Disordered Motifs and Domains in Cell Control
Poster Session II
34-POS
Board 10
NMR Study of the 30 kDa Fucose-binding Lectin from
Ralstonia solanacearum
Pawel Antonik
1,2
, Alex Volkov
3
, Michaela Wimmerova
4
, Ursula Broder
1
, Nico Van Nuland
3
,
Peter Crowley
1
.
1
National University of Ireland, Galway, Galway, Ireland,
2
Teagasc Food Research Centre,
Ashtown, Dublin, Ireland,
3
Vrije Universiteit Brussel, Brussels, Belgium,
4
Masaryk University,
Brno, Czech Republic.
RSL (30 kDa trimer) is a fucose-binding lectin,
1
which is found in
Ralstonia solanacearum
, a
worldwide distributed plant pathogen, responsible for wilting in a wide range of crops.
2
NMR experiments were carried out to assign the
1
H/
15
N HSQC spectrum of RSL, a useful
“fingerprint” for future studies. RSL dynamics are being studied in addition to numerous
biological processes pertaining to folding and assembly, ligand binding and molecular
recognition.
3
Wt-RSL presents an extraordinarily strong thermostability from 86°C in the free
form to 96°C in the bound form.
4
Both NMR dynamics and SDS-PAGE experiments show how
the stability and flexibility of RSL change in the presence of different monosaccharides.
The results will aid the identification of inhibitors of RSL that function by blocking the sugar-
binding site. Such inhibitors could be further developed to prevent pathogen binding in crops.
[1] Kostlanova, N.; Mitchell, E. P.; Lortat-Jacob, H.; Oscarson, S.; Lahmann, M.; Gilboa-Garber,
N.; Chambat, G.; Wimmerova, M.; Imberty,
A. J. Biol. Chem.
2005, 280, 27839.
[2] Genin, S.; Boucher, C.
Mol. Plant Pathol.
2002, 3, 111.
[3] Palmer, A. G.
Chem. Rev.
2004, 104, 3623.
[4] Arnaud, J.; Claudinon, J.; Tröndle, K.; Trovaslet, M.; Larson, G.; Thomas, A.; Varrot, A.;
Römer, W.; Imberty, A.; Audfray, A.
ACS Chemical Biology
2013, 8, 1918.
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