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Functional analysis of a lipid galactosyltransferase synthesizing the major envelope lipid in the Lyme disease spirochete Borrelia burgdorferi.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2007 (English)In: FEMS Microbiol Lett, ISSN 0378-1097, Vol. 272, no 1, 22-9 p.Article in journal (Other academic) Published
Abstract [en]

One of the major lipids in the membranes of Borrelia burgdorferi is

monogalactosyl diacylglycerol (MGalDAG), a glycolipid recently shown to carry

antigenic potency. Herein, it is shown that the gene mgs (TIGR designation

bb0454) of B. burgdorferi encodes for the protein bbMGS that, when expressed in

Escherichia coli, catalyzes the glycosylation of 1,2-diacylglycerol with

specificity for the donor substrate UDP-Gal yielding MGalDAG. Related lipid

enzymes were found in many Gram-positive bacteria. The presence of this

galactosyltransferase activity and synthesis of a cholesteryl galactoside by

another enzyme were verified in B. burgdorferi cell extract. Besides MGalDAG,

phosphatidylcholine, phosphatidylglycerol, and cholesterol were also found as

major lipids in the cell envelope. The high isoelectric point of bbMGS and

clustered basic residues in its amino acid sequence suggest that the enzyme

interacts with acidic lipids in the plasma membrane, in agreement with strong

enzymatic activation of bbMGS by phosphatidylglycerol. The membrane packing and

immunological properties of MGalDAG are likely to be of great importance in vivo.

Place, publisher, year, edition, pages
2007. Vol. 272, no 1, 22-9 p.
Keyword [en]
Bacterial Proteins/genetics/*metabolism, Borrelia burgdorferi/*enzymology/genetics, Cell Membrane/chemistry, Cholesterol/analysis/isolation & purification, Cloning; Molecular, Diglycerides/*biosynthesis/metabolism, Enzyme Activators/analysis/isolation & purification/pharmacology, Escherichia coli/genetics/metabolism, Galactolipids/*metabolism, Galactosyltransferases/genetics/*metabolism, Genes; Bacterial, Isoelectric Point, Lipid Metabolism, Membrane Lipids/*biosynthesis, Phosphatidylcholines/analysis/isolation & purification, Phosphatidylglycerols/analysis/isolation & purification/pharmacology, Recombinant Proteins/genetics/metabolism, Sequence Analysis; Protein, Transcription; Genetic, Uridine Diphosphate Galactose/metabolism
URN: urn:nbn:se:su:diva-12062ISI: 000247317000004PubMedID: 17456185OAI: diva2:178582
Available from: 2008-01-15 Created: 2008-01-15 Last updated: 2011-01-11Bibliographically approved

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