Lipopolysaccharides of Herbaspirillum species and their relevance for bacterium–host interactions

The lipopolysaccharides of Herbaspirillum lusitanum P6–12T (HlP6–12T) and H. frisingense GSF30T (HfGSF30T) was isolated by phenol-water extraction from bacterial cells and was characterized using chemical analysis and SDS–PAGE. It was shown that these bacteria produce LPSs that differ in their physi...

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Veröffentlicht in:International journal of biological macromolecules 2024-03, Vol.261 (Pt 1), p.129516-129516, Article 129516
Hauptverfasser: Velichko, Natalya S., Kokoulin, Maxim S., Dmitrenok, Pavel S., Grinev, Vyacheslav S., Kuchur, Polina D., Komissarov, Aleksey S., Fedonenko, Yulia P.
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container_end_page 129516
container_issue Pt 1
container_start_page 129516
container_title International journal of biological macromolecules
container_volume 261
creator Velichko, Natalya S.
Kokoulin, Maxim S.
Dmitrenok, Pavel S.
Grinev, Vyacheslav S.
Kuchur, Polina D.
Komissarov, Aleksey S.
Fedonenko, Yulia P.
description The lipopolysaccharides of Herbaspirillum lusitanum P6–12T (HlP6–12T) and H. frisingense GSF30T (HfGSF30T) was isolated by phenol-water extraction from bacterial cells and was characterized using chemical analysis and SDS–PAGE. It was shown that these bacteria produce LPSs that differ in their physicochemical properties and macromolecular organization. In this paper, the lipid A structure of the HlP6–12T LPS, was characterized through chemical analyses and matrix-assisted laser desorption ionization (MALDI) mass spectrometry. To prove the effect of the size of micelles on their bioavailability, we examined the activity of both LPSs toward the morphology of wheat seedlings. Analysis of the HlP6–12T and HfGSF30T genomes showed no significant differences between the operons that encode proteins involved in the biosynthesis of the lipids A and core oligosaccharides. The difference may be due to the composition of the O-antigen operon. HfGSF30T has two copies of the rfb operon, with the main one divided into two fragments. In contrast, the HlP6–12T genome contains only a single rfb-containing operon, and the other O-antigen operons are not comparable at all. The integrity of O–antigen–related genes may also affect LPS variability of. Specifically, we have observed a hairpin structure in the middle of the O-antigen glycosyltransferase gene, which led to the division of the gene into two fragments, resulting in incorrect protein synthesis and potential abnormalities in O-antigen production.
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It was shown that these bacteria produce LPSs that differ in their physicochemical properties and macromolecular organization. In this paper, the lipid A structure of the HlP6–12T LPS, was characterized through chemical analyses and matrix-assisted laser desorption ionization (MALDI) mass spectrometry. To prove the effect of the size of micelles on their bioavailability, we examined the activity of both LPSs toward the morphology of wheat seedlings. Analysis of the HlP6–12T and HfGSF30T genomes showed no significant differences between the operons that encode proteins involved in the biosynthesis of the lipids A and core oligosaccharides. The difference may be due to the composition of the O-antigen operon. HfGSF30T has two copies of the rfb operon, with the main one divided into two fragments. In contrast, the HlP6–12T genome contains only a single rfb-containing operon, and the other O-antigen operons are not comparable at all. 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The integrity of O–antigen–related genes may also affect LPS variability of. Specifically, we have observed a hairpin structure in the middle of the O-antigen glycosyltransferase gene, which led to the division of the gene into two fragments, resulting in incorrect protein synthesis and potential abnormalities in O-antigen production.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>38278393</pmid><doi>10.1016/j.ijbiomac.2024.129516</doi><tpages>1</tpages></addata></record>
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subjects Antioxidant enzymes
bioavailability
biosynthesis
chemical analysis
desorption
Gas Chromatography-Mass Spectrometry
Herbaspirillum
Herbaspirillum - genetics
Host Microbial Interactions
ionization
Lipid A
Lipopolysaccharide (LPS)
Lipopolysaccharides - chemistry
mass spectrometry
micelles
O Antigens - metabolism
O-antigen genes
O-antigens
oligosaccharides
operon
polyacrylamide gel electrophoresis
protein synthesis
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
wheat
title Lipopolysaccharides of Herbaspirillum species and their relevance for bacterium–host interactions
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