A chimeric, half-life extended lysin with a unique mode of action

Visram Z, Kestemont D, Bauer B, Qiao R, Durica-Mitic S, Majoros-Hashempour A, Schmidt J, Berdaguer R, Krey K, Mutti M, Zerbs M, von Freyberg M, Corsini L, Badarau A, Frontiers in Microbiology 17 (2026) DOI

SASDZ98 – Engineered fusion of derivative of S.aureus LytN (CHAP domain) and derivative of S.simulans lysostaphin (Fc-L1-CHAP(opt)-LSN(HEK))

Fc-L1-CHAP(opt)-LSN(HEK)
MWexperimental 120 kDa
MWexpected 148 kDa
log I(s) 1.16×104 1.16×103 1.16×102 1.16×101
Fc-L1-CHAP(opt)-LSN(HEK) small angle scattering data  s, nm-1
ln I(s)
Fc-L1-CHAP(opt)-LSN(HEK) Guinier plot ln 1.17×104 Rg: 7.3 nm 0 (7.3 nm)-2 s2
(sRg)2I(s)/I(0)
Fc-L1-CHAP(opt)-LSN(HEK) Kratky plot 1.104 0 3 sRg
p(r)
Fc-L1-CHAP(opt)-LSN(HEK) pair distance distribution function Rg: 8.8 nm 0 Dmax: 40 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Engineered fusion of derivative of S.aureus LytN (CHAP domain) and derivative of S.simulans lysostaphin (Fc-L1-CHAP(opt)-LSN(HEK)) in 20 mM HEPES, 150 mM NaCl, pH 7.0, pH 7 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 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 25.00 μl sample at 5 mg/ml was injected at a 0.35 ml/min flow rate onto a Cytiva Superdex 200 Increase 5/150 column at 25°C. 1800 successive 0.500 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.

Fc-L1-CHAP(opt)-LSN(HEK) (L1829)
Mol. type   Protein
Organism   synthetic construct
Olig. state   Dimer
Mon. MW   73.9 kDa
Sequence   FASTA