Production, purification and crystallization of a trans-sialidase from Trypanosoma vivax.

TitleProduction, purification and crystallization of a trans-sialidase from Trypanosoma vivax.
Publication TypeJournal Article
Year of Publication2015
AuthorsHaynes, C. L. F., P. Ameloot, H. Remaut, N. Callewaert, Y. G. J. Sterckx, and S. Magez
JournalActa Crystallogr F Struct Biol Commun
Volume71
IssuePt 5
Pagination577-85
Date Published2015 May
ISSN2053-230X
KeywordsCrystallization, Crystallography, X-Ray, Glycoproteins, Neuraminidase, Trypanosoma vivax
Abstract

Sialidases and trans-sialidases play important roles in the life cycles of various microorganisms. These enzymes can serve nutritional purposes, act as virulence factors or mediate cellular interactions (cell evasion and invasion). In the case of the protozoan parasite Trypanosoma vivax, trans-sialidase activity has been suggested to be involved in infection-associated anaemia, which is the major pathology in the disease nagana. The physiological role of trypanosomal trans-sialidases in host-parasite interaction as well as their structures remain obscure. Here, the production, purification and crystallization of a recombinant version of T. vivax trans-sialidase 1 (rTvTS1) are described. The obtained rTvTS1 crystals diffracted to a resolution of 2.5 Å and belonged to the orthorhombic space group P212121, with unit-cell parameters a = 57.3, b = 78.4, c = 209.0 Å.

DOI10.1107/S2053230X15002496
Alternate JournalActa Crystallogr F Struct Biol Commun
PubMed ID25945712
Research group: