Open AccessStudy of the differentially abundant proteins among Leishmania amazonensis, L. braziliensis, and L. infantum
Author(s) -
Bruna Soares de Souza Lima,
Barbara Beiral Esteves,
Luiz Carlos Fialho-Júnior,
Tiago Antônio de Oliveira Mendes,
Simone da Fonseca Pires,
Alexander Chapeourouge,
Jonás Perales,
Hélida Monteiro de Andrade
Publication year - 2020
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0240612
Subject(s) - leishmania infantum , biology , leishmania braziliensis , leishmaniasis , leishmania , proteome , biochemistry , microbiology and biotechnology , genetics , visceral leishmaniasis , parasite hosting , cutaneous leishmaniasis , world wide web , computer science
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 .