POTELLIGENT Technology involves the reduction of the amount of fucose
in the carbohydrate structure of an antibody using a proprietary fucosyl transferase-knockout CHO cell line as a production cell.
Biopolymer tubes were made from a continuous surface film of an exopolyssacharide, a bioactive copolymer consisting of 87 % glucose, 8.5 % xylose, 1.68 % ribose, 0.83 % glucuronic acid, 0.82 % mannose, 0.37 % arabinose, 0.13 % galactose, 0.01 % rhamnose and 0.01 % fucose
obtained from sugar polymerization of sugarcane molasses by biotechnological means, as suggested by Paterson-Beedle et al.
The FUT2 gene encodes fucosyl transferases that transfer a terminal fucose
residue to a pre-existing precursor substance to form a soluble H antigen in secretor tissues, which serves as a precursor for soluble ABH antigens.
The standard monosaccharides mannose (Man), rhamnose (Rha), glucuronic acid (GlcA), galacturonic acid (GalA), glucose (Glc), galactose (Gal), xylose (Xyl), arabinose (Ara) and fucose
(Fuc) were all purchased from Sigma.
Among the identified glycopeptides, EEQYNSTYR_3(hexose)_3(N-acetylhexosamine)_1(fucose
)_0(sialic acid) was eluted at the retention time (RT), 28.25 min.
Analyses of neutral sugars including fucose
(Fuc), rhamnose (Rha), arabinose (Ara), galactose (Gal), and xylose (Xyl) were performed using the method described by Njoroge et al.
Standard monosaccharides (rhamnose, arabinose, fucose
, xylose, mannose, glucose, and galactose) are used as reference.
The results showed that the DCs stimulated by LPS and fucose
together did not induce [T.sub.FH] polarisation.
The preliminary chemical characterization showed that, other than fucose
, the most abundant sugars were trehalose and galactose in the polysaccharidic extract from F.
One terminal bears an a1,2-linked fucose
residue (Fuca1-2Gal[beta]1-4GlcNAc) while the other terminal bears an a1,3- or 1,4-linked fucose
residue producing a L[e.sup.x] structure (Gal [beta]1-4 (Fuca1-3) GlcNAc).
Lens culinaris agglutinin–fluorescein isothiocyanate (LCA-FITC; Vector Laboratories, Burlingame, USA) was used to detect the expression of core fucose
; and staining was performed as described previously.[sup],
Compared with the histo-blood group antigen (HBGA) binding surface of strain SMV, the GII.2 strains in this study had 15 aa mutations in VP1, including 8 aa mutations at residues 335-349 around the HBGA binding site I in the P2 domain, although the conserved set of residues (Asn352, Arg353, Asp382, and Gly445) required for binding the fucose
moiety of HBGAs in SMV was unchanged.