pathogen and redirected at the expense of the pathogen’s needs. |
| first_indexed | 2024-03-11T22:36:42Z |
| format | Article |
| id | doaj.art-35c78706aad843fcafda8ae3487b3c64 |
| institution | Directory Open Access Journal |
| issn | 2297-1769 |
| language | English |
| last_indexed | 2024-03-11T22:36:42Z |
| publishDate | 2023-09-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Veterinary Science |
| spelling | doaj.art-35c78706aad843fcafda8ae3487b3c642023-09-22T13:01:41ZengFrontiers Media S.A.Frontiers in Veterinary Science2297-17692023-09-011010.3389/fvets.2023.12258731225873An alternative vaccine target for bovine Anaplasmosis based on enolase, a moonlighting proteinRosa Estela Quiroz-CastañedaHugo Aguilar-DíazItzel Amaro-EstradaThe discovery of new targets for preventing bovine anaplasmosis has moved away from focusing on proteins that have already been extensively studied in Anaplasma marginale, including the Major Surface Proteins, Outer Membrane Proteins, and Type IV Secretion System proteins. An alternative is moonlighting or multifunctional proteins, capable of performing various biological functions within various cellular compartments. There are several reports on the role of moonlighting proteins as virulence factors in various microorganisms. Moreover, it is known that about 25% of all moonlighting is involved in the virulence of pathogens. In this work, for the first time, we present the identification of three enolase proteins (AmEno01, AmEno15, and AmEno31) in the genome of Mexican strains of A. marginale. Using bioinformatics tools, we predicted the catalytic domains, enolase signature, and amino acids binding magnesium ion of the catalytic domain and performed a phylogenetic reconstruction. In addition, by molecular docking analysis, we found that AmEno01 would bind to erythrocyte proteins spectrin, ankyrin, and stomatin. This adhesion function has been reported for enolases from other pathogens. It is considered a promising target since blocking this function would impede the fundamental adhesion process that facilitates the infection of erythrocytes. Additionally, molecular docking predicts that AmEno01 could bind to extracellular matrix protein fibronectin, which would be significant if we consider that some proteins with fibronectin domains are localized in tick gut cells and used as an adhesion strategy to gather bacteria before traveling to salivary glands. Derived from the molecular docking analysis of AmEno01, we hypothesized that enolases could be proteins driven by the pathogen and redirected at the expense of the pathogen’s needs.https://www.frontiersin.org/articles/10.3389/fvets.2023.1225873/fullmultifunctional proteinsenolaseerythrocytesticksextracellular matrixveterinary diseases |
| spellingShingle | Rosa Estela Quiroz-Castañeda Hugo Aguilar-Díaz Itzel Amaro-Estrada An alternative vaccine target for bovine Anaplasmosis based on enolase, a moonlighting protein Frontiers in Veterinary Science multifunctional proteins enolase erythrocytes ticks extracellular matrix veterinary diseases |
| title | An alternative vaccine target for bovine Anaplasmosis based on enolase, a moonlighting protein |
| title_full | An alternative vaccine target for bovine Anaplasmosis based on enolase, a moonlighting protein |
| title_fullStr | An alternative vaccine target for bovine Anaplasmosis based on enolase, a moonlighting protein |
| title_full_unstemmed | An alternative vaccine target for bovine Anaplasmosis based on enolase, a moonlighting protein |
| title_short | An alternative vaccine target for bovine Anaplasmosis based on enolase, a moonlighting protein |
| title_sort | alternative vaccine target for bovine anaplasmosis based on enolase a moonlighting protein |
| topic | multifunctional proteins enolase erythrocytes ticks extracellular matrix veterinary diseases |
| url | https://www.frontiersin.org/articles/10.3389/fvets.2023.1225873/full |
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