Recombinant proteins of Plasmodium malariae merozoite surface protein 1 (PmMSP1): Testing immunogenicity in the BALB/c model and potential use as diagnostic tool.

Autor: Elizardez YB; Núcleo de Estudos em Malária, Superintendência de Controle de Endemias/Instituto de Medicina Tropical, Universidade de São Paulo, São Paulo, Brazil., Fotoran WL; Departamento de Parasitologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil., Junior AJG; Laboratório de Protozoologia, Instituto de Medicina Tropical, Universidade de São Paulo, São Paulo, Brazil., Curado I; Laboratório de Imunoepidemiologia, Superintendência de Controle de Endemias, São Paulo, Brazil., Junior NK; Laboratório de Protozoologia, Instituto de Medicina Tropical, Universidade de São Paulo, São Paulo, Brazil., Monteiro EF; Núcleo de Estudos em Malária, Superintendência de Controle de Endemias/Instituto de Medicina Tropical, Universidade de São Paulo, São Paulo, Brazil., Romero Neto I; Laboratório de Protozoologia, Instituto de Medicina Tropical, Universidade de São Paulo, São Paulo, Brazil., Wunderlich G; Departamento de Parasitologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil., Kirchgatter K; Núcleo de Estudos em Malária, Superintendência de Controle de Endemias/Instituto de Medicina Tropical, Universidade de São Paulo, São Paulo, Brazil.
Jazyk: angličtina
Zdroj: PloS one [PLoS One] 2019 Jul 25; Vol. 14 (7), pp. e0219629. Date of Electronic Publication: 2019 Jul 25 (Print Publication: 2019).
DOI: 10.1371/journal.pone.0219629
Abstrakt: Background: Plasmodium malariae is the third most prevalent human malaria-causing species and has a patchy, but ample distribution in the world. Humans can host the parasite for years without presenting significant symptoms, turning its diagnosis and control into a difficult task. Here, we investigated the immunogenicity of recombinant proteins of P. malariae MSP1.
Methods: Five regions of PmMSP1 were expressed in Escherichia coli as GST-fusion proteins and immunized in BALB/c mice. The specificity, subtyping, and affinity of raised antibodies were evaluated by enzyme-linked immunosorbent assays. Cellular immune responses were analyzed by lymphoproliferation assays and cytokine levels produced by splenocytes were detected by cytometry.
Results: We found that N-terminal, central regions, and PmMSP119 are strongly immunogenic in mice. After three doses, the induced immune responses remained high for 70 days. While antibodies induced after immunization with N-terminal and central regions showed similar affinities to the target antigens, affinities of IgG against PmMSP119 were higher. All proteins induced similar antibody subclass patterns (predominantly IgG1, IgG2a, and IgG2b), characterizing a mixed Th1/Th2 response. Further, autologous stimulation of splenocytes from immunized mice led to the secretion of IL2 and IL4, independently of the antigen used. Importantly, IgG from P. malariae-exposed individuals reacted against PmMSP1 recombinant proteins with a high specificity. On the other hand, sera from P. vivax or P. falciparum-infected individuals did not react at all against recombinant PmMSP1 proteins.
Conclusion: Recombinant PmMSP1 proteins are very useful diagnostic markers of P. malariae in epidemiological studies or in the differential diagnosis of malaria caused by this species. Immunization with recombinant PmMSP1 proteins resulted in a significant humoral immune response, which may turn them potential component candidates for a vaccine against P. malariae.
Competing Interests: The authors have declared that no competing interests exist.
Databáze: MEDLINE
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