Babesia Bovis Ligand-Receptor Interaction: AMA-1 Contains Small Regions Governing Bovine Erythrocyte Binding
Apical membrane antigen 1 is a microneme protein which plays an indispensable role during Apicomplexa parasite invasion. The detailed mechanism of AMA-1 molecular interaction with its receptor on bovine erythrocytes has not been completely defined in Babesia bovis. This study was focused on identify...
- Autores:
-
Cuy-Chaparro, Laura
Bohórquez, Michel David
Arevalo-Pinzon, Gabriela
Castañeda-Ramírez, Jeimmy Johana
Suárez, Carlos F.
- Tipo de recurso:
- Article of investigation
- Fecha de publicación:
- 2021
- Institución:
- Universidad de Ciencias Aplicadas y Ambientales U.D.C.A
- Repositorio:
- Repositorio Institucional UDCA
- Idioma:
- eng
- OAI Identifier:
- oai:repository.udca.edu.co:11158/3801
- Acceso en línea:
- https://www.mdpi.com/1422-0067/22/2/714
- Palabra clave:
- Merozoítos
Plasmodium vivax
Vacunas contra la Malaria
Babesia bovis
- Rights
- openAccess
- License
- https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode.es
Summary: | Apical membrane antigen 1 is a microneme protein which plays an indispensable role during Apicomplexa parasite invasion. The detailed mechanism of AMA-1 molecular interaction with its receptor on bovine erythrocytes has not been completely defined in Babesia bovis. This study was focused on identifying the minimum B. bovis AMA-1-derived regions governing specific and high-affinity binding to its target cells. Different approaches were used for detecting ama-1 locus genetic variability and natural selection signatures. The binding properties of twelve highly conserved 20-residue-long peptides were evaluated using a sensitive and specific binding assay based on radio-iodination. B. bovis AMA-1 ectodomain structure was modelled and refined using molecular modelling software. NetMHCIIpan software was used for calculating B-and T-cell epitopes. The B. bovis ama-1 gene had regions under functional constraint, having the highest negative selective pressure intensity in the Domain I encoding region. Interestingly, B. bovis AMA-1-DI (100YMQKFDIPRNHGSGIYVDLG119 and120GYESVGSKSYRMPVGKCPVV139 ) and DII (302CPMHPVRDAIFGKWSGGSCV321 )-derived peptides had high specificity interaction with erythrocytes and bound to a chymotrypsin and neuraminidase-treatment sensitive receptor. DI-derived peptides appear to be exposed on the protein’s surface and contain predicted B-and T-cell epitopes. These findings provide data (for the first-time) concerning B. bovis AMA-1 functional subunits which are important for establishing receptor-ligand interactions which could be used in synthetic vaccine development. |
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