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Coleção de Protozários da Fundação Os... 1 Grupo de Biofísica Computacional e Mo... 1 Laboratório de Biologia Computacional... 1 Laboratório de Estudos Avançados de M... 1 Laboratório de Estudos Integrados em ... 1 Laboratório de Genômica Funcional e B... 1 Life Science Research Centre Faculty ... 1 Martsinovsky Institute of Medical Par... 1 Programa de Pós Graduação em Bioquími... 1
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Coleção de Protozários da Fundação Os... 1 Grupo de Biofísica Computacional e Mo... 1 Laboratório de Biologia Computacional... 1 Laboratório de Estudos Avançados de M... 1 Laboratório de Estudos Integrados em ... 1 Laboratório de Genômica Funcional e B... 1 Life Science Research Centre Faculty ... 1 Martsinovsky Institute of Medical Par... 1 Programa de Pós Graduação em Bioquími... 1
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- Ennes-Vidal, Vítor
- Antunes, Deborah
- Poláková, Ester
- Yurchenko, Vyacheslav
- Oliveira, Simone S C
- Faria da Mota, Fabio
- Guimaraes, Ana Carolina R
- Caffarena, Ernesto R
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S Santos, André L
Autor S Santos, André L ORCID Laboratório de Estudos Avançados de Microrganismos Emergentes e Resistentes, Instituto de Microbiologia Paulo de Góes, Universidade Federal do Rio de Janeiro (UFRJ), Rio de Janeiro 21941-902, Brazil Programa de Pós-Graduação em Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro (UFRJ), Rio de Janeiro 21941-902, Brazil
- Branquinha, Marta H
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PubMed
35887004
DOI
10.3390/ijms23147660
Knihovny.cz E-zdroje
Leishmania tarentolae is a non-pathogenic trypanosomatid isolated from lizards widely used for heterologous protein expression and extensively studied to understand the pathogenic mechanisms of leishmaniasis. The repertoire of leishmanolysin genes was reported to be expanded in L. tarentolae genome, but no proteolytic activity was detected. Here, we analyzed L. tarentolae leishmanolysin proteins from the genome to the structural levels and evaluated the enzymatic activity of the wild-type and overexpressing mutants of leishmanolysin. A total of 61 leishmanolysin sequences were retrieved from the L. tarentolae genome. Five of them were selected for phylogenetic analysis, and for three of them, we built 3D models based on the crystallographic structure of L. major ortholog. Molecular dynamics simulations of these models disclosed a less negative electrostatic potential compared to the template. Subsequently, L. major LmjF.10.0460 and L. tarentolae LtaP10.0650 leishmanolysins were cloned in a pLEXSY expression system into L. tarentolae. Proteins from the wild-type and the overexpressing parasites were submitted to enzymatic analysis. Our results revealed that L. tarentolae leishmanolysins harbor a weak enzymatic activity about three times less abundant than L. major leishmanolysin. Our findings strongly suggest that the less negative electrostatic potential of L. tarentolae leishmanolysin can be the reason for the reduced proteolytic activity detected in this parasite.
- MeSH
- fylogeneze MeSH
- Leishmania * genetika metabolismus MeSH
- leishmanióza * parazitologie MeSH
- metaloendopeptidasy metabolismus MeSH
- paraziti * MeSH
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- časopisecké články MeSH
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