Structure of PLA2R reveals presentation of the dominant membranous nephropathy epitope and an immunogenic patch

Fresquet M, Lockhart-Cairns M, Rhoden S, Jowitt T, Briggs D, Baldock C, Brenchley P, Lennon R, Proceedings of the National Academy of Sciences 119(29) (2022) DOI

SASDNP3 – Recombinant phospholipase A2 receptor at pH 7.2

Secretory phospholipase A2 receptor
MWexperimental 242 kDa
MWexpected 189 kDa
VPorod 504 nm3
log I(s) 3.04×10-1 3.04×10-2 3.04×10-3 3.04×10-4
Secretory phospholipase A2 receptor small angle scattering data  s, nm-1
ln I(s)
Secretory phospholipase A2 receptor Guinier plot ln 3.04×10-1 Rg: 5.9 nm 0 (5.9 nm)-2 s2
Secretory phospholipase A2 receptor Kratky plot 1.104 0 3 sRg
Secretory phospholipase A2 receptor pair distance distribution function Rg: 6.0 nm 0 Dmax: 26 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of the phospholipase A2 receptor in 10 mM Bis-Tris, 150 mM NaCl, pH 7.2 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.1 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 5 mg/ml was injected at a 0.08 ml/min flow rate onto a GE Superdex 200 Increase 3.2/300 column at 25°C. 620 successive 3 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.

Data frames 353 - 381 were used for the sample and 262 - 320 for the buffer. Recombinantly expressed protein purified from HEK293 secreted media using a His-tag. PLA2R is heavily glycosylated, accounting for additional mass.

Secretory phospholipase A2 receptor
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   159.8 kDa
UniProt   Q13018 (21-1397)
Sequence   FASTA