Lipopolysaccharide Structure and Biosynthesis in Helicobacter pylori
This review covers the current knowledge and gaps in Helicobacter pylori lipopolysaccharide (LPS) structure and biosynthesis. H. pylori is a Gram‐negative bacterium which colonizes the luminal surface of the human gastric epithelium. Both a constitutive alteration of the lipid A preventing TLR4 elic...
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Veröffentlicht in: | Helicobacter (Cambridge, Mass.) Mass.), 2016-12, Vol.21 (6), p.445-461 |
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description | This review covers the current knowledge and gaps in Helicobacter pylori lipopolysaccharide (LPS) structure and biosynthesis. H. pylori is a Gram‐negative bacterium which colonizes the luminal surface of the human gastric epithelium. Both a constitutive alteration of the lipid A preventing TLR4 elicitation and host mimicry of the Lewis antigen decorated O‐antigen of H. pylori LPS promote immune escape and chronic infection. To date, the complete structure of H. pylori LPS is not available, and the proposed model is a linear arrangement composed of the inner core defined as the hexa‐saccharide (Kdo‐LD‐Hep‐LD‐Hep‐DD‐Hep‐Gal‐Glc), the outer core composed of a conserved trisaccharide (‐GlcNAc‐Fuc‐DD‐Hep‐) linked to the third heptose of the inner core, the glucan, the heptan and a variable O‐antigen, generally consisting of a poly‐LacNAc decorated with Lewis antigens. Although the glycosyltransferases (GTs) responsible for the biosynthesis of the H. pylori O‐antigen chains have been identified and characterized, there are many gaps in regard to the biosynthesis of the core LPS. These limitations warrant additional mutagenesis and structural studies to obtain the complete LPS structure and corresponding biosynthetic pathway of this important gastric bacterium. |
doi_str_mv | 10.1111/hel.12301 |
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H. pylori is a Gram‐negative bacterium which colonizes the luminal surface of the human gastric epithelium. Both a constitutive alteration of the lipid A preventing TLR4 elicitation and host mimicry of the Lewis antigen decorated O‐antigen of H. pylori LPS promote immune escape and chronic infection. To date, the complete structure of H. pylori LPS is not available, and the proposed model is a linear arrangement composed of the inner core defined as the hexa‐saccharide (Kdo‐LD‐Hep‐LD‐Hep‐DD‐Hep‐Gal‐Glc), the outer core composed of a conserved trisaccharide (‐GlcNAc‐Fuc‐DD‐Hep‐) linked to the third heptose of the inner core, the glucan, the heptan and a variable O‐antigen, generally consisting of a poly‐LacNAc decorated with Lewis antigens. Although the glycosyltransferases (GTs) responsible for the biosynthesis of the H. pylori O‐antigen chains have been identified and characterized, there are many gaps in regard to the biosynthesis of the core LPS. These limitations warrant additional mutagenesis and structural studies to obtain the complete LPS structure and corresponding biosynthetic pathway of this important gastric bacterium.</description><identifier>ISSN: 1083-4389</identifier><identifier>EISSN: 1523-5378</identifier><identifier>DOI: 10.1111/hel.12301</identifier><identifier>PMID: 26934862</identifier><language>eng</language><publisher>England: Blackwell Publishing Ltd</publisher><subject>Antigens ; Biosynthesis ; Glycosyltransferases - metabolism ; Helicobacter pylori ; Helicobacter pylori - enzymology ; Helicobacter pylori - immunology ; Helicobacter pylori - physiology ; Humans ; Immune Evasion ; lipopolysaccharide ; Lipopolysaccharides - chemistry ; Lipopolysaccharides - immunology ; Metabolic Networks and Pathways ; structure</subject><ispartof>Helicobacter (Cambridge, Mass.), 2016-12, Vol.21 (6), p.445-461</ispartof><rights>2016 John Wiley & Sons Ltd</rights><rights>2016 John Wiley & Sons Ltd.