Surface Topology Evolution of Trypanosoma Trans-Sialidase
The trans-sialidase (TS) from Trypanosoma cruzi is a multifunctional protein given by its enzymatic activity and binding properties. The complex structure of TS promotes topology changes over the protozoa’s surface with dramatic consequences for its biolo
- PDF / 523,719 Bytes
- 14 Pages / 439.37 x 666.14 pts Page_size
- 78 Downloads / 247 Views
Surface Topology Evolution of Trypanosoma Trans-Sialidase Sergio Steven Cornejo Rubin De Celis
Abstract The trans-sialidase (TS) from Trypanosoma cruzi is a multifunctional protein given by its enzymatic activity and binding properties. The complex structure of TS promotes topology changes over the protozoa’s surface with dramatic consequences for its biology. Detailed sequence analyses show that the evolution of TS in T. cruzi and other trypanosomes as well as its genomic organization is even more complex than it has been supposed before. All of these aspects are still neglected when TS is selected as a target for drug design and chemotherapy of Chagas’ disease. Herein these aspects are discussed in the context of TS multifunctionality and dynamics drug design.
Abbreviations GH-33 GPI MDS SAPA TS TS342His/− TS342His/SAPA TS342Tyr/− TS342Tyr/SAPA
Glycoside hydrolase family number 33 Glycosylphosphatidylinositol Multidimensional scaling plot Shed Acute Phase Antigen Trans-Siliadase Inactive Trans-Siliadase without SAPA Inactive Trans-Siliadase with SAPA Active Trans-Siliadase without SAPA Active Trans-Siliadase with SAPA
S.S.C.D.C. Rubin (*) Laboratorium voor Microbiële Ecologie en Technologie, Faculteit Bio-ingenieurswetenschappen, Universiteit Gent, Coupure Links 653, B-9000 Gent, Belgium Centro Nacional de Investigaciones Biotecnológicas – CNIB, Calle Alcides Arguedas 429, Cala Cala, Cochabamba, Bolívia e-mail: [email protected] A.L.S. Santos et al. (eds.), Proteins and Proteomics of Leishmania and Trypanosoma, Subcellular Biochemistry 74, DOI 10.1007/978-94-007-7305-9_9, © Springer Science+Business Media Dordrecht 2014
203
204
1
S.S.C.D.C. Rubin
Origin and Evolution of Trypanosoma Trans-Sialidase (TS)
Recent post-genomic phylogenetic analysis, including new sequences, indicates that the evolution of TS in Trypanosoma cruzi is monophyletic, while polyphyletic in others trypanosomes (Carvajal and Rubin in progress). Sialic acids have appeared in co-evolution, precisely from Echinoderms (Varki 1997; Lewis et al. 2009). The proposal of a sialidase origin in higher animals is based on the presence of apparently homologous enzymes in this kingdom, supporting the idea that some microorganisms may have acquired genetic information during association with their animal hosts. Furthermore, a sialidase gene was transferred via phages among bacteria (Roggentin et al. 1993). Acquisition in trypanosomes might have occurred from bacteria through the blood ingested by hematophogous insects. Interestingly, a sialidase activity was detected in the salivary gland of Triatoma infestans (Amino et al. 1998), supporting the notion that the origin of TS in T. cruzi could be through a parasite living within the insect vector. Within trypanosomatids, T. cruzi TS probably evolved from a conventional sialidase of a common trypanosomatid ancestor. Genetically, the stage-specific expression of T. cruzi TS involves a highly conserved 3′ untranslated region (Jager et al. 2008), suggesting that all TS genes had a common ancestor.
Data Loading...
