The Open Parasitology Journal
2010, 4 : 120-131Published online 2010 December 10. DOI: 10.2174/1874421401004010120
Publisher ID: TOPARAJ-4-120
RESEARCH ARTICLE
Peptidases: An Overview
2 Instituto Militar de Engenharia (IME), Praça General Tibúrcio 80, Praia Vermelha, CEP 22290-270 RJ, Brazil
3 Laboratório de Ultraestrutura Celular, Departamento de Ultraestrutura e Biologia Celular, Instituto Oswaldo Cruz, FIOCRUZ, Avenida Brasil 4365, 21045-900, Rio de Janeiro, RJ, Brazil
* Address correspondence to this author at the Departamento de Microbiologia Geral, Instituto de Microbiologia Prof. Paulo de Góes, Universidade Federal do Rio de Janeiro-UFRJ /CCS, Bloco I, Cidade Universitária, Ilha do Fundão, Rio de Janeiro, R.J, CEP: 21941-590, Brazil; Tel: (021) 25626743; Fax: (021) 25608344; E-mail: abvermelho@micro.ufrj.br
ABSTRACT
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.