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Title: The major leucyl aminopeptidase of Trypanosoma cruzi (LAPTc) assembles into a homohexamer and belongs to the M17 family of metallopeptidases
Authors: Cadavid-Restrepo, Gloria Ester
Gastardelo, Thiago Santana
Faudry, Eric
Silva, Hugo de Almeida
Bastos, Izabela Marques Dourado
Negreiros, Raquel Silva de
Lima, Meire Maria de
Assumpção, Teresa Cristina França de
Almeida, Keyla Caroline de
Ragno, Michel
Ebel, Christine
Ribeiro, Bergmann Morais
Felix, Carlos Roberto
Santana, Jaime Martins de
Assunto:: Tripanossoma cruzi
Chagas, Doença de
Patogênese
Issue Date: Aug-2011
Publisher: BioMed Central
Citation: RESTREPO-CADAVID, Gloria et al. The major leucyl aminopeptidase of Trypanosoma cruzi (LAPTc) assembles into a homohexamer and belongs to the M17 family of metallopeptidases. BMC Biochemistry, v. 12, n. 46, ago. 2011. Disponível em: <http://www.biomedcentral.com/1471-2091/12/46>. Acesso em: 13 de dez. 2012.
Abstract: Background Pathogens depend on peptidase activities to accomplish many physiological processes, including interaction with their hosts, highlighting parasitic peptidases as potential drug targets. In this study, a major leucyl aminopeptidolytic activity was identified in Trypanosoma cruzi, the aetiological agent of Chagas disease. Results The enzyme was isolated from epimastigote forms of the parasite by a two-step chromatographic procedure and associated with a single 330-kDa homohexameric protein as determined by sedimentation velocity and light scattering experiments. Peptide mass fingerprinting identified the enzyme as the predicted T. cruzi aminopeptidase EAN97960. Molecular and enzymatic analysis indicated that this leucyl aminopeptidase of T. cruzi (LAPTc) belongs to the peptidase family M17 or leucyl aminopeptidase family. LAPTc has a strong dependence on neutral pH, is mesophilic and retains its oligomeric form up to 80°C. Conversely, its recombinant form is thermophilic and requires alkaline pH. Conclusions LAPTc is a 330-kDa homohexameric metalloaminopeptidase expressed by all T. cruzi forms and mediates the major parasite leucyl aminopeptidolytic activity. Since biosynthetic pathways for essential amino acids, including leucine, are lacking in T. cruzi, LAPTc could have a function in nutritional supply.
Licença:: © 2011 Cadavid-Restrepo et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
DOI: https://dx.doi.org/10.1186/1471-2091-12-46
Appears in Collections:CEL - Artigos publicados em periódicos

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