title: Surface topology evolution of Trypanosoma trans-sialidase.
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.
authors.affiliation: Laboratorium voor Microbiële Ecologie en Technologie, Faculteit Bio-ingenieurswetenschappen, Universiteit Gent, Coupure Links 653, B-9000, Gent, Belgium, sergio.rubin@ugent.be.
authors.forename: Sergio Steven Cornejo Rubin
authors.initials: SS
authors.lastname: De Celis
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006023:Glycoproteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D009439:Neuraminidase / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D013499:Surface Properties; D014349:Trypanosoma cruzi / Q000201:enzymology*
chemical_list: D006023:Glycoproteins; C069715:trans-sialidase; D009439:Neuraminidase