Trypanosoma cruzi Peptidases: An Overview
Alane Beatriz Vermelho*, 1, Ana Cristina Nogueira de Melo1, Rosangela Araújo Soares1, Daniela Sales Alviano1, Edilma Paraguai Souza1, Thaïs Souto-Padrón 1, Giseli Capaci Rodrigues2, Alcino Palermo de Aguiar2, Mirian Claudia Pereira3, Antonio Ferreira-Pereira1, Maria Socorro S. Rosa1, Maria Nazareth Leal Meirelles3, Celuta Sales Alviano1
Identifiers and Pagination:Year: 2010
First Page: 120
Last Page: 131
Publisher Id: TOPARAJ-4-120
Article History:Received Date: 15/11/2009
Revision Received Date: 15/8/2010
Acceptance Date: 16/8/2010
Electronic publication date: 10/12/2010
Collection year: 2010
open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: https://creativecommons.org/licenses/by/4.0/legalcode. This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Peptidases are a group of enzymes which have a catalytic function that is to hydrolyze peptide bonds of proteins. The enzymes that hydrolyze peptide bonds at the amino- or carboxy- terminus are classified as exopeptidases, and those that cleave peptide bonds inside the polypeptide are endopeptidases. Endopeptidases, such as cysteine-, metalo-, serine- and threonine peptidases as well as some exopeptidases, have been characterized in Trypanosoma cruzi. Understanding the pathogenesis of T. cruzi requires the identification of functional properties of those peptidases, as they are implied in virulence, are important for host-parasite interactions and are critical for successful survival in their hosts. Here we examine the main T. cruzi peptidases, focusing on their biological roles, especially concerning the parasite-mammalian host relations.