Novel cysteine proteinase in<i>Trypanosoma cruzi</i>metacyclogenesis

Duschak, Vilma G.; Barboza, Mariana; García, Gabriela Andrea; Lammel, E.; Couto, Alicia S.; Isola, E.L.D.

doi:10.1017/s0031182005009030

Cited by 24 publications

(19 citation statements)

References 46 publications

(46 reference statements)

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“…This fact reinforces a possible role for this cysteine peptidase during metacyclogenesis. In addition, the authors also suggest the involvement of this enzyme in the protein degradation processes necessary for this stage-specific transformation [80].…”

Section: C14mentioning

confidence: 89%

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Biological Roles of Peptidases in Trypanosomatids~!2009-11-26~!2010-02-15~!2010-03-18~!

Vermelho

Branquinha²,

d’Avila-Levy³

et al. 2010

TOPARAJ

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Abstract:In this review, we report the recent developments in the characterization of peptidases and their possible biological functions in the Trypanosomatidae family. The focus will be on peptidases from Trypanosoma cruzi, Leishmania spp., African trypanosomes and plant and insect trypanosomatids. There are numerous events in parasite development where the involvement of peptidases has been established, and they will be approached in the present review. Also in this review we will discuss the central roles have been proposed for peptidases in diverse processes such as virulence, host cell interaction and invasion, catabolism of host proteins, differentiation, cell cycle progression and both stimulation and evasion of host immune responses.

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Section: C14mentioning

confidence: 89%

“…A novel cysteine peptidase released to the culture medium during T. cruzi metacyclogenesis was described by Duschak et al [80]. This proteolytic activity, named TcCPmet, has a molecular mass between 97 and 116 kDa, being active at pH 6.0 in SDS-PAGE.…”

Section: C14mentioning

confidence: 99%

Biological Roles of Peptidases in Trypanosomatids~!2009-11-26~!2010-02-15~!2010-03-18~!

Vermelho

Branquinha²,

d’Avila-Levy³

et al. 2010

TOPARAJ

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“…Supernatants from spontaneously generated metacyclic trypomastigotes [34] were dialyzed against 50 mM Tris-ClH pH 7.6 and applied onto the Siglec-E-Sepharose column (1 ml) three times, washed and consecutively eluted with 0.5 M and 3 M NaCl. Purification steps were tested by SDS-PAGE followed by silver staining and Western blot with rabbit polyclonal sera specific for Cz.…”

Section: Purification Of Cz By Affinity To Siglec-e-fcmentioning

confidence: 99%

Involvement of sulfates from cruzipain, a major antigen of Trypanosoma cruzi, in the interaction with immunomodulatory molecule Siglec-E

Ferrero

Heins

Soprano

et al. 2015

Med Microbiol Immunol

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In order to investigate the involvement of sulfated groups in the Trypanosoma cruzi host-parasite relationship, we studied the interaction between the major cysteine proteinase of T. cruzi, cruzipain (Cz), a sulfate-containing sialylated molecule and the sialic acid-binding immunoglobulin like lectin-E (Siglec-E). To this aim, ELISA, indirect immunofluorescence assays and flow cytometry, using mouse Siglec-E-Fc fusion molecules and glycoproteins of parasites, were performed. Competition assays verified that the lectins, Maackia amurensis II (Mal II) and Siglec-E-Fc, compete for the same binding sites. Taking into account that Mal II binding remains unaltered by sulfation, we established this lectin as sialylation degree control. Proteins of an enriched microsomal fraction showed the highest binding to Siglec-E as compared with those from the other parasite subcellular fractions. ELISA assays and the affinity purification of Cz by a Siglec-E column confirmed the interaction between both molecules. The significant decrease in binding of Siglec-E-Fc to Cz and to its C-terminal domain (C-T) after desulfation of these molecules suggests that sulfates contribute to the interaction between Siglec-E-Fc and these glycoproteins. Competitive ELISA assays confirmed the involvement of sulfated epitopes in the affinity between Siglec-E and Cz, probably modified by natural protein environment. Interestingly, data from flow cytometry of untreated and chlorate-treated parasites suggested that sulfates are not primary receptors, but enhance the binding of Siglec-E to trypomastigotic forms. Altogether, our findings support the notion that sulfate-containing sialylated glycoproteins interact with Siglec-E, an ortholog protein of human Siglec-9, and might modulate the immune response of the host, favoring parasitemia and persistence of the parasite.

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“…In addition, this CP has demonstrated an ability to induce the production of the proinflammatory peptide Lys-bradykinin by the proteolysis of kininogen or by activation of plasmatic pre-kallikrein (Del Nery, 1997;Benítez-Hernández, 2010;Capaci-Rodrigues, 2010 (Garcia, 1998;Yong, 2000;Duschak, 2006;Capaci-Rodrigues, 2010). The structure of the active site, of the cruzipain , has been reported through X-ray crystal structures of the enzyme in complex with reversible and irreversible inhibitors.…”

Section: Peptidasesmentioning

confidence: 99%