Cysteine Proteases Inhibitors with Immunoglobulin-Like Fold in Protozoan Parasites and their Role in Pathogenesis.

Abstract:

:The number of protein folds in nature is limited, thus is not surprising that proteins with the same fold are able to exert different functions. The cysteine protease inhibitors that adopt an immunoglobulin- like fold (Ig-ICPs) are inhibitors encoded in bacteria and protozoan parasites. Structural studies indicate that these inhibitors resemble the structure of archetypical proteins with an Ig fold, like antibodies, cadherins or cell receptors. The structure of Ig-ICPs from four different protozoan parasites clearly shows the presence of three loops that form part of a protein-ligand interaction surface that resembles the antigen binding sites of antibodies. Thus, Ig-ICPs bind to different cysteine proteases using a tripartite mechanism in which their BC, DE and FG loops are responsible for the main interactions with the target cysteine protease. Ig-ICPs from different protozoan parasites regulate the enzymatic activity of host or parasite's proteases and thus regulate virulence and pathogenesis.

journal_name

Curr Protein Pept Sci

authors

Jimenez-Sandoval P,Lopez-Castillo LM,Trasviña-Arenas CH,Brieba LG

doi

10.2174/1389203717666160813163837

subject

Has Abstract

pub_date

2017-01-01 00:00:00

pages

1035-1042

issue

10

eissn

1389-2037

issn

1875-5550

pii

CPPS-EPUB-77733

journal_volume

18

pub_type

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