Beyond the VSG Layer: Exploring the Role of Intrinsic Disorder in the Invariant Surface Glycoproteins of African Trypanosomes.

Sülzen H, Volkov AN, Geens R, Zahedifard F, Stijlemans B, Zoltner M, Magez S, Sterckx YG, Zoll S, PLoS Pathog 20(4):e1012186 (2024) Europe PMC

SASDT95 – Trypanosoma brucei gambiense invariant surface glycoprotein 75 (ISG75)

ISG75
MWexperimental 51 kDa
MWexpected 50 kDa
VPorod 85 nm3
log I(s) 7.89×101 7.89×100 7.89×10-1 7.89×10-2
ISG75 small angle scattering data  s, nm-1
ln I(s)
ISG75 Guinier plot ln 7.89×101 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
ISG75 Kratky plot 1.104 0 √3 sRg
p(r)
ISG75 pair distance distribution function Rg: 3.3 nm 0 Dmax: 11.1 nm

Data validation

Fits and models

log I(s)
 s, nm-1
ISG75 BILBOMD model
ISG75 BILBOMD model
Synchrotron SAXS data from solutions of Trypanosoma brucei gambiense invariant surface glycoprotein 75 (ISG75) in 20 mM HEPES, 150 mM NaCl, 3% glycerol, pH 7.5 were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.099 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 9.8 mg/ml was injected at a 0.20 ml/min flow rate onto a Cytiva Superdex 200 Increase 3.2/300 column at 20°C. 1000 successive 0.750 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

ISG75 (ISG75)
Mol. type   Protein
Organism   Trypanosoma brucei gambiense
Olig. state   Monomer
Mon. MW   50.1 kDa
 
UniProt   Q1WK95 (29-462)
Sequence   FASTA