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


Journal

Veterinary parasitology
ISSN: 1873-2550
Titre abrégé: Vet Parasitol
Pays: Netherlands
ID NLM: 7602745

Informations de publication

Date de publication:
Dec 2022
Historique:
received: 19 05 2022
revised: 23 09 2022
accepted: 19 10 2022
pubmed: 8 11 2022
medline: 6 12 2022
entrez: 7 11 2022
Statut: ppublish

Résumé

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 (

Identifiants

pubmed: 36343530
pii: S0304-4017(22)00188-1
doi: 10.1016/j.vetpar.2022.109834
pii:
doi:

Substances chimiques

Merozoite Surface Protein 1 0
Antigens, Protozoan 0
Protozoan Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

109834

Informations de copyright

Copyright © 2022 Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Laura Cuy-Chaparro (L)

Molecular Biology and Immunology Department, Fundación Instituto de Inmunología de Colombia [FIDIC], Carrera 50#26-20, Bogotá DC 111321, Colombia; PhD Programme in Biotechnology, Universidad Nacional de Colombia, Carrera 45#26-85, Bogotá DC 111321, Colombia. Electronic address: lauracuy@outlook.com.

Laura Alejandra Ricaurte-Contreras (LA)

Molecular Biology and Immunology Department, Fundación Instituto de Inmunología de Colombia [FIDIC], Carrera 50#26-20, Bogotá DC 111321, Colombia. Electronic address: lricaurte@unal.edu.co.

Michel David Bohórquez (MD)

Molecular Biology and Immunology Department, Fundación Instituto de Inmunología de Colombia [FIDIC], Carrera 50#26-20, Bogotá DC 111321, Colombia. Electronic address: mdbohorqueza@unal.edu.co.

Gabriela Arévalo-Pinzón (G)

Receptor-Ligand Department, Fundación Instituto de Inmunología de Colombia [FIDIC], Carrera 50#26-20, Bogotá DC 111321, Colombia. Electronic address: gabarpi@gmail.com.

Adriana Barreto-Santamaria (A)

Receptor-Ligand Department, Fundación Instituto de Inmunología de Colombia [FIDIC], Carrera 50#26-20, Bogotá DC 111321, Colombia. Electronic address: adrianasantamaria10@gmail.com.

Laura Pabón (L)

Chemistry Department, Fundación Instituto de Inmunología de Colombia [FIDIC], Carrera 50#26-20, Bogotá DC 111321, Colombia. Electronic address: mlpabona@gmail.com.

César Reyes (C)

Structure Analysis Department, Fundación Instituto de Inmunología de Colombia [FIDIC], Carrera 50#26-20, Bogotá DC 111321, Colombia. Electronic address: cmreyessa@unal.edu.co.

Darwin Andrés Moreno-Pérez (DA)

Animal Science Faculty, Universidad de Ciencias Aplicadas y Ambientales [U.D.C.A.], Calle 222#55-37, Bogotá DC 111166, Colombia. Electronic address: darmoreno@udca.edu.co.

Manuel Alfonso Patarroyo (MA)

Molecular Biology and Immunology Department, Fundación Instituto de Inmunología de Colombia [FIDIC], Carrera 50#26-20, Bogotá DC 111321, Colombia; Microbiology Department, Faculty of Medicine, Universidad Nacional de Colombia, Carrera 45#26-85, Bogotá DC 111321, Colombia. Electronic address: mapatarr.fidic@gmail.com.

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Classifications MeSH