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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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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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.</description><identifier>ISSN: 0141-8130</identifier><identifier>EISSN: 1879-0003</identifier><identifier>DOI: 10.1016/j.ijbiomac.2024.129516</identifier><identifier>PMID: 38278393</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>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</subject><ispartof>International journal of biological macromolecules, 2024-03, Vol.261 (Pt 1), p.129516-129516, Article 129516</ispartof><rights>2024 Elsevier B.V.</rights><rights>Copyright © 2024 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c348t-257b3e2993452e0d51a035d9d507dd2cb498b6ffebf964ef671bfe610279068c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ijbiomac.2024.129516$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3541,27915,27916,45986</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38278393$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Velichko, Natalya S.</creatorcontrib><creatorcontrib>Kokoulin, Maxim S.</creatorcontrib><creatorcontrib>Dmitrenok, Pavel S.</creatorcontrib><creatorcontrib>Grinev, Vyacheslav S.</creatorcontrib><creatorcontrib>Kuchur, Polina D.</creatorcontrib><creatorcontrib>Komissarov, Aleksey S.</creatorcontrib><creatorcontrib>Fedonenko, Yulia P.</creatorcontrib><title>Lipopolysaccharides of Herbaspirillum species and their relevance for bacterium–host interactions</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><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.</description><subject>Antioxidant enzymes</subject><subject>bioavailability</subject><subject>biosynthesis</subject><subject>chemical analysis</subject><subject>desorption</subject><subject>Gas Chromatography-Mass Spectrometry</subject><subject>Herbaspirillum</subject><subject>Herbaspirillum - genetics</subject><subject>Host Microbial Interactions</subject><subject>ionization</subject><subject>Lipid A</subject><subject>Lipopolysaccharide (LPS)</subject><subject>Lipopolysaccharides - chemistry</subject><subject>mass spectrometry</subject><subject>micelles</subject><subject>O Antigens - metabolism</subject><subject>O-antigen genes</subject><subject>O-antigens</subject><subject>oligosaccharides</subject><subject>operon</subject><subject>polyacrylamide gel electrophoresis</subject><subject>protein synthesis</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>wheat</subject><issn>0141-8130</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1q3DAQx0VpaTZpXyH4mIu3-rBk6ZYQmqSwkEt7FvoYsVpsy5XsQG55h75hn6RaNuk1p0Gj38zA74_QJcFbgon4dtjGg41pNG5LMe22hCpOxAe0IbJXLcaYfUQbTDrSSsLwGTov5VC7ghP5GZ0xSXvJFNsgt4tzmtPwXIxze5Ojh9Kk0DxAtqbMMcdhWMemzOBi_TGTb5Y9xNxkGODJTA6akHJjjVsgx3X8-_Jnn8rSxKm-azOmqXxBn4IZCnx9rRfo1933n7cP7e7x_sftza51rJNLS3lvGVClWMcpYM-JwYx75TnuvafOdkpaEQLYoEQHQfTEBhAE015hIR27QFenvXNOv1coix5jcTAMZoK0Fs0IZ1ywnsl3Uaoo5n11SSoqTqjLqZQMQc85jiY_a4L1MQt90G9Z6GMW-pRFHbx8vbHaEfz_sTf5Fbg-AVClPEXIulTJVamPGdyifYrv3fgHvBCgQA</recordid><startdate>202403</startdate><enddate>202403</enddate><creator>Velichko, Natalya S.</creator><creator>Kokoulin, Maxim S.</creator><creator>Dmitrenok, Pavel S.</creator><creator>Grinev, Vyacheslav S.</creator><creator>Kuchur, Polina D.</creator><creator>Komissarov, Aleksey S.</creator><creator>Fedonenko, Yulia P.</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope></search><sort><creationdate>202403</creationdate><title>Lipopolysaccharides of Herbaspirillum species and their relevance for bacterium–host interactions</title><author>Velichko, Natalya S. ; Kokoulin, Maxim S. ; Dmitrenok, Pavel S. ; Grinev, Vyacheslav S. ; Kuchur, Polina D. ; Komissarov, Aleksey S. ; Fedonenko, Yulia P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c348t-257b3e2993452e0d51a035d9d507dd2cb498b6ffebf964ef671bfe610279068c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Antioxidant enzymes</topic><topic>bioavailability</topic><topic>biosynthesis</topic><topic>chemical analysis</topic><topic>desorption</topic><topic>Gas Chromatography-Mass Spectrometry</topic><topic>Herbaspirillum</topic><topic>Herbaspirillum - genetics</topic><topic>Host Microbial Interactions</topic><topic>ionization</topic><topic>Lipid A</topic><topic>Lipopolysaccharide (LPS)</topic><topic>Lipopolysaccharides - chemistry</topic><topic>mass spectrometry</topic><topic>micelles</topic><topic>O Antigens - metabolism</topic><topic>O-antigen genes</topic><topic>O-antigens</topic><topic>oligosaccharides</topic><topic>operon</topic><topic>polyacrylamide gel electrophoresis</topic><topic>protein synthesis</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>wheat</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Velichko, Natalya S.</creatorcontrib><creatorcontrib>Kokoulin, Maxim S.</creatorcontrib><creatorcontrib>Dmitrenok, Pavel S.</creatorcontrib><creatorcontrib>Grinev, Vyacheslav S.</creatorcontrib><creatorcontrib>Kuchur, Polina D.</creatorcontrib><creatorcontrib>Komissarov, Aleksey S.</creatorcontrib><creatorcontrib>Fedonenko, Yulia P.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><jtitle>International journal of biological macromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Velichko, Natalya S.</au><au>Kokoulin, Maxim S.</au><au>Dmitrenok, Pavel S.</au><au>Grinev, Vyacheslav S.</au><au>Kuchur, Polina D.</au><au>Komissarov, Aleksey S.</au><au>Fedonenko, Yulia P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Lipopolysaccharides of Herbaspirillum species and their relevance for bacterium–host interactions</atitle><jtitle>International journal of biological macromolecules</jtitle><addtitle>Int J Biol Macromol</addtitle><date>2024-03</date><risdate>2024</risdate><volume>261</volume><issue>Pt 1</issue><spage>129516</spage><epage>129516</epage><pages>129516-129516</pages><artnum>129516</artnum><issn>0141-8130</issn><eissn>1879-0003</eissn><abstract>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.</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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