Advanced search
Start date
Betweenand
Related content
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Functional and structural characterization of an ecotin-like serine protease inhibitor from Trypanosoma cruzi

Full text
Author(s):
Show less -
Garcia, Felipe Baena [1] ; Cabral, Aline Diniz [1] ; Fuhlendorf, Max Mario [1] ; da Cruz, Geomar Feitosa [2] ; dos Santos, Juliete Vitorino [1] ; Ferreira, Graziele Cristina [1] ; Carneiro de Rezende, Bernard Robin [1] ; Santana, Carla Moreira [1] ; Puzer, Luciano [1] ; Sasaki, Sergio Daishi [1] ; Garcia, Wanius [2] ; Speranca, Marcia Aparecida [1]
Total Authors: 12
Affiliation:
[1] Univ Fed ABC, Ctr Ciencias Nat & Humanas, Rua Acturus 03, Sala 226, Lab 105, BR-09606070 Sao Bernardo Do Campo, SP - Brazil
[2] Univ Fed ABC, Ctr Ciencias Nat & Humanas, BR-09210170 Santo Andre, SP - Brazil
Total Affiliations: 2
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 151, p. 459-466, MAY 15 2020.
Web of Science Citations: 0
Abstract

Ecotin, a seri ne peptidase inhibitor (ISP), discovered in Escherichia coil, inhibit a wide range of nypsin-like serine peptidases, protecting microorganisms from the host's immune response. In eukaryotes, ISPs encoding genes were found only in Trypanosomatidae protozoa, including the genus Trypanosome, which harbors Trypanosome cruzi, the ethiological agent of Chagas' disease. T. cruzi encodes the ISP2 Trypanosomatidae orthologous, which in Leishmania species present inhibitory activity on mammalian proteases from S1A family suggesting its role in vertebrate-host-parasite interactions. In this study, the structural and biochemical characterization of the recombinant T. cruzi ISP2 (rTdSP2), produced in E. coli was purified in soluble form and analyzed by circular dichroism, fluorescence spectroscopy, native electrophoresis, dynamic light scattering, low X-ray scattering and homology modeling. The obtained data revealed that rTdSP2 was biologically active and forms homodimers in solution. Furthermore, inhibitory activity of rTcISP2 against human neutrophil elastase (HNE) is the highest among ISP2 orthologous from bacteria and trypanosomatids. The role of NE to control T. cruzi parasites through modulation of cellular and humoral innate immune responses in vertebrate hosts, make TcISP2 a key molecular component for parasite infection efficiency, providing a useful basis for investigation of host-parasite interactions and the potential of TcISP2 for biotechnological applications. (C) 2020 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 13/26096-4 - Heterologous expression of the chitinase enzyme of Leishmania (L.) infantum chagasi, Leishmania (V.) braziliensis and Leishmania (V.) amazonensis: serological diagnosis and comparative molecular study using expression systems of insects cell and bacteria
Grantee:Aline Diniz Cabral
Support Opportunities: Scholarships in Brazil - Post-Doctoral
FAPESP's process: 17/17275-3 - Studies of the mode of action of two lytic polysaccharide monooxygenases from insect (order: isoptera): molecular structure, bioinorganic chemistry and biotechnological applications
Grantee:Wanius José Garcia da Silva
Support Opportunities: Regular Research Grants
FAPESP's process: 16/14514-4 - Characterization of the chitinase from South American endemic Leishmania species: use in diagnosis in humans, dogs and sandflies.
Grantee:Marcia Aparecida Speranca
Support Opportunities: Regular Research Grants