Antibodies response induced by recombinant virus-like particles from Triatoma virus and chimeric antigens from Trypanosoma cruzi

Aline Maria Vasconcelos Queiroz; Yulia Aleksandrovna Yanshina; Emily Thays da Silva Rodrigues; Fred Luciano Neves Santos; Paola Alejandra Fiorani Celedon; Sweta Maheshwari; Sandra Beatriz Gabelli; Carla Stephanie Peucelle Rubio; Aritz Durana; Diego M A Guérin; Marcelo Sousa Silva

doi:10.1016/j.vaccine.2021.05.039

Antibodies response induced by recombinant virus-like particles from Triatoma virus and chimeric antigens from Trypanosoma cruzi

Vaccine. 2021 Jul 30;39(33):4723-4732. doi: 10.1016/j.vaccine.2021.05.039. Epub 2021 May 27.

Affiliations

¹ Postgraduate Programme in Pharmaceutical Sciences, Federal University of Rio Grande do Norte, Rua Gen, Gustavo Cordeiro de Farias, 384, 59012-570 Natal, Brazil; Immunoparasitology Laboratory, Department of Clinical and Toxicological Analysis, Federal University of Rio Grande do Norte, Rua Gen, Gustavo Cordeiro de Farias, 384, 59012-570 Natal, Brazil.
² Global Health and Tropical Medicine, Institute of Hygiene and Tropical Medicine, Universidade Nova de Lisboa, Rua da Juqueira, 100, 1800-166 Lisbon, Portugal.
³ Immunoparasitology Laboratory, Department of Clinical and Toxicological Analysis, Federal University of Rio Grande do Norte, Rua Gen, Gustavo Cordeiro de Farias, 384, 59012-570 Natal, Brazil.
⁴ Advanced Public Health Laboratory, Gonçalo Moniz Institute, Fiocruz, Rua Waldemar Falcão, 121, 40296-710 Salvador, Brazil. Electronic address: fred.santos@fiocruz.br.
⁵ Molecular Biology Institute of Paraná, Rua Professor Algacyr Munhoz Mader, 3775, 81350-010 Curitiba, Brazil. Electronic address: paolafc@ibmp.org.br.
⁶ School of Medicine, Johns Hopkins University, 725 N Wolfe St, Baltimore, MD 21205, USA.
⁷ School of Medicine, Johns Hopkins University, 725 N Wolfe St, Baltimore, MD 21205, USA. Electronic address: gabelli@jhmi.edu.
⁸ Departamento de Bioquímica y Biología Molecular, Instituto Biofisika, Universidad del País Vasco (UBF, CSIC, UPV-EHU), B° Sarriena S/N, 48940 Leioa, Bizkaia, Spain; Ikosaedrika Biologicals S.L. ZITEK Edificio Rectorado UPV/EHU, B° Sarriena S/N, 48940 Leioa, Vizcaya, Spain.
⁹ Instituto Biofisika (CSIC, UPV/EHU), Fundación Biofísica Bizkaia, B° Sarriena S/N, 48940 Leioa, Vizcaya, Spain.
¹⁰ Departamento de Bioquímica y Biología Molecular, Instituto Biofisika, Universidad del País Vasco (UBF, CSIC, UPV-EHU), B° Sarriena S/N, 48940 Leioa, Bizkaia, Spain; Ikosaedrika Biologicals S.L. ZITEK Edificio Rectorado UPV/EHU, B° Sarriena S/N, 48940 Leioa, Vizcaya, Spain. Electronic address: diego.guerin@ehu.es.
¹¹ Postgraduate Programme in Pharmaceutical Sciences, Federal University of Rio Grande do Norte, Rua Gen, Gustavo Cordeiro de Farias, 384, 59012-570 Natal, Brazil; Immunoparasitology Laboratory, Department of Clinical and Toxicological Analysis, Federal University of Rio Grande do Norte, Rua Gen, Gustavo Cordeiro de Farias, 384, 59012-570 Natal, Brazil; Global Health and Tropical Medicine, Institute of Hygiene and Tropical Medicine, Universidade Nova de Lisboa, Rua da Juqueira, 100, 1800-166 Lisbon, Portugal. Electronic address: mssilva@ihmt.unl.pt.

PMID: 34053789
DOI: 10.1016/j.vaccine.2021.05.039

Abstract

Background: The infection caused by the protozoan Trypanosoma cruzi affects humans and is called as Chagas disease. Currently, the main measures available to reduce the incidence of this disease are drug treatment and vector control. Traditionally, the development of vaccines occurs mainly through the use of antigenic candidates of the etiologic agent in the form of a vaccine preparation. Virus-like particles (VLPs) are structures analogous to viral capsids composed essentially of structural proteins and are widely used in vaccination protocols because of their immunostimulatory properties. In this context, the objective of this study was to use strategies in a murine immunization model to characterize the immunostimulatory capacity of VLPs from Triatoma virus (TrV-VLPs), analysed in the presence or absence of the aluminium vaccine adjuvant. In parallel, to characterize the immunogenic behaviour of four T. cruzi chimeric recombinant proteins (mix-IBMP) associated with TrV-VLPs or aluminium vaccine adjuvant.

Method: We immunized BALB/c mice once or twice, depending on the strategy, and collected serum samples at 15, 30 and 45 days after the immunization. Subsequently, serum samples from animals immunized with TrV-VLPs were used to determine total IgG, IgG1, IgG2a, IgG2b and IgG3 anti-TrV-VLPs by enzyme-linked immunosorbent assay (ELISA).

Results: Data obtained demonstrate the ability of TrV-VLPs to preferably induce IgG2b and IgG3 type antibodies in the absence of aluminium adjuvant. In fact, the use of aluminium did not interfere with the total IgG profile of anti-TrV-VLPs. Interestingly, mix-IBMP had a better profile of total IgG, IgG1 and IgG3 subclasses when mixed with TrV-VLPs.

Conclusion: In conclusion, these results suggest the potential of TrV-VLPs as a vaccine adjuvant and the use of T. cruzi chimeric antigens as a rational strategy for the development of vaccines against the experimental model of Chagas disease.

Keywords: Adjuvant; Chagas disease; Humoral immune response; Triatoma virus; Trypanosoma cruzi; Virus-like particles (VLPs).

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Chagas Disease* / prevention & control
Dicistroviridae*
Mice
Mice, Inbred BALB C
Trypanosoma cruzi*

Supplementary concepts

Triatoma virus