Identification of Babesia bovis MSA-1 functionally constraint regions capable of binding to bovine erythrocytes

Merozoite surface antigen-1 is a glycoprotein expressed by Babesia bovis and is considered a vaccine candidate given that antibodies against it are able to partially block in vitro invasion of bovine erythrocytes. Despite this, no study to date has confirmed the target cell binding properties of the...

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Autores:
Cuy Chaparro, Laura
Ricaurte-Contreras, Laura Alejandra
Bohórquez, Michel David
Arevalo-Pinzon, Gabriela
Barreto-Santamaría, Adriana
Pabón, Laura
Reyes, César
Moreno Pérez, Darwin Andrés
Patarroyo, Manuel-Alfonso
Tipo de recurso:
Article of investigation
Fecha de publicación:
2022
Institución:
Universidad de Ciencias Aplicadas y Ambientales U.D.C.A
Repositorio:
Repositorio Institucional UDCA
Idioma:
eng
OAI Identifier:
oai:repository.udca.edu.co:11158/5016
Acceso en línea:
https://repository.udca.edu.co/handle/11158/5016
https://doi.org/10.1016/j.vetpar.2022.109834
https://repository.udca.edu.co/
Palabra clave:
Babesia bovis
Babesiosis
Parásitos
Péptidos
Proteínas Protozoarias
Adhesión de parásitos
Enfermedades del ganado
Rights
openAccess
License
https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode.es
Description
Summary:Merozoite surface antigen-1 is a glycoprotein expressed by Babesia bovis and is considered a vaccine candidate given that antibodies against it are able to partially block in vitro invasion of bovine erythrocytes. Despite this, no study to date has confirmed the target cell binding properties of the full MSA-1 or its fragments. This research has thus been focused on identifying protein regions playing a role in erythrocyte attachment, based on genetic diversity and natural selection analysis. Two regions under functional constraint (nucleotides 134–428 and 464–629) having a preponderance of negatively-selected signals were identified in silico. Three non-overlapping peptides derived from functionally constraint regions (42422 (39PEGSFYDDMSKFYGAVGSFD58), 42424 (91NALIKNNPMIRPDLFNATIV110) and 42426 (150TDIVEEDREKAVEYFKKHVY169)) were able to specifically bind to a sialoglycoprotein located on the bovine erythrocyte surface as confirmed by sensitive and specific peptide-cell interaction competition assays using both enzymatically treated and untreated red blood cells. Interestingly, it was predicted that peptides 42422 and 42426 have a helical structure and conserved motifs in all strain/isolates. These findings provide evidence, for the first time, related to B. bovis MSA-1 short regions used by the parasite in erythrocyte binding which could be predicted using natural selection analysis. Future work focused on evaluating these peptides’ antigenic ability during natural infection, and their ability to induce protection in immunisation assays are needed to confirm their usefulness as synthetic vaccine candidates.