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Artículo

Production of a Highly Immunogenic Antigen from SARS-CoV-2 by Covalent Coupling of the Receptor Binding Domain of Spike Protein to a Multimeric Carrier

Argentinian AntiCovid Consortium; Berguer, Paula MercedesIcon ; Blaustein, Matías; Bredeston, Luis MaríaIcon ; Craig, Patricio OliverIcon ; D’aAlessio, Cecili; Elias, Fernanda Gabriela; Farré, Paola C.; Fernández, Natalia BrendaIcon ; Gentili, Hernan GustavoIcon ; Gándola, Yamila BelénIcon ; Gasulla, JavierIcon ; Gudesblat, Gustavo EduardoIcon ; Herrera, Maria GeorginaIcon ; Ibañez, Lorena ItatíIcon ; Idrovo Hidalgo, Tommy; Nadra, Alejandro DanielIcon ; Noseda, Diego GabrielIcon ; Pavan, Carlos HumbertoIcon ; Pavan, Maria FlorenciaIcon ; Pignataro, María FlorenciaIcon ; Roman, Ernesto AndresIcon ; Ruberto, Lucas Adolfo MauroIcon ; Rubinstein, NataliaIcon ; Sanchez Sanchez, Maria VictoriaIcon ; Santos, JavierIcon ; Wetzler, Diana ElenaIcon ; Zelada, Alicia MercedesIcon
Fecha de publicación: 26/04/2021
Editorial: Cold Spring Harbor Laboratory Press
Revista: bioRxiv
ISSN: 2692-8205
Idioma: Inglés
Tipo de recurso: Artículo publicado
Clasificación temática:
Biología Celular, Microbiología

Resumen

Since the discovery of SARS-CoV-2, several antigens have been proposed to be part of COVID-19 vaccines. The receptor binding domain (RBD) of Spike protein is one of the promising candidates to develop effective vaccines since it can induce potent neutralizing antibodies. We previously reported the production of RBD in Pichia pastoris and showed it is structurally identical to the protein produced in mammalian HEK-293T cells. In this work we designed an RBD multimer construct with the purpose of increasing RBD immunogenicity. We produced multimeric particles by a transpeptidation reaction between the RBD expressed in P. pastoris and Lumazine Synthase from Brucella abortus (BLS), which is a highly immunogenic and very stable decameric protein of 170 kDa. We vaccinated mice with two doses 30 days apart, and then we measured humoral immune response. When the number of RBD copies coupled to BLS was high (6-7 RBD molecules per BLS decamer, in average), the immune response was significantly better than that elicited by RBD alone or even by RBD-BLS comprising low number of RBD copies (1-2 RBD molecules per BLS decamer). Remarkably, the construct with high number of RBD copies induced high IgG titers with high neutralizing capacity. Furthermore, a superior immune response was observed when Al(OH)3 adjuvant was added to this formulation, exhibiting a higher titer of neutralizing antibodies. Altogether our results suggest that RBD covalent coupled to BLS forming a multimer-particle shows an advantageous architecture to the antigen-presentation to the immune system which enhances immune responses. This new antigen should be considered a potent candidate for a protein-based vaccine.
Palabras clave: SARS-CoV-2 , RBD antigen , BLS decamer , sortase , COVID-19
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info:eu-repo/semantics/openAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution 2.5 Unported (CC BY 2.5)
Identificadores
URI: http://hdl.handle.net/11336/135607
URL: https://www.biorxiv.org/content/10.1101/2021.04.25.441271v1
DOI: https://doi.org/10.1101/2021.04.25.441271
Colecciones
Articulos(IBBEA)
Articulos de INSTITUTO DE BIODIVERSIDAD Y BIOLOGIA EXPERIMENTAL Y APLICADA
Citación
Argentinian AntiCovid Consortium; Berguer, Paula Mercedes; Blaustein, Matías; Bredeston, Luis María; Craig, Patricio Oliver; et al.; Production of a Highly Immunogenic Antigen from SARS-CoV-2 by Covalent Coupling of the Receptor Binding Domain of Spike Protein to a Multimeric Carrier; Cold Spring Harbor Laboratory Press; bioRxiv; 2021; 26-4-2021; 1-38
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