Alane Beatriz Vermelho, Ana Cristina Nogueira de Melo, Rosangela Araújo Soares, Daniela Sales Alviano, Edilma Paraguai Souza, Thaïs Souto-Padrón , Giseli Capaci Rodrigues , Alcino Palermo de Aguiar , Mirian Claudia Pereira , Antonio Ferreira-Pereira , Maria Socorro S. Rosa , Maria Nazareth Leal Meirelles , Celuta Sales Alviano
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.
Abstract HTML Views: 454 PDF Downloads: 166 Total Views/Downloads: 853
Abstract HTML Views: 317 PDF Downloads: 121 Total Views/Downloads: 616
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