Study of the differentially abundant proteins among leishmania amazonensis, l. braziliensis, and l. infantum

• Autor(a) principal: Bruna Soares de Souza Lima Rodrigues
• Data de Publicação: 2020
• Outros Autores: Bárbara Beiral Esteves, Luiz Carlos Fialho Júnior, Tiago Antônio de Oliveira Mendes, Simone da Fonseca Pires, Donat Alexander de Chapeaurouge, Jonas Enrique Aguilar Perales, Hélida Monteiro de Andrade
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UFMG
• Texto Completo: https://doi.org/10.1371/journal.pone.0240612; http://hdl.handle.net/1843/52638
• topic: Leishmaniasis; Leishmania braziliensis; Leishmania infantum; Proteins; Parasitic diseases; Leishmaniose; Leishmania braziliensis; Leishmania infantum; Proteínas; Doenças parasitárias

Leishmaniasis has been considered as emerging and re-emerging disease, and its increasing global incidence has raised concerns. The great clinical diversity of the disease is mainly determined by the species. In several American countries, tegumentary leishmaniasis (TL) is associated with both Leishmania amazonensis and L. braziliensis, while visceral leishmaniasis (VL) is associated with L. (L.) infantum. The major molecules that determine the most diverse biological variations are proteins. In the present study, through a DIGE approach, we identified differentially abundant proteins among the species mentioned above. We observed a variety of proteins with differential abundance among the studied species; and the biological networks predicted for each species showed that many of these proteins interacted with each other. The prominent proteins included the heat shock proteins (HSPs) and the protein network involved in oxide reduction process in L. amazonensis, the protein network of ribosomes in L. braziliensis, and the proteins involved in energy metabolism in L. infantum. The important proteins, as revealed by the PPI network results, enrichment categories, and exclusive proteins analysis, were arginase, HSPs, and trypanothione reductase in L. amazonensis; enolase, peroxidoxin, and tryparedoxin1 in L. braziliensis; and succinyl-CoA ligase [GDP -forming] beta-chain and transaldolase in L. infantum.