Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5509029 | Biochimie | 2017 | 9 Pages |
Abstract
Leishmania (Viannia) braziliensis presents adaptive protease-dependent mechanisms, as cysteine proteinases B (CPB). This study investigates the expression of three cpb gene isoforms and CPB enzymatic activity during the parasite differentiation. Relative expression levels of LbrM.08.0810 gene were assessed, exhibiting a higher quantity of transcripts in the logarithmic promastigotes phase than in the stationary promastigotes phase (>1.5 times). The cbp gene tends to decrease during acid pH shock and increases when the temperature rises (>1.3 times). LbrM.08.0820 and LbrM.08.0830 genes exhibited similar expression profiles to LbrM.08.0810 gene, with lower levels being observed overall. The proteolytic activity exhibits a gradual increase during the parasite's differentiation with low levels in samples of logarithmic promastigotes phase (3.2 ± 0.08 mmol minâ1 mg proteinâ1) to a peak of activity after 72 h of incubation at 32 °C (4.2 ± 0.026 mmol minâ1 mg proteinâ1) followed by a subsequent decrease of 68 % of peak activity levels after 96 h of incubation at 32 °C (2.8 ± 0.37 mmol minâ1 mg proteinâ1). These activities were also measured in the presence of selective inhibitors for cysteine proteinases, such as Z-Phe-Phe-fluoromethyl ketone and trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane, demonstrating their source as cathepsin-like proteinases. To the best of our knowledge, this report presents the first description of a modulation of cathepsin L-like expression during the L. (V.) braziliensis in vitro differentiation induced by acid pH and high temperature.
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Authors
Cinthia Bernardes Gomes, Franklin Souza -Silva, Karen dos Santos Charret, Bernardo Acácio Santini Pereira, Léa Cysne Finkelstein, Raquel Santos-de-Souza, Luzia Monteiro de Castro Côrtes, Mirian Claudia Souza Pereira, Francisco Odêncio Jr.,