Bacterial targeting of the neutrophil inhibitory receptor LILRB3 to evade antibody immunity.

Rumpret M, Lewis Marffy AL, Zhang Y van Woudenbergh E, van der Lans SPA, Xu X, Fu Z, Zhao Y, Catton EA, Paré G, McGregor F, Spiller OB, Fernandes MJ, de Haas CJC, van Strijp JAG, van Sorge NM, Geisbrecht BV, McCarthy AJ, Nat Commun (2026) Europe PMC

SASDXF8 – β-Antigen C Protein bound to Leukocyte Immunoglobulin-Like Receptor LILR-B3

IgA FC receptor β-Antigen C Protein
Leukocyte immunoglobulin-like receptor subfamily B3
MWexperimental 177 kDa
MWexpected 165 kDa
VPorod 447 nm3
log I(s) 6.65×101 6.65×100 6.65×10-1 6.65×10-2
IgA FC receptor β-Antigen C Protein Leukocyte immunoglobulin-like receptor subfamily B3 small angle scattering data  s, nm-1
ln I(s)
IgA FC receptor β-Antigen C Protein Leukocyte immunoglobulin-like receptor subfamily B3 Guinier plot ln 6.66×101 Rg: 7.0 nm 0 (7.0 nm)-2 s2
(sRg)2I(s)/I(0)
IgA FC receptor β-Antigen C Protein Leukocyte immunoglobulin-like receptor subfamily B3 Kratky plot 1.104 0 3 sRg
p(r)
IgA FC receptor β-Antigen C Protein Leukocyte immunoglobulin-like receptor subfamily B3 pair distance distribution function Rg: 7.8 nm 0 Dmax: 26.5 nm

Data validation


Fits and models


log I(s)
 s, nm-1
IgA FC receptor β-Antigen C Protein Leukocyte immunoglobulin-like receptor subfamily B3 FOXSDOCK model

Synchrotron small-angle X-ray scattering (SAXS) data for β-Antigen C protein in complex with two molecules of leukocyte immunoglobulin-like receptor LILR-B3 were collected at SIBYLS beamline 12.3.1 of the Advanced Light Source in SEC-SAXS mode. In-line size-exclusion chromatography (SEC) was performed using an Agilent 1260 HPLC system. The SEC conditions were as follows: a 60 µL sample at 5 mg/mL was injected onto a Shodex KW-803 column at 4 °C that had been previously equilibrated in 20 mM HEPES, 140 mM NaCl, pH 7.4, and eluted at 0.65 mL/min. Scattering was recorded on a Pilatus3 X 2M detector at a sample-to-detector distance of 2.1 m and a wavelength of λ = 0.1127 nm (I(q) vs q; q = 4π sin θ/λ, where 2θ is the scattering angle). 913 successive 2-s frames were collected. The scattering curves were normalized to the transmitted-beam intensity, radially averaged, and corrected by subtracting the solvent blank.

IgA FC receptor β-Antigen C Protein (β-Antigen C Protein)
Mol. type   Protein
Organism   Streptococcus agalactiae
Olig. state   Monomer
Mon. MW   70.9 kDa
 
UniProt   P27951 (258-826)
Sequence   FASTA
 
Leukocyte immunoglobulin-like receptor subfamily B3 (LILRB3)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   47.0 kDa
 
UniProt   A0A0G2JM46 (24-443)
Sequence   FASTA