Disease relevance of chitotriose

• Because a chitinase had not been previously reported in Legionella, we determined that wild type secretes activity against both p-nitrophenyl triacetyl chitotriose and glycol chitin [1].
• The specificity of the interaction between OmpA and GlcNAc beta 1-4GlcNAc epitopes was verified by the demonstration that chitotriose-bound OmpA and wheat germ agglutinin-bound brain microvascular endothelial cell membrane proteins inhibit E. coli K1 invasion [2].
• Chitosanase from the culture filtrate of Nocardia orientalis was purified to apparent homogeneity by precipitation with ammonium sulfate followed by CM-Sephadex chromatography, biospecific affinity chromatography on a Sepharose CL-4B with immobilized chitotriose and by gel filtration on Sephadex G-75 [3].

High impact information on chitotriose

• Heat-inactivated SaG as well as SaG treated with both polyclonal and monoclonal specific antibodies or enzyme inhibitors such as chitotriose or hydrolyzed peptidoglycan had no effect on lymphocyte response to mitogens [4].
• The gene product hydrolyzes methylumbelliferyl beta-D conjugates of chitotriose, chitobiose, N-acetylglucosamine, and N-acetylgalactosamine and has, therefore, been termed a beta-N-acetylhexosaminidase [5].
• However, the binding site of AVR4 is larger than that of Hevein, i.e. AVR4 interacts strictly with chitotriose, whereas Hevein can also interact with the monomer N-acetylglucosamine [6].
• The absence of this domain does not affect the ability of the enzyme to hydrolyze the soluble substrate, triacetylchitotriose, but abolishes hydrolysis of insoluble chitin [7].
• The protein binds specifically to tri-N-acetyl chitotriose and reacetylated chitosan in vitro [8].

Biological context of chitotriose

• Differences in the binding of the substrate analogue chitotriose to lysozymes correlate with amino acid substitutions in the binding site and not with substitutions elsewhere [9].
• Kinetic studies showed that ChiB followed Michaelis-Menten kinetics toward chitotriose, although substrate inhibition was observed for larger chitooligomers [10].
• Also, chitopentaose, chitotetraose, chitotriose, and chitobiose were able to induce cortical cell divisions and cell expansion in a radial direction in transgenic roots, but not in control roots [11].
• The absolute oral bioavailability of chitobiose was higher than that of chitotriose at all doses (30, 100, and 300 mg/kg) examined [12].

Anatomical context of chitotriose

• Epithelial cell surfaces bound fluoresceinated pokeweed mitogen, indicating the constitutive presence of LAG-bearing molecules at the cell surface; pokeweed mitogen binding to the cell surface was completely blocked by 10 mM chitotriose [13].
• The 220-kDa protein agglutinates human erythrocytes, and agglutination is inhibited by micromolar concentrations of hyaluronic acid, chitin, chitin-derived products (chitotriose), and antibodies to the purified protein [14].
• All interactions were specifically inhibited by low concentrations of chitotriose (GlcNAcbeta1 leads to 4GlcNAcbeta1 leads to 4GlcNAc) and the bacterial cell wall tetrasaccharide, GlcNAcbeta1 leads to 4MurNAcbeta1 leads to 4GlcNAcbeta1 leads to 4MurNAc [15].
• In a 4 h biological assay concentration dependent partial inhibition of neurite growth on laminin was observed in the presence of (i) alpha-lactalbumin, a specific inhibitor of the enzyme, (ii) N-acetylglucosamine (GlcNac), the appropriate acceptor substrate, or its polymer chitotriose, and (iii) UDPgal, the catalytic substrate [16].
• This study indicates that among various chitooligosaccharides, only chitobiose and chitotriose can be appreciably absorbed from the gastrointestinal tract [12].

Associations of chitotriose with other chemical compounds

• These latter results suggested that the essential bactericidal property of lysozyme was its extreme cationic nature and that some bacterial endogenous activities, inhibitable by chitotriose and chitobiose, were essential for expression of the bactericidal activity of either native or muramidase-inactive lysozyme or of the cationic homopolypeptides [17].
• Inactivation of the muramidase activity of lysozyme was achieved by reduction of essential disulfides with dithiothreitol (DTT) or by incubation with the chitin oligosaccharides chitotriose and chitobiose [17].
• We further localize its binding site to a variant of the chitotriose structure in the tri-mannosyl core of the membrane glycoprotein [18].
• Chitobiose and chitotriose were more potent than the 3 reference compounds in scavenging hydroxyl radicals produced by photolysis of zinc oxide: IC(50) values of the 2 oligomers were 30 and 55 microM, respectively [19].

Gene context of chitotriose

• With the wild-type h-beta4Gal-T1, the K(m) of 1,2-1,6-arm is approximately tenfold lower than for 1,2-1,3-arm and 1,4-1,3-arm, and 22-fold lower than for chitotriose [20].
• The Mr = 92,000 protein bound to wheat germ agglutinin-agarose was not eluted by N-acetylglucosamine but was by triacetylchitotriose, providing a considerable purification of the somatostatin receptor [21].
• The solution-state conformations of N,N',N"-triacetyl chitotriose (1) and other potential chitinase inhibitors 2-4 were studied using a combination of NMR spectroscopy (NOESY) and molecular mechanics calculations [22].
• Antioxidant activities of chitobiose and chitotriose [19].

Analytical, diagnostic and therapeutic context of chitotriose

• HPLC analysis indicated that during the hydrolysis of chitotriose, both chitinases initially produce N-acetylglucosamine and only one anomer of chitobiose [23].
• Inhibition of Caco-2 binding of WGA-functionalized microspheres by chitotriose indicated for specificity of the interaction [24].

References