Source:http://linkedlifedata.com/resource/pubmed/id/11535603
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
46
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pubmed:dateCreated |
2001-11-12
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pubmed:abstractText |
Lipid A of Salmonella typhimurium can be resolved into multiple molecular species. Many of these substances are more polar than the predominant hexa-acylated lipid A 1,4'-bisphosphate of Escherichia coli K-12. By using new isolation methods, we have purified six lipid A subtypes (St1 to St6) from wild type S. typhimurium. We demonstrate that these lipid A variants are covalently modified with one or two 4-amino-4-deoxy-l-arabinose (l-Ara4N) moieties. Each lipid A species with a defined set of polar modifications can be further derivatized with a palmitoyl moiety and/or a 2-hydroxymyristoyl residue in place of the secondary myristoyl chain at position 3'. The unexpected finding that St5 and St6 contain two l-Ara4N residues accounts for the anomalous structures of lipid A precursors seen in S. typhimurium mutants defective in 3-deoxy-d-manno-octulosonic acid biosynthesis in which only the 1-phosphate group is modified with the l-Ara4N moiety (Strain, S. M., Armitage, I. M., Anderson, L., Takayama, K., Quershi, N., and Raetz, C. R. H. (1985) J. Biol. Chem. 260, 16089-16098). Phosphoethanolamine (pEtN)-modified lipid A species are much less abundant than l-Ara4N containing forms in wild type S. typhimurium grown in broth but accumulate to high levels when l-Ara4N synthesis is blocked in pmrA(C)pmrE(-) and pmrA(C)pmrF(-) mutants. Purification and analysis of selected compounds demonstrate that one or two pEtN moieties may be present. Our findings show that S. typhimurium contains versatile enzymes capable of modifying both the 1- and 4'-phosphates of lipid A with l-Ara4N and/or pEtN groups. PmrA null mutants of S. typhimurium produce lipid A species without any pEtN or l-Ara4N substituents. However, PmrA is not needed for the incorporation of 2-hydroxymyristate or palmitate.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-amino-4-deoxyarabinose,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Sugars,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ethanolamines,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid A,
http://linkedlifedata.com/resource/pubmed/chemical/Myristic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Palmitic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-hydroxymyristic acid,
http://linkedlifedata.com/resource/pubmed/chemical/phosphorylethanolamine,
http://linkedlifedata.com/resource/pubmed/chemical/pmrA protein, Bacteria
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
43111-21
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11535603-Amino Sugars,
pubmed-meshheading:11535603-Bacterial Proteins,
pubmed-meshheading:11535603-Carbohydrate Sequence,
pubmed-meshheading:11535603-Chromatography,
pubmed-meshheading:11535603-Escherichia coli,
pubmed-meshheading:11535603-Ethanolamines,
pubmed-meshheading:11535603-Hydrolysis,
pubmed-meshheading:11535603-Lipid A,
pubmed-meshheading:11535603-Models, Chemical,
pubmed-meshheading:11535603-Molecular Sequence Data,
pubmed-meshheading:11535603-Mutation,
pubmed-meshheading:11535603-Myristic Acids,
pubmed-meshheading:11535603-Palmitic Acid,
pubmed-meshheading:11535603-Protein Binding,
pubmed-meshheading:11535603-Protein Conformation,
pubmed-meshheading:11535603-Salmonella typhimurium,
pubmed-meshheading:11535603-Spectrometry, Mass, Matrix-Assisted Laser...
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pubmed:year |
2001
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pubmed:articleTitle |
Lipid A modifications in polymyxin-resistant Salmonella typhimurium: PMRA-dependent 4-amino-4-deoxy-L-arabinose, and phosphoethanolamine incorporation.
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pubmed:affiliation |
Department of Biochemistry and the Duke NMR Spectroscopy Center, Duke University Medical Center, Durham, North Carolina 27710, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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