Babesia bovis ligand-receptor interaction: AMA-1 contains small regions governing bovine erythrocyte binding

Laura Cuy-Chaparro, Michel David Bohórquez, Gabriela Arévalo-Pinzón, Jeimmy Johana Castañeda-Ramírez, Carlos Fernando Suárez, Laura Pabón, Diego Ordóñez, Gina Marcela Gallego-López, Carlos Esteban Suárez, Darwin Andrés Moreno-Pérez, Manuel Alfonso Patarroyo

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

Resumen

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.

Idioma originalInglés estadounidense
Número de artículo714
Páginas (desde-hasta)1-15
Número de páginas15
PublicaciónInternational Journal of Molecular Sciences
Volumen22
N.º2
DOI
EstadoPublicada - ene 2 2021
Publicado de forma externa

All Science Journal Classification (ASJC) codes

  • Catálisis
  • Biología molecular
  • Espectroscopia
  • Informática aplicada
  • Química física y teórica
  • Química orgánica
  • Química inorgánica

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