{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,2]],"date-time":"2026-06-02T07:00:45Z","timestamp":1780383645502,"version":"3.54.1"},"reference-count":24,"publisher":"Microbiology Society","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2004,2,1]]},"abstract":"<jats:p>Phospholipids are an important component of bacterial membranes.<jats:italic>Borrelia burgdorferi<\/jats:italic>differs from many other bacteria in that it contains only two major membrane phospholipids: phosphatidylglycerol (PG) and phosphatidylcholine (PC).<jats:italic>B. burgdorferi<\/jats:italic>appears to lack enzymes required for synthesis of PC through the well-described methylation pathway. However,<jats:italic>B. burgdorferi<\/jats:italic>does contain a gene (<jats:italic>BB0249<\/jats:italic>) with significant identity to a recently described phosphatidylcholine synthase gene (<jats:italic>pcs<\/jats:italic>) of<jats:italic>Sinorhizobium meliloti. B. burgdorferi<\/jats:italic>also contains a gene (<jats:italic>BB0721<\/jats:italic>) with significant identity to the gene (<jats:italic>pgs<\/jats:italic>) encoding phosphatidylglycerolphosphate synthase, an enzyme in the synthetic pathway of PG. Activity of BB0249 was confirmed by cloning the gene into<jats:italic>Escherichia coli<\/jats:italic>, which does not produce PC. Transformation with a plasmid carrying<jats:italic>BB0249<\/jats:italic>resulted in production of PC by<jats:italic>E. coli<\/jats:italic>, but only in the presence of exogenously supplied choline, as would be predicted for a Pcs. Because loss of Pgs activity is lethal to<jats:italic>E. coli<\/jats:italic>, activity of<jats:italic>BB0721<\/jats:italic>was confirmed by the ability of BB0721 to complement an<jats:italic>E. coli<\/jats:italic>Pgs<jats:sup>\u2212<\/jats:sup>mutant. A plasmid containing<jats:italic>BB0721<\/jats:italic>was transformed into a Pgs<jats:sup>\u2212<\/jats:sup>mutant of<jats:italic>E. coli<\/jats:italic>containing a copy of the native gene on a temperature-regulated plasmid. The temperature-regulated plasmid was exchanged for a plasmid containing<jats:italic>BB0721<\/jats:italic>and it was shown that BB0721 was able to replace the lost Pgs function and restore bacterial growth. This study has established the existence and function of two critical enzymes in the synthesis of PC and PG in<jats:italic>B. burgdorferi<\/jats:italic>. Understanding of the biosynthetic pathways of PC and PG in<jats:italic>B. burgdorferi<\/jats:italic>is the first step in delineating the role of these phospholipids in the pathogenesis of Lyme disease.<\/jats:p>","DOI":"10.1099\/mic.0.26752-0","type":"journal-article","created":{"date-parts":[[2004,2,6]],"date-time":"2004-02-06T22:06:59Z","timestamp":1076105219000},"page":"391-397","source":"Crossref","is-referenced-by-count":36,"title":["Phospholipid synthesis in Borrelia burgdorferi: BB0249 and BB0721 encode functional phosphatidylcholine synthase and phosphatidylglycerolphosphate synthase proteins"],"prefix":"10.1099","volume":"150","author":[{"given":"Xing-Guo","family":"Wang","sequence":"first","affiliation":[{"name":"Tupper Research Institute, Division of Geographic Medicine and Infectious Diseases, New England Medical Center, Tufts University School of Medicine, Box 41, 750 Washington Street, Boston, MA 02111, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joanna P.","family":"Scagliotti","sequence":"additional","affiliation":[{"name":"Tupper Research Institute, Division of Geographic Medicine and Infectious Diseases, New England Medical Center, Tufts University School of Medicine, Box 41, 750 Washington Street, Boston, MA 02111, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Linden T.","family":"Hu","sequence":"additional","affiliation":[{"name":"Tupper Research Institute, Division of Geographic Medicine and Infectious Diseases, New England Medical Center, Tufts University School of Medicine, Box 41, 750 Washington Street, Boston, MA 02111, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"345","reference":[{"key":"R1","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1128\/JB.95.3.833-843.1968","article-title":"Lipids of Salmonella typhimurium and Escherichia coli : structure and metabolism","volume":"95","author":"Ames","year":"1968","journal-title":"J Bacteriol"},{"key":"R2","doi-asserted-by":"crossref","first-page":"2151","DOI":"10.1128\/JB.176.8.2151-2157.1994","article-title":"Fatty acids of Treponema pallidum and Borrelia burgdorferi lipoproteins","volume":"176","author":"Belisle","year":"1994","journal-title":"J Bacteriol"},{"key":"R3","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1074\/jbc.270.2.732","article-title":"Phosphatidylethanolamine is required for in vivo function of the membrane-associated lactose permease of Escherichia coli","volume":"270","author":"Bogdanov","year":"1995","journal-title":"J Biol Chem"},{"key":"R4","doi-asserted-by":"crossref","first-page":"5255","DOI":"10.1093\/emboj\/17.18.5255","article-title":"Phospholipid-assisted protein folding: phosphatidylethanolamine is required at a late step of the conformational maturation of the polytopic membrane protein lactose permease","volume":"17","author":"Bogdanov","year":"1998","journal-title":"EMBO J"},{"key":"R5","doi-asserted-by":"crossref","first-page":"36827","DOI":"10.1074\/jbc.274.52.36827","article-title":"Lipid-assisted protein folding","volume":"274","author":"Bogdanov","year":"1999","journal-title":"J Biol Chem"},{"key":"R6","doi-asserted-by":"crossref","first-page":"11615","DOI":"10.1074\/jbc.271.20.11615","article-title":"A phospholipid acts as a chaperone in assembly of a membrane transport protein","volume":"271","author":"Bogdanov","year":"1996","journal-title":"J Biol Chem"},{"key":"R7","doi-asserted-by":"crossref","first-page":"12339","DOI":"10.1074\/jbc.274.18.12339","article-title":"Phospholipid-assisted refolding of an integral membrane protein. 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