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

被引:4
作者
Jimenez-Sandoval, Pedro [1 ]
Margarita Lopez-Castillo, Laura [1 ]
Trasvina-Arenas, Carlos H. [1 ]
Brieba, Luis G. [1 ]
机构
[1] IPN, Lab Nacl Genom Biodiversidad, Ctr Invest & Estudios Avanzados, Apartado Postal 629, Guanajuato 36821, Mexico
关键词
Immunoglobulin fold; evolution; cysteine protease inhibitors; cysteine proteases; parasites; pathogenesis; ENTAMOEBA-HISTOLYTICA; CRYSTAL-STRUCTURE; 3-DIMENSIONAL STRUCTURE; CRYPTOSPORIDIUM-PARVUM; CRYSTALLOGRAPHIC STRUCTURE; PEPTIDASE INHIBITOR; VIRULENCE FACTORS; STRUCTURAL BASIS; FAB FRAGMENT; CHAGASIN;
D O I
10.2174/1389203717666160813163837
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1035 / 1042
页数:8
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