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Methyl 2-acetamido-2-deoxy-β-D-glucopyranosyl-(1→4)-2-acetamido-2-deoxy-β-D-glucopyranoside (methyl β-chitobioside), (IV), crystallizes from aqueous methanol at room temperature to give a structure (C17H30N2O22·CH3OH) containing conformational disorder in the exocyclic hydroxymethyl group of one of its βGlcNAc residues. As observed in other X-ray structures of disaccharides containing β-(1→4)O-glycosidic linkages, inter-residue hydrogen bonding between O3H of the βGlcNAc bearing the OCH3aglycone and O5 of the adjacent βGlcNAc is observed based on the 2.79 Å internuclear distance between the O atoms. The structure of (IV) was compared to that determined previously for 2-acetamido-2-deoxy-β-D-glucopyranosyl-(1→4)-2-acetamido-2-deoxy-β-D-glucopyranose (β-chitobiose), (III). TheO-glycosidic linkage torsion angles,phi(ϕ) andpsi(ψ), in (III) and (IV) differ by 6–8°. TheN-acetyl side chain conformation in (III) and (IV) shows some context dependence, with the C1—C2—N—Ccartorsion angle 10–15° smaller for the βGlcNAc residue involved in the internalO-glycosidic linkage. In (IV), conformational disorder is observed in the exocyclic hydroxymethyl (–CH2OH) group in the βGlcNAc residue bearing the OCH3aglycone, and a fitting of the electron density indicates an approximate 50:50 distribution of thegauche–gauche(gg) andgauche–trans(gt) conformers in the lattice. Similar behavior is not observed in (III), presumably due to the different packing structure in the vicinity of the –CH2OH substituent that affects its ability to hydrogen bond to proximal donors/acceptors. Unlike (IV), a re-examination of the previously reported electron density of (III) revealed conformational disorder in theN-acetyl side chain attached to the reducing-end βGlcNAc residue caused by rotation about the C2—N bond.
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Structural and genetic basis for the binding of a mouse monoclonal antibody to Flavobacterium psychrophilum lipopolysaccharide
Abstract A mouse monoclonal antibody (mAb FL100A) previously prepared againstFlavobacterium psychrophilum(Fp) CSF259‐93 has now been examined for binding to lipopolysaccharides (LPS) of this strain andFp950106‐1/1. The corresponding O‐polysaccharides (O‐PS) of these strains are formed by identical trisaccharide repeats composed ofl‐Rhamnose (l‐Rha), 2‐acetamido‐2‐deoxy‐l‐fucose (l‐FucNAc) and 2‐acetamido‐4‐R1‐2,4‐dideoxy‐d‐quinovose (d‐Qui2NAc4NR1) where R1represents a dihydroxyhexanamido moiety. The O‐PS loci of these strains are also identical except for the gene (wzy1orwzy2) that encodes the polysaccharide polymerase. Accordingly, adjacent O‐PS repeats are joined throughd‐Qui2NAc4NR1andl‐Rha bywzy2‐dependent α(1–2) linkages inFpCSF259‐93 versuswzy1‐dependent β(1–3) linkages inFp950106‐1/1. mAb FL100A reacted strongly withFpCSF259‐93 O‐PS and LPS but weakly or not at all withFp950106‐1/1 LPS and O‐PS. Importantly, it also labelled cell surface blebs on the former but not the latter strain. Additionally, mAb binding was approximately 5‐times stronger to homologousFpCSF259‐93 LPS than to LPS from a strain with a different R‐group gene. A conformational epitope for mAb FL100A binding was suggested from molecular dynamic simulations of each O‐PS. Thus,FpCSF259‐93 O‐PS formed a stable well‐defined compact helix in which the R1groups were displayed in a regular pattern on the helix exterior while unreactiveFp950106‐1/1 O‐PS adopted a flexible extended linear conformation. Taken together, the findings establish the specificity of mAb FL100A for Wzy2‐linkedF. psychrophilumO‐PS and LPS.
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- Award ID(s):
- 1933525
- PAR ID:
- 10512194
- Publisher / Repository:
- Wiley-Blackwell
- Date Published:
- Journal Name:
- Journal of Fish Diseases
- ISSN:
- 0140-7775
- Format(s):
- Medium: X
- Sponsoring Org:
- National Science Foundation
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