</rights><rights>Copyright © 2016 John Wiley & Sons Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fhel.12301$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fhel.12301$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26934862$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Hong</creatorcontrib><creatorcontrib>Liao, Tingting</creatorcontrib><creatorcontrib>Debowski, Aleksandra W.</creatorcontrib><creatorcontrib>Tang, Hong</creatorcontrib><creatorcontrib>Nilsson, Hans-Olof</creatorcontrib><creatorcontrib>Stubbs, Keith A.</creatorcontrib><creatorcontrib>Marshall, Barry J.</creatorcontrib><creatorcontrib>Benghezal, Mohammed</creatorcontrib><title>Lipopolysaccharide Structure and Biosynthesis in Helicobacter pylori</title><title>Helicobacter (Cambridge, Mass.)</title><addtitle>Helicobacter</addtitle><description>This review covers the current knowledge and gaps in Helicobacter pylori lipopolysaccharide (LPS) structure and biosynthesis. H. pylori is a Gram‐negative bacterium which colonizes the luminal surface of the human gastric epithelium. Both a constitutive alteration of the lipid A preventing TLR4 elicitation and host mimicry of the Lewis antigen decorated O‐antigen of H. pylori LPS promote immune escape and chronic infection. To date, the complete structure of H. pylori LPS is not available, and the proposed model is a linear arrangement composed of the inner core defined as the hexa‐saccharide (Kdo‐LD‐Hep‐LD‐Hep‐DD‐Hep‐Gal‐Glc), the outer core composed of a conserved trisaccharide (‐GlcNAc‐Fuc‐DD‐Hep‐) linked to the third heptose of the inner core, the glucan, the heptan and a variable O‐antigen, generally consisting of a poly‐LacNAc decorated with Lewis antigens. Although the glycosyltransferases (GTs) responsible for the biosynthesis of the H. pylori O‐antigen chains have been identified and characterized, there are many gaps in regard to the biosynthesis of the core LPS. These limitations warrant additional mutagenesis and structural studies to obtain the complete LPS structure and corresponding biosynthetic pathway of this important gastric bacterium.</description><subject>Antigens</subject><subject>Biosynthesis</subject><subject>Glycosyltransferases - metabolism</subject><subject>Helicobacter pylori</subject><subject>Helicobacter pylori - enzymology</subject><subject>Helicobacter pylori - immunology</subject><subject>Helicobacter pylori - physiology</subject><subject>Humans</subject><subject>Immune Evasion</subject><subject>lipopolysaccharide</subject><subject>Lipopolysaccharides - chemistry</subject><subject>Lipopolysaccharides - immunology</subject><subject>Metabolic Networks and Pathways</subject><subject>structure</subject><issn>1083-4389</issn><issn>1523-5378</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkE1LxDAQhoMoun4c_ANS8OKlbqZJmuTo51ZYVFDRW0jbLJu129akRfvvje66B-cyA_O8w_AgdAz4HEKN56Y6h4Rg2EIjYAmJGeFiO8xYkJgSIffQvvcLjDEjVO6ivSSVhIo0GaHrqW2btqkGr4tirp0tTfTUub7oemciXZfRpW38UHdz462PbB1lprJFk-uiMy5qh6px9hDtzHTlzdG6H6CX25vnqyyePkzuri6msaUMIC5LDtjkMJPaYC0KzmekTFOBpZBEcp2WXONZAoTIHBJDaAlCCwKMaYkpluQAna3utq756I3v1NL6wlSVrk3TewWCYS6ThEJAT_-hi6Z3dfguUJRKFmyJQJ2sqT5fmlK1zi61G9SfnwCMV8Cnrcyw2QNWP-JVEK9-xavsZvo7hES8Sljfma9NQrt3lXLCmXq9nyj5xiF7fH5SlHwDfU6CdA</recordid><startdate>201612</startdate><enddate>201612</enddate><creator>Li, Hong</creator><creator>Liao, Tingting</creator><creator>Debowski, Aleksandra W.</creator><creator>Tang, Hong</creator><creator>Nilsson, Hans-Olof</creator><creator>Stubbs, Keith A.</creator><creator>Marshall, Barry J.</creator><creator>Benghezal, Mohammed</creator><general>Blackwell Publishing Ltd</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>C1K</scope><scope>K9.</scope></search><sort><creationdate>201612</creationdate><title>Lipopolysaccharide Structure and Biosynthesis in Helicobacter pylori</title><author>Li, Hong ; Liao, Tingting ; Debowski, Aleksandra W. ; Tang, Hong ; Nilsson, Hans-Olof ; Stubbs, Keith A. ; Marshall, Barry J. ; Benghezal, Mohammed</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i4511-dd710eb1f9ae0a8c77f3d6680989397a6d7a0f21339b12e34d18a83155a904093</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Antigens</topic><topic>Biosynthesis</topic><topic>Glycosyltransferases - metabolism</topic><topic>Helicobacter pylori</topic><topic>Helicobacter pylori - enzymology</topic><topic>Helicobacter pylori - immunology</topic><topic>Helicobacter pylori - physiology</topic><topic>Humans</topic><topic>Immune Evasion</topic><topic>lipopolysaccharide</topic><topic>Lipopolysaccharides - chemistry</topic><topic>Lipopolysaccharides - immunology</topic><topic>Metabolic Networks and Pathways</topic><topic>structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Hong</creatorcontrib><creatorcontrib>Liao, Tingting</creatorcontrib><creatorcontrib>Debowski, Aleksandra W.</creatorcontrib><creatorcontrib>Tang, Hong</creatorcontrib><creatorcontrib>Nilsson, Hans-Olof</creatorcontrib><creatorcontrib>Stubbs, Keith A.</creatorcontrib><creatorcontrib>Marshall, Barry J.</creatorcontrib><creatorcontrib>Benghezal, Mohammed</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><jtitle>Helicobacter (Cambridge, Mass.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Hong</au><au>Liao, Tingting</au><au>Debowski, Aleksandra W.</au><au>Tang, Hong</au><au>Nilsson, Hans-Olof</au><au>Stubbs, Keith A.</au><au>Marshall, Barry J.</au><au>Benghezal, Mohammed</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Lipopolysaccharide Structure and Biosynthesis in Helicobacter pylori</atitle><jtitle>Helicobacter (Cambridge, Mass.)</jtitle><addtitle>Helicobacter</addtitle><date>2016-12</date><risdate>2016</risdate><volume>21</volume><issue>6</issue><spage>445</spage><epage>461</epage><pages>445-461</pages><issn>1083-4389</issn><eissn>1523-5378</eissn><abstract>This review covers the current knowledge and gaps in Helicobacter pylori lipopolysaccharide (LPS) structure and biosynthesis. H. pylori is a Gram‐negative bacterium which colonizes the luminal surface of the human gastric epithelium. Both a constitutive alteration of the lipid A preventing TLR4 elicitation and host mimicry of the Lewis antigen decorated O‐antigen of H. pylori LPS promote immune escape and chronic infection. To date, the complete structure of H. pylori LPS is not available, and the proposed model is a linear arrangement composed of the inner core defined as the hexa‐saccharide (Kdo‐LD‐Hep‐LD‐Hep‐DD‐Hep‐Gal‐Glc), the outer core composed of a conserved trisaccharide (‐GlcNAc‐Fuc‐DD‐Hep‐) linked to the third heptose of the inner core, the glucan, the heptan and a variable O‐antigen, generally consisting of a poly‐LacNAc decorated with Lewis antigens. Although the glycosyltransferases (GTs) responsible for the biosynthesis of the H. pylori O‐antigen chains have been identified and characterized, there are many gaps in regard to the biosynthesis of the core LPS. These limitations warrant additional mutagenesis and structural studies to obtain the complete LPS structure and corresponding biosynthetic pathway of this important gastric bacterium.</abstract><cop>England</cop><pub>Blackwell Publishing Ltd</pub><pmid>26934862</pmid><doi>10.1111/hel.12301</doi><tpages>17</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Antigens Biosynthesis Glycosyltransferases - metabolism Helicobacter pylori Helicobacter pylori - enzymology Helicobacter pylori - immunology Helicobacter pylori - physiology Humans Immune Evasion lipopolysaccharide Lipopolysaccharides - chemistry Lipopolysaccharides - immunology Metabolic Networks and Pathways structure |
title | Lipopolysaccharide Structure and Biosynthesis in Helicobacter pylori |
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