Lipopolysaccharide (LPS) of a new Pantoea agglomerans strain P324 was studied by chemical and biological methods. Mild acid hydrolysis of the LPS resulted in lipid A and O-specific polysaccharide (OPS) fractions. Studies by negative-ion mode HR ESI mass spectrometry showed heterogeneity of the lipid A, the major form being a hexa-acylated derivative containing biphosphorylated GlcN disaccharide, four 14:0 (3-OH), one 18:0, and one 12:0 residues. The following structure of the OPS was elucidated by chemical, NMR and computational methods: →3)-α-L-Rhap-(1→4)-α-D-Glcp-(1→. The P. agglomerans P324 LPS showed medium level of toxic and pyrogenic activities. Structural components of the LPS exhibited varying effects on the activity of Bacillus peptidases. Thus, the OPS and lipid A played a significant role in the hydrolysis of fibrin by Bacillus proteases but did not affect the activity of protease 2 of B. thuringiensis IMV B-7465 and protease 1 of B. thuringiensis IMV B-7324. Hydrolysis of elastin was intensified by core oligosaccharide and lipid A. Hydrolysis of collagen in the presence of the isolated fractions was accompanied by the inhibition of activity as compared to the native LPS.
Pantoea agglomerans, Bacillus peptidases activity, O-specific polysaccharide and lipid A structure
Publication DOI: 10.1134/S0026261721010124Journal NLM ID: 0376652Publisher: Moskva: Izdatelstvo Nauka
Correspondence: tati20@ukr.net
Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Mendeleev University of Chemical Technology of Russia, High Chemical College, 125047, Moscow, Russia, Zabolotny Institute of Microbiology and Virology of the National Academy of Sciences, 03143, Kiev, Ukraine
Methods: 13C NMR, 1H NMR, GLC-MS, NMR-2D, ESI-MS, GLC, mild acid hydrolysis, composition analysis, GPC, statistical analysis, immunization, assay of polymyxin sensitivity, toxicity assays, pyrogenicity assays, GODDESS NMR simulation, Bacillus proteases treatment
Found