Trans-sialidase and mucins of Trypanosoma cruzi: an important interplay for the parasite

被引:64
作者
Giorgi, M. Eugenia [1 ]
de Lederkremer, Rosa M. [1 ]
机构
[1] Univ Buenos Aires, Dept Quim Organ, Fac Ciencias Exactas & Nat, CIHIDECAR, RA-1428 Buenos Aires, DF, Argentina
关键词
Trypanosoma cruzi; Chagas disease; Trans-sialidase; Mucins; ALPHA-GALACTOSYL ANTIBODIES; N-ACETYLGLUCOSAMINE; CHAGAS-DISEASE; IN-VIVO; LINKED OLIGOSACCHARIDES; TRYPOMASTIGOTE FORMS; STRUCTURAL INSIGHTS; VIRULENCE FACTOR; MAMMALIAN-CELLS; O-GLYCANS;
D O I
10.1016/j.carres.2011.04.006
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
A dense glycocalix covers the surface of Trypanosoma cruzi, the agent of Chagas disease. Sialic acid in the surface of the parasite plays an important role in the infectious process, however, T. cruzi is unable to synthesize sialic acid or the usual donor CMP-sialic acid. Instead, T. cruzi expresses a unique enzyme, the trans-sialidase (TcTS) involved in the transfer of sialic acid from host glycoconjugates to mucins of the parasite. The mucins are the major glycoproteins in the insect stage epimastigotes and in the infective trypomastigotes. Both, the mucins and the TcTS are anchored to the plasma membrane by a glycosylphosphatidylinositol anchor. Thus, TcTS may be shed into the bloodstream of the mammal host by the action of a parasite phosphatidylinositol-phospholipase C, affecting the immune system. The composition and structure of the sugars in the parasite mucins is characteristic of each differentiation stage, also, interstrain variations were described for epimastigote mucins. This review focus on the characteristics of the interplay between the trans-sialidase and the mucins of T. cruzi and summarizes the known carbohydrate structures of the mucins. (C) 2011 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1389 / 1393
页数:5
相关论文
共 50 条
[31]   Trans-sialidase from Trypanosoma cruzi catalyzes sialoside hydrolysis with retention of configuration [J].
Todeschini, AR ;
Mendonça-Previato, L ;
Previato, JO ;
Varki, A ;
van Halbeek, H .
GLYCOBIOLOGY, 2000, 10 (02) :213-221
[32]   Development of New and Selective Trypanosoma cruzi trans-Sialidase Inhibitors from Sulfonamide Chalcones and Their Derivatives [J].
Kim, Jin Hyo ;
Ryu, Hyung Won ;
Shim, Jae Hoon ;
Park, Ki Hun ;
Withers, Stephen G. .
CHEMBIOCHEM, 2009, 10 (15) :2475-2479
[33]   Structure-Based Virtual Screening of New Benzoic Acid Derivatives as Trypanosoma cruzi Trans-sialidase Inhibitors [J].
Karina Vazquez-Jimenez, Lenci ;
Delia Paz-Gonzalez, Alma ;
Juarez-Saldivar, Alfredo ;
Laura Uhrig, Maria ;
Agusti, Rosalia ;
Reyes-Arellano, Alicia ;
Nogueda-Torres, Benjamin ;
Rivera, Gildardo .
MEDICINAL CHEMISTRY, 2021, 17 (07) :724-731
[34]   Identification of glycoproteins targeted by Trypanosoma cruzi trans-sialidase, a virulence factor that disturbs lymphocyte glycosylation [J].
Muia, Romina P. ;
Yu, Hai ;
Prescher, Jennifer A. ;
Hellman, Ulf ;
Chen, Xi ;
Bertozzi, Carolyn R. ;
Campetella, Oscar .
GLYCOBIOLOGY, 2010, 20 (07) :833-842
[35]   Improved bioavailability of inhibitors of Trypanosoma cruzi trans-sialidase: PEGylation of lactose analogs with multiarm polyethyleneglycol [J].
Eugenia Giorgi, M. ;
Ratier, Laura ;
Agusti, Rosalia ;
Frasch, Alberto C. C. ;
de Lederkremer, Rosa M. .
GLYCOBIOLOGY, 2012, 22 (10) :1363-1373
[36]   Synthesis of oseltamivir conjugates with lactose analogs for inhibition studies on Trypanosoma cruzi trans-sialidase [J].
Eugenia Giorgi, M. ;
Piuselli, Damian ;
Agusti, Rosalia ;
de Lederkremer, Rosa M. .
ARKIVOC, 2011, :260-271
[37]   trans-Sialidase Neutralizing Antibody Detection in Trypanosoma cruzi-Infected Domestic Reservoirs [J].
Sartor, Paula A. ;
Cardinal, Martha V. ;
Orozco, Marcela M. ;
Guertler, Ricardo E. ;
Leguizamon, M. Susana .
CLINICAL AND VACCINE IMMUNOLOGY, 2011, 18 (06) :984-989
[38]   Modulation of Catalytic Function by Differential Plasticity of the Active Site: Case Study of Trypanosoma cruzi trans-Sialidase and Trypanosoma rangeli Sialidase [J].
Demir, Oezlem ;
Roitberg, Adrian E. .
BIOCHEMISTRY, 2009, 48 (15) :3398-3406
[39]   SEQUENCE OF A TRYPANOSOMA-RANGELI GENE CLOSELY-RELATED TO TRYPANOSOMA-CRUZI TRANS-SIALIDASE [J].
BUSCHIAZZO, A ;
CREMONA, ML ;
CAMPETELLA, O ;
FRASCH, ACC ;
SANCHEZ, DO .
MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 1993, 62 (01) :115-116
[40]   The role of natural selection in shaping genetic variation in a promising Chagas disease drug target: Trypanosoma cruzi trans-sialidase [J].
Gallane, Joseph P. ;
Lima-Cordon, Raquel Asuncion ;
Justi, Silvia A. ;
Monroy, Maria Carlota ;
Viola, Toni ;
Stevens, Lori .
INFECTION GENETICS AND EVOLUTION, 2018, 62 :151-159