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Peptidoglycan structure of Salmonella typhimurium growing within cultured mammalian cells
The cell wall structure of Salmonella typhimurium has been studied for the first time during transit from free‐living to parasitic lifestyles. Peptidoglycan of S. typhimurium proliferating within human epithelial cells contains a high proportion of previously unidentified muropeptides (5–10‐fold hig...
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Published in: | Molecular microbiology 1997-02, Vol.23 (4), p.693-704 |
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description | The cell wall structure of Salmonella typhimurium has been studied for the first time during transit from free‐living to parasitic lifestyles. Peptidoglycan of S. typhimurium proliferating within human epithelial cells contains a high proportion of previously unidentified muropeptides (5–10‐fold higher than in extracellular bacteria). Amino acid and mass‐spectrometry analyses showed that these new components consist of dimeric cross‐linked muropeptides lacking one of the two disaccharide (N‐acetyl‐glucosamine‐β‐(1→4)‐N‐acetyl‐muramic acid) molecules. This unique structure suggests an active role for an N‐acetyl‐muramyl‐l‐alanine‐amidase in remodelling the peptidoglycan of intracellular S. typhimurium. Additional alterations observed included: (i) the absence of glycine‐containing muropeptides; (ii) the increase in the relative proportion of muropeptides cross‐linked by l(meso)‐diaminopimelyl‐d(meso)‐diaminopimelic acid (l–d) peptide bridges; and, (iii) the decrease in the global cross‐linkage of the macromolecule. The structural alterations observed in the peptidoglycan of intracellular bacteria do not produce loss of the cell envelope. These results show that intracellular residence of S. typhimurium within epithelial cells is accompanied by significant changes in the bacterial cell wall. Remodelling of peptidoglycan structure may constitute another sophisticated strategy of this pathogen for adapting to and colonizing the intracellular niche of eukaryotic cells. |
doi_str_mv | 10.1046/j.1365-2958.1997.2561621.x |
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Peptidoglycan of S. typhimurium proliferating within human epithelial cells contains a high proportion of previously unidentified muropeptides (5–10‐fold higher than in extracellular bacteria). Amino acid and mass‐spectrometry analyses showed that these new components consist of dimeric cross‐linked muropeptides lacking one of the two disaccharide (N‐acetyl‐glucosamine‐β‐(1→4)‐N‐acetyl‐muramic acid) molecules. This unique structure suggests an active role for an N‐acetyl‐muramyl‐l‐alanine‐amidase in remodelling the peptidoglycan of intracellular S. typhimurium. Additional alterations observed included: (i) the absence of glycine‐containing muropeptides; (ii) the increase in the relative proportion of muropeptides cross‐linked by l(meso)‐diaminopimelyl‐d(meso)‐diaminopimelic acid (l–d) peptide bridges; and, (iii) the decrease in the global cross‐linkage of the macromolecule. The structural alterations observed in the peptidoglycan of intracellular bacteria do not produce loss of the cell envelope. These results show that intracellular residence of S. typhimurium within epithelial cells is accompanied by significant changes in the bacterial cell wall. Remodelling of peptidoglycan structure may constitute another sophisticated strategy of this pathogen for adapting to and colonizing the intracellular niche of eukaryotic cells.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1046/j.1365-2958.1997.2561621.x</identifier><identifier>PMID: 9157241</identifier><language>eng</language><publisher>Oxford BSL: Blackwell Science Ltd</publisher><subject>Carbohydrate Conformation ; Carbohydrate Sequence ; Cell Wall - chemistry ; Chromatography, High Pressure Liquid ; HeLa Cells ; Humans ; Molecular Sequence Data ; Molecular Structure ; Peptidoglycan - chemistry ; Salmonella typhimurium - chemistry ; Salmonella typhimurium - growth & development ; Salmonella typhimurium - pathogenicity ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><ispartof>Molecular microbiology, 1997-02, Vol.23 (4), p.693-704</ispartof><rights>Blackwell Science Ltd, Oxford</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4876-a63cde66bdfab1929a5b3e53d630a42d55882cc99d4187a0d8f27025cbf973723</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9157241$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Quintela, José Carlos</creatorcontrib><creatorcontrib>De Pedro, Miguel A.</creatorcontrib><creatorcontrib>Zo¨llner, Peter</creatorcontrib><creatorcontrib>Allmaier, Gu¨nter</creatorcontrib><creatorcontrib>Garcia‐del Portillo, Francisco</creatorcontrib><title>Peptidoglycan structure of Salmonella typhimurium growing within cultured mammalian cells</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>The cell wall structure of Salmonella typhimurium has been studied for the first time during transit from free‐living to parasitic lifestyles. Peptidoglycan of S. typhimurium proliferating within human epithelial cells contains a high proportion of previously unidentified muropeptides (5–10‐fold higher than in extracellular bacteria). Amino acid and mass‐spectrometry analyses showed that these new components consist of dimeric cross‐linked muropeptides lacking one of the two disaccharide (N‐acetyl‐glucosamine‐β‐(1→4)‐N‐acetyl‐muramic acid) molecules. This unique structure suggests an active role for an N‐acetyl‐muramyl‐l‐alanine‐amidase in remodelling the peptidoglycan of intracellular S. typhimurium. Additional alterations observed included: (i) the absence of glycine‐containing muropeptides; (ii) the increase in the relative proportion of muropeptides cross‐linked by l(meso)‐diaminopimelyl‐d(meso)‐diaminopimelic acid (l–d) peptide bridges; and, (iii) the decrease in the global cross‐linkage of the macromolecule. The structural alterations observed in the peptidoglycan of intracellular bacteria do not produce loss of the cell envelope. These results show that intracellular residence of S. typhimurium within epithelial cells is accompanied by significant changes in the bacterial cell wall. Remodelling of peptidoglycan structure may constitute another sophisticated strategy of this pathogen for adapting to and colonizing the intracellular niche of eukaryotic cells.</description><subject>Carbohydrate Conformation</subject><subject>Carbohydrate Sequence</subject><subject>Cell Wall - chemistry</subject><subject>Chromatography, High Pressure Liquid</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Molecular Structure</subject><subject>Peptidoglycan - chemistry</subject><subject>Salmonella typhimurium - chemistry</subject><subject>Salmonella typhimurium - growth & development</subject><subject>Salmonella typhimurium - pathogenicity</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><recordid>eNqVkEtL9DAUhoMofuPlJwjFhbvWXJrbtxBEvIGioIKuQpqkY4amHZOWcf69LTO4d3U4vJdzeAA4RbBAsGTniwIRRnMsqSiQlLzAlCGGUfG9A2a_0i6YQUlhTgR-_wcOUlpAiAhkZB_sS0Q5LtEMfDy7Ze9tN2_WRrdZ6uNg-iG6rKuzF92ErnVNo7N-vfz0YYh-CNk8divfzrOV7z99m5mhmQI2CzoE3fixxYyZdAT2at0kd7ydh-Dt5vr16i5_eLq9v7p8yE0pOMs1I8Y6xipb6wpJLDWtiKPEMgJ1iS2lQmBjpLQlElxDK2rMIaamqiUnHJNDcLbpXcbua3CpV8Gn6QPdum5IigvBS87RaPy_MZrYpRRdrZbRBx3XCkE1cVULNcFTEzw1cVVbrup7DJ9srwxVcPY3ugU56hcbfeUbt_5Ds3p8vB8X8gMjZ4lM</recordid><startdate>199702</startdate><enddate>199702</enddate><creator>Quintela, José Carlos</creator><creator>De Pedro, Miguel A.</creator><creator>Zo¨llner, Peter</creator><creator>Allmaier, Gu¨nter</creator><creator>Garcia‐del Portillo, Francisco</creator><general>Blackwell Science Ltd</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></search><sort><creationdate>199702</creationdate><title>Peptidoglycan structure of Salmonella typhimurium growing within cultured mammalian cells</title><author>Quintela, José Carlos ; De Pedro, Miguel A. ; Zo¨llner, Peter ; Allmaier, Gu¨nter ; Garcia‐del Portillo, Francisco</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4876-a63cde66bdfab1929a5b3e53d630a42d55882cc99d4187a0d8f27025cbf973723</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Carbohydrate Conformation</topic><topic>Carbohydrate Sequence</topic><topic>Cell Wall - chemistry</topic><topic>Chromatography, High Pressure Liquid</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Molecular Structure</topic><topic>Peptidoglycan - chemistry</topic><topic>Salmonella typhimurium - chemistry</topic><topic>Salmonella typhimurium - growth & development</topic><topic>Salmonella typhimurium - pathogenicity</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Quintela, José Carlos</creatorcontrib><creatorcontrib>De Pedro, Miguel A.</creatorcontrib><creatorcontrib>Zo¨llner, Peter</creatorcontrib><creatorcontrib>Allmaier, Gu¨nter</creatorcontrib><creatorcontrib>Garcia‐del Portillo, Francisco</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><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Quintela, José Carlos</au><au>De Pedro, Miguel A.</au><au>Zo¨llner, Peter</au><au>Allmaier, Gu¨nter</au><au>Garcia‐del Portillo, Francisco</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Peptidoglycan structure of Salmonella typhimurium growing within cultured mammalian cells</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>1997-02</date><risdate>1997</risdate><volume>23</volume><issue>4</issue><spage>693</spage><epage>704</epage><pages>693-704</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>The cell wall structure of Salmonella typhimurium has been studied for the first time during transit from free‐living to parasitic lifestyles. Peptidoglycan of S. typhimurium proliferating within human epithelial cells contains a high proportion of previously unidentified muropeptides (5–10‐fold higher than in extracellular bacteria). Amino acid and mass‐spectrometry analyses showed that these new components consist of dimeric cross‐linked muropeptides lacking one of the two disaccharide (N‐acetyl‐glucosamine‐β‐(1→4)‐N‐acetyl‐muramic acid) molecules. This unique structure suggests an active role for an N‐acetyl‐muramyl‐l‐alanine‐amidase in remodelling the peptidoglycan of intracellular S. typhimurium. Additional alterations observed included: (i) the absence of glycine‐containing muropeptides; (ii) the increase in the relative proportion of muropeptides cross‐linked by l(meso)‐diaminopimelyl‐d(meso)‐diaminopimelic acid (l–d) peptide bridges; and, (iii) the decrease in the global cross‐linkage of the macromolecule. The structural alterations observed in the peptidoglycan of intracellular bacteria do not produce loss of the cell envelope. These results show that intracellular residence of S. typhimurium within epithelial cells is accompanied by significant changes in the bacterial cell wall. Remodelling of peptidoglycan structure may constitute another sophisticated strategy of this pathogen for adapting to and colonizing the intracellular niche of eukaryotic cells.</abstract><cop>Oxford BSL</cop><pub>Blackwell Science Ltd</pub><pmid>9157241</pmid><doi>10.1046/j.1365-2958.1997.2561621.x</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Carbohydrate Conformation Carbohydrate Sequence Cell Wall - chemistry Chromatography, High Pressure Liquid HeLa Cells Humans Molecular Sequence Data Molecular Structure Peptidoglycan - chemistry Salmonella typhimurium - chemistry Salmonella typhimurium - growth & development Salmonella typhimurium - pathogenicity Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
title | Peptidoglycan structure of Salmonella typhimurium growing within cultured mammalian cells |
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