Production, purification and crystallization of a trans‐sialidase from Trypanosoma vivax. Issue 5 (1st May 2015)

• Record Type: Journal Article
• Authors: Haynes, Carole L. F.; Ameloot, Paul; Remaut, Han; Callewaert, Nico; Sterckx, Yann G.‐J.; Magez, Stefan
• Is Part Of: Acta crystallographica. Volume 71:Issue 5(2015:May)
• Page Start: 577
• Page End: 585
• Publication Date: 2015-05-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X15002496
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Sialidases and <italic>trans</italic>‐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 <italic>Trypanosoma vivax</italic>, <italic>trans</italic>‐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 <italic>trans</italic>‐sialidases in host–parasite interaction as well as their structures remain obscure. Here, the production, purification and crystallization of a recombinant version of <italic>T. vivax</italic><italic>trans</italic>‐sialidase 1 (rTvTS1) are described. The obtained rTvTS1 crystals diffracted to a resolution of 2.5 Å and belonged to the orthorhombic space group <italic>P</italic>2₁2₁2₁, with unit‐cell parameters <italic>a</italic> = 57.3, <italic>b</italic> = 78.4, <italic>c</italic> = 209.0 Å.</p> </abstract